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Journal articles on the topic 'L-selectin'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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1

Peng, Shuang, Shen-Bao Chen, Lin-Da Li, Chun-Fang Tong, Ning Li, Shou-Qin Lü, and Mian Long. "Impact of real-time shedding on binding kinetics of membrane-remaining L-selectin to PSGL-1." American Journal of Physiology-Cell Physiology 316, no. 5 (May 1, 2019): C678—C689. http://dx.doi.org/10.1152/ajpcell.00212.2018.

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L-selectin shedding induced by various cytokines is crucial in activating neutrophils (PMNs) in inflammatory cascade. While the real-time shedding in vivo lasts ~10 min after PMN activation, the impact of time-dependent shedding on binding kinetics of membrane-remaining L-selectins to its ligands is poorly understood at transient or steady state. Here, we developed an in vitro L-selectin shedding dynamics approach, together with competitive assays of cell adhesion, and proposed a theoretical model for quantifying the impact of real-time shedding on the binding kinetics of membrane-remaining L-selectins to P-selectin glycoprotein ligand-1 (PSGL-1). Our data indicated that the extent of L-selectin shedding on PMA activation is higher, but the terminating time is longer for Jurkat cells than those for human PMNs. Meanwhile, fMLF or IL-8 stimulation yields the longer terminating time than that on PMA stimulation but results in a similar shedding extent for PMNs. L-selectin shedding reduces L-selectin-PSGL-1-mediated cell adhesion in three ways: decreasing membrane-anchored L-selectins, increasing soluble L-selectins competitively binding to ligands, and presenting conformational alteration of membrane-remaining L-selectins themselves. Compared with those on intact cells, the binding affinities of membrane-remaining L-selectin-PSGL-1 pairs were all enhanced at initial and lowered at the late shedding phase for both PMN and Jurkat cells even with varied transition time points. The rolling velocities of both PMNs and Jurkat cells were increased following mechanically or biochemically induced shedding of L-selectin under shear flow. These findings help to further our understanding of the function of time-dependent L-selectin shedding during the inflammation cascade.
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2

Mattila, Polly E., Chad E. Green, Ulrich Schaff, Scott I. Simon, and Bruce Walcheck. "Cytoskeletal interactions regulate inducible L-selectin clustering." American Journal of Physiology-Cell Physiology 289, no. 2 (August 2005): C323—C332. http://dx.doi.org/10.1152/ajpcell.00603.2004.

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L-selectin (CD62L) amplifies neutrophil capture within the microvasculature at sites of inflammation. Activation by G protein-coupled stimuli or through ligation of L-selectin promotes clustering of L-selectin and serves to increase its adhesiveness, signaling, and colocalization with β2-integrins. Currently, little is known about the molecular process regulating the lateral mobility of L-selectin. On neutrophil stimulation, a progressive change takes place in the organization of its plasma membrane, resulting in membrane domains that are characteristically enriched in glycosyl phosphatidylinositol (GPI)-anchored proteins and exclude the transmembrane protein CD45. Clustering of L-selectin, facilitated by E-selectin engagement or antibody cross-linking, resulted in its colocalization with GPI-anchored CD55, but not with CD45 or CD11c. Disrupting microfilaments in neutrophils or removing a conserved cationic motif in the cytoplasmic domain of L-selectin increased its mobility and membrane domain localization in the plasma membrane. In addition, the conserved element was critical for L-selectin-dependent tethering under shear flow. Our data indicate that L-selectin’s lateral mobility is regulated by interactions with the actin cytoskeleton that in turn fortifies leukocyte tethering. We hypothesize that both membrane mobility and stabilization augment L-selectin’s effector functions and are regulated by dynamic associations with membrane domains and the actin cytoskeleton.
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3

Miles, Mary P., Sharyn K. Leach, William J. Kraemer, Keiichiro Dohi, Jill A. Bush, and Andrea M. Mastro. "Leukocyte adhesion molecule expression during intense resistance exercise." Journal of Applied Physiology 84, no. 5 (May 1, 1998): 1604–9. http://dx.doi.org/10.1152/jappl.1998.84.5.1604.

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We hypothesized that expression of L-selectin and very late antigen-4 (VLA-4) integrin adhesion molecules would influence cell type-specific redistribution during exercise. Women subjects performed six sets of 10-repetition maximum squats. L-selectin and VLA-4 integrin were measured by using flow cytometry pre- and postexercise on peripheral blood neutrophils and lymphocytes ( n = 29 subjects) and lymphocyte subsets ( n = 70 subjects), respectively. Neutrophil concentration increased 41.8% ( P < 0.001), whereas the percent expressing L-selectin was unchanged (79%). Lymphocyte concentration increased 61.8% ( P < 0.001). The percent of T cells expressing L-selectin decreased from 73.5 ± 8.9 to 68.2 ± 11.4% ( P < 0.001); the combined population of natural killer and B cells expressing L-selectin decreased from 80.4 ± 22.5 to 62.7 ± 25.8% ( P < 0.001). VLA-4 integrin was expressed by nearly all lymphocytes both pre- and postexercise. The proportional decrease in L-selectin positive cells could have resulted from 1) shedding of L-selectin, 2) selective entry of L-selectin-negative subsets, or 3) selective removal of L-selectin-positive subsets.
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4

Alon, R., R. C. Fuhlbrigge, E. B. Finger, and T. A. Springer. "Interactions through L-selectin between leukocytes and adherent leukocytes nucleate rolling adhesions on selectins and VCAM-1 in shear flow." Journal of Cell Biology 135, no. 3 (November 1, 1996): 849–65. http://dx.doi.org/10.1083/jcb.135.3.849.

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We demonstrate an additional step and a positive feedback loop in leukocyte accumulation on inflamed endothelium. Leukocytes in shear flow bind to adherent leukocytes through L-selectin/ligand interactions and subsequently bind downstream and roll on inflamed endothelium, purified E-selectin, P-selectin, L-selectin, VCAM-1, or peripheral node addressin. Thus adherent leukocytes nucleate formation of strings of rolling cells and synergistically enhance leukocyte accumulation. Neutrophils, monocytes, and activated T cell lines, but not peripheral blood T lymphocytes, tether to each other through L-selectin. L-selectin is not involved in direct binding to either E- or P-selectin and is not a major counterreceptor of endothelial selectins. Leukocyte-leukocyte tethers are more tolerant to high shear than direct tethers to endothelial selectins and, like other L-selectin-mediated interactions, require a shear threshold. Synergism between leukocyte-leukocyte and leukocyte-endothelial interactions introduces novel regulatory mechanisms in recruitment of leukocytes in inflammation.
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5

Nelson, RM, O. Cecconi, WG Roberts, A. Aruffo, RJ Linhardt, and MP Bevilacqua. "Heparin oligosaccharides bind L- and P-selectin and inhibit acute inflammation." Blood 82, no. 11 (December 1, 1993): 3253–58. http://dx.doi.org/10.1182/blood.v82.11.3253.3253.

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Abstract Initial attachment of leukocytes to the vessel wall at sites of inflammation is supported by a family of carbohydrate-binding adhesion molecules called the selectins. Selectin ligands include sialyl-Lewis x (sLex, Neu5Ac alpha 2–3Gal beta 1–4[Fuc alpha 1–3]GlcNAc--) and related structures. We report here that defined heparin oligosaccharides interact with the selectins. Heparin chains containing four or more monosaccharide residues inhibited the function of L- and P-selectin, but not E-selectin, in vitro. In a competition enzyme-linked immunosorbent assay measuring inhibition of solution-phase selectin-Ig fusion proteins (selectin-Ig) binding to immobilized bovine serum albumin-sLex neoglycoprotein, a heparin-derived tetrasaccharide mixture inhibited 50% of L- and P-selectin-Ig binding (IC50) at 200 +/- 40 mumol/L and 850 +/- 110 mumol/L, respectively. A single hexasulfated tetrasaccharide (delta UA2S alpha 1–4GlcNS6S alpha 1–4IdoA2S alpha 1- 4GlcNS6S) was particularly active against L- and P-selectin-Ig (IC50 = 46 +/- 5 mumol/L and 341 +/- 24 mumol/L). By comparison, the tetrasaccharide sLex was not inhibitory at concentrations up to 1 mmol/L. In cell adhesion assays, heparin tetrasaccharides reduced binding of neutrophils to COS cells expressing P-selectin but not to COS cells expressing E-selectin. They also blocked colon cancer cell adhesion to L- and P-selectin but not E-selectin. In a model of acute inflammation, intravenously administered heparin tetrasaccharides diminished influx of neutrophils into the peritoneal cavities of thioglycollate-treated mice. We conclude that heparin oligosaccharides, including non-anticoagulant tetrasaccharides, are effective L- and P- selectin inhibitors in vitro and have anti-inflammatory activity in vivo.
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6

Nelson, RM, O. Cecconi, WG Roberts, A. Aruffo, RJ Linhardt, and MP Bevilacqua. "Heparin oligosaccharides bind L- and P-selectin and inhibit acute inflammation." Blood 82, no. 11 (December 1, 1993): 3253–58. http://dx.doi.org/10.1182/blood.v82.11.3253.bloodjournal82113253.

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Initial attachment of leukocytes to the vessel wall at sites of inflammation is supported by a family of carbohydrate-binding adhesion molecules called the selectins. Selectin ligands include sialyl-Lewis x (sLex, Neu5Ac alpha 2–3Gal beta 1–4[Fuc alpha 1–3]GlcNAc--) and related structures. We report here that defined heparin oligosaccharides interact with the selectins. Heparin chains containing four or more monosaccharide residues inhibited the function of L- and P-selectin, but not E-selectin, in vitro. In a competition enzyme-linked immunosorbent assay measuring inhibition of solution-phase selectin-Ig fusion proteins (selectin-Ig) binding to immobilized bovine serum albumin-sLex neoglycoprotein, a heparin-derived tetrasaccharide mixture inhibited 50% of L- and P-selectin-Ig binding (IC50) at 200 +/- 40 mumol/L and 850 +/- 110 mumol/L, respectively. A single hexasulfated tetrasaccharide (delta UA2S alpha 1–4GlcNS6S alpha 1–4IdoA2S alpha 1- 4GlcNS6S) was particularly active against L- and P-selectin-Ig (IC50 = 46 +/- 5 mumol/L and 341 +/- 24 mumol/L). By comparison, the tetrasaccharide sLex was not inhibitory at concentrations up to 1 mmol/L. In cell adhesion assays, heparin tetrasaccharides reduced binding of neutrophils to COS cells expressing P-selectin but not to COS cells expressing E-selectin. They also blocked colon cancer cell adhesion to L- and P-selectin but not E-selectin. In a model of acute inflammation, intravenously administered heparin tetrasaccharides diminished influx of neutrophils into the peritoneal cavities of thioglycollate-treated mice. We conclude that heparin oligosaccharides, including non-anticoagulant tetrasaccharides, are effective L- and P- selectin inhibitors in vitro and have anti-inflammatory activity in vivo.
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7

Matala, Erik, Shelia R. Alexander, Takashi K. Kishimoto, and Bruce Walcheck. "The Cytoplasmic Domain of L-Selectin Participates in Regulating L-Selectin Endoproteolysis." Journal of Immunology 167, no. 3 (August 1, 2001): 1617–23. http://dx.doi.org/10.4049/jimmunol.167.3.1617.

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8

Jutila, M. A., G. Watts, B. Walcheck, and G. S. Kansas. "Characterization of a functionally important and evolutionarily well-conserved epitope mapped to the short consensus repeats of E-selectin and L-selectin." Journal of Experimental Medicine 175, no. 6 (June 1, 1992): 1565–73. http://dx.doi.org/10.1084/jem.175.6.1565.

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Selectins represent a new family of adhesion molecules, expressed by leukocytes and endothelial cells, that are involved in the regulation of leukocyte traffic. Here we have characterized a new monoclonal antibody (mAb) (EL-246) that recognizes both human leukocyte L-selectin (previously called LAM-1, LECAM-1, or gp90MEL-14) and endothelial cell E-selectin (previously called ELAM-1). EL-246 recognized a 110-kD protein expressed on cells transfected with E-selectin cDNA and stained many postcapillary venules in inflamed human tonsil. EL-246 also stained human peripheral blood leukocytes and showed identity with anti-L-selectin mAb in two-color flow cytometric analysis. The expression of the leukocyte EL-246 antigen was regulated in the same manner as L-selectin and EL-246 recognized anti-L-selectin mAb affinity-purified antigen in SDS/PAGE Western blot analysis. Further, L-selectin cDNA transfectants were specifically stained by EL-246. EL-246 blocked greater than 95% of lymphocyte adhesion to peripheral lymph node high endothelial venules and greater than 90% of neutrophil adhesion to E-selectin transfectants. In addition to the EL-246 epitope being expressed on two different human selectins, it was detected on L-selectin from a variety of different animals. Interestingly, domain mapping studies localized the EL-246 epitope to the short consensus repeat (SCR) domains of L-selectin. EL-246 is the first mAb that recognizes two different selectins and potentially defines a functional epitope encoded by the SCR domains. Inhibitors of selectin function targeted to this region would be expected to have the added advantage of simultaneously blocking the activity of two distinct adhesion proteins involved in inflammation.
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9

Alon, Ronen, Shuqi Chen, Kamal D. Puri, Erik B. Finger, and Timothy A. Springer. "The Kinetics of L-selectin Tethers and the Mechanics of Selectin-mediated Rolling." Journal of Cell Biology 138, no. 5 (September 8, 1997): 1169–80. http://dx.doi.org/10.1083/jcb.138.5.1169.

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Two mechanisms have been proposed for regulating rolling velocities on selectins. These are (a) the intrinsic kinetics of bond dissociation, and (b) the reactive compliance, i.e., the susceptibility of the bond dissociation reaction to applied force. To determine which of these mechanisms explains the 7.5–11.5-fold faster rolling of leukocytes on L-selectin than on E- and P-selectins, we have compared the three selectins by examining the dissociation of transient tethers. We find that the intrinsic kinetics for tether bond dissociation are 7–10-fold more rapid for L-selectin than for E- and P-selectins, and are proportional to the rolling velocities through these selectins. The durations of pauses during rolling correspond to the duration of transient tethers on low density substrates. Moreover, applied force increases dissociation kinetics less for L-selectin than for E- and P-selectins, demonstrating that reactive compliance is not responsible for the faster rolling through L-selectin. Further measurements provide a biochemical and biophysical framework for understanding the molecular basis of rolling. Displacements of tethered cells during flow reversal, and measurements of the distance between successive pauses during rolling provide estimates of the length of a tether and the length of the adhesive contact zone, and suggest that rolling occurs with as few as two tethers per contact zone. Tether bond lifetime is an exponential function of the force on the bond, and the upper limit for the tether bond spring constant is of the same order of magnitude as the estimated elastic spring constant of the lectin–EGF unit. Shear uniquely enhances the rate of L-selectin transient tether formation, and conversion of tethers to rolling adhesions, providing further understanding of the shear threshold requirement for rolling through L-selectin.
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10

Dwir, Oren, Geoffrey S. Kansas, and Ronen Alon. "Cytoplasmic anchorage of L-selectin controls leukocyte capture and rolling by increasing the mechanical stability of the selectin tether." Journal of Cell Biology 155, no. 1 (October 1, 2001): 145–56. http://dx.doi.org/10.1083/jcb.200103042.

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L-selectin is a leukocyte lectin that mediates leukocyte capture and rolling in the vasculature. The cytoplasmic domain of L-selectin has been shown to regulate leukocyte rolling. In this study, the regulatory mechanisms by which this domain controls L-selectin adhesiveness were investigated. We report that an L-selectin mutant generated by truncation of the COOH-terminal 11 residues of L-selectin tail, which impairs association with the cytoskeletal protein α-actinin, could capture leukocytes to glycoprotein L-selectin ligands under physiological shear flow. However, the conversion of initial tethers into rolling was impaired by this partial tail truncation, and was completely abolished by a further four-residue truncation of the L-selectin tail. Physical anchorage of both cell-free tail-truncated mutants within a substrate fully rescued their adhesive deficiencies. Microkinetic analysis of full-length and truncated L-selectin–mediated rolling at millisecond temporal resolution suggests that the lifetime of unstressed L-selectin tethers is unaffected by cytoplasmic tail truncation. However, cytoskeletal anchorage of L-selectin stabilizes the selectin tether by reducing the sensitivity of its dissociation rate to increasing shear forces. Low force sensitivity (reactive compliance) of tether lifetime is crucial for selectins to mediate leukocyte rolling under physiological shear stresses. This is the first demonstration that reduced reactive compliance of L-selectin tethers is regulated by cytoskeletal anchorage, in addition to intrinsic mechanical properties of the selectin–carbohydrate bond.
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11

MALHOTRA, Rajneesh, Neil R. TAYLOR, and Michael I. BIRD. "Anionic phospholipids bind to L-selectin (but not E-selectin) at a site distinct from the carbohydrate-binding site." Biochemical Journal 314, no. 1 (February 15, 1996): 297–303. http://dx.doi.org/10.1042/bj3140297.

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It is known that L-selectin binds to glycoconjugates containing the tetrasaccharide sialyl Lewis X in a Ca2+-dependent manner. In addition, a number of other acidic oligosaccharides (for example heparin or chondroitin sulphate) or glycolipids (for example sulphatides) bind to L-selectin independent of cations. In this paper we have established that L-selectin binds to charged phospholipids, such as cardiolipin and phosphatidylserine, but not to neutral phospholipids such as phosphatidylcholine. No interaction between E-selectin and any phospholipid was observed. The interaction between L-selectin and cardiolipin was inhibited by dextran sulphate, fucoidan, mannose 6-phosphate and monoclonal antibodies previously reported to block the interaction between L-selectin and its natural ligands. Analysis of the amino acid sequence of the selectins indicated that L-selectin, but not E-selectin, contains a sequence homologous to the putative cardiolipin-binding epitope found in plasma glycoprotein β2I. Glycoprotein β2I and a peptide corresponding to the putative cardiolipin-binding epitope in β2I inhibited the binding of L-selectin to cardiolipin or fucoidin. Based on the binding characteristics, sequence analysis and structural modelling of L-selectin, we suggest that the amino acid sequence KKNKED (residues 84–89) is a novel site for the binding of acidic species to L-selectin. This motif is localized close to the putative carbohydrate-binding domain of L-selectin and may be a second site within the lectin domain for the interaction of leucocyte L-selectin with its natural endothelial ligands.
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12

Mowery, Patricia, Zhi-Qiang Yang, Eva J. Gordon, Oren Dwir, Andrew G. Spencer, Ronen Alon, and Laura L. Kiessling. "Synthetic Glycoprotein Mimics Inhibit L-Selectin-Mediated Rolling and Promote L-Selectin Shedding." Chemistry & Biology 11, no. 5 (May 2004): 725–32. http://dx.doi.org/10.1016/j.chembiol.2004.03.027.

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13

Foxall, C., SR Watson, D. Dowbenko, C. Fennie, LA Lasky, M. Kiso, A. Hasegawa, D. Asa, and BK Brandley. "The three members of the selectin receptor family recognize a common carbohydrate epitope, the sialyl Lewis(x) oligosaccharide." Journal of Cell Biology 117, no. 4 (May 15, 1992): 895–902. http://dx.doi.org/10.1083/jcb.117.4.895.

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The selectins (lectin-EGF-complement binding-cell adhesion molecules [LEC-CAMs]) are a family of mammalian receptors implicated in the initial interactions between leukocytes and vascular endothelia, leading to lymphocyte homing, platelet binding, and neutrophil extravasation. The three known selectins, L-selectin (leukocyte adhesion molecule-1 [LECAM-1]), E-selectin (endothelial-leukocyte adhesion molecule-1 [ELAM-1]), and P-selectin (GMP-140) share structural features that include a calcium-dependent lectin domain. The sialyl Lewis(x) carbohydrate epitope has been reported as a ligand for both E- and P-selectins. Although L-selectin has been demonstrated to bind to carbohydrates, structural features of potential mammalian carbohydrate ligand(s) have not been well defined. Using an ELISA developed with a sialyl Lewis(x)-containing glycolipid and an E-selectin-IgG chimera, we have demonstrated the direct binding of the L-selectin-IgG chimera to sialyl Lewis(x). This recognition was calcium dependent, and could be blocked by Mel-14 antibody but not by other antibodies. Recognition was confirmed by the ability of cells expressing the native L-selectin to adhere to immobilized sialyl Lewis(x). These data suggest that the sialyl Lewis(x) oligosaccharide may form the basis of a recognition domain common to all three selectins.
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14

Li, Ying, Jennifer Brazzell, Amy Herrera, and Bruce Walcheck. "ADAM17 deficiency by mature neutrophils has differential effects on L-selectin shedding." Blood 108, no. 7 (October 1, 2006): 2275–79. http://dx.doi.org/10.1182/blood-2006-02-005827.

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Abstract L-selectin directs neutrophils to sites of inflammation, and upon their activation, surface expression of the receptor is rapidly down-regulated by ectodomain shedding. Tumor necrosis factor–α–converting enzyme (TACE, or ADAM17) is a sheddase of L-selectin; however, Adam17 gene targeting (ADAM17ΔZn/ΔZn) in mice is perinatal lethal and its role in L-selectin shedding by mature neutrophils has not been determined. This was addressed here by using radiation-chimeric mice reconstituted with ADAM17ΔZn/ΔZn fetal liver cells. ADAM17-deficient neutrophils, monocytes, and lymphocytes failed to shed L-selectin in response to PMA, as did neutrophils infiltrating the inflamed peritoneum. In addition, the absence of functional ADAM17 resulted in significantly increased levels of L-selectin surface expression by peripheral-blood leukocytes, indicating the sheddase also plays a role in the constitutive cleavage of L-selectin. Interestingly, not all manners of L-selectin turnover required ADAM17. Plasma L-selectin levels were similar between ADAM17ΔZn/ΔZn-chimeric and control mice, as was the shedding of L-selectin by neutrophils undergoing spontaneous apoptosis. The latter process, however, was diminished by a metalloprotease inhibitor, indicating the role of a sheddase other than ADAM17. Together, our data reveal that L-selectin's surface density on neutrophils is regulated by ADAM17, but homeostatic L-selectin cleavage is not.
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15

Haznedaroğlu, I. C., M. Benekli, M. C. Savaş, I. H. Güllū, S. V. Dündar, and Ş. Kirazli. "Serum L-Selectin and P-Selectin levels in lymphomas." European Journal of Cancer 33 (September 1997): S268. http://dx.doi.org/10.1016/s0959-8049(97)86122-9.

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16

Haznedaroğlu, I. C., I. H. Güllü, M. C. Savaş, Ş. Kirazli, S. V. Dündar, O. Ozcebe, and M. Benekli. "Serum L-selectin and P-selectin levels in lymphomas." Haematologia 30, no. 1 (March 1, 2000): 27–30. http://dx.doi.org/10.1163/15685590051129841.

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17

Bélanger, Simon D., and Yves St-Pierre. "Role of selectins in the triggering, growth, and dissemination of T-lymphoma cells: implication of L-selectin in the growth of thymic lymphoma." Blood 105, no. 12 (June 15, 2005): 4800–4806. http://dx.doi.org/10.1182/blood-2004-04-1406.

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Abstract We previously showed that intercellular adhesion molecule-1 (ICAM-1) expression by the host is essential for lymphoma dissemination. Because selectins usually act in a coordinated fashion with ICAM-1 in the recruitment of circulating normal cells, we investigated their implication in lymphomagenesis and metastasis. Using selectin-deficient mice, we found that though the absence of E-, P-, or L-selectins did not affect the triggering of radiation-induced thymic lymphoma, the absence of L-selectin on lymphoma cells reduced their capacity to grow in the thymus. This defect, however, was overcome by altering the integrity of the L-selectin-mediated interactions in the thymus, as shown in L-selectin-deficient mice and by adoptive transfer experiments. We also found that lack of selectin expression by the host significantly delayed the dissemination of lymphomas to peripheral tissues. This resistance of selectin-deficient mice to lymphoma metastasis was dependent on the intrinsic properties of lymphoma cells because highly tumorigenic variants were insensitive to the absence of selectins. Observations that lymphoma cells disseminate with the same efficiency in normal and selectin-deficient mice suggest that selectins exert their influence at the posthoming stage of metastasis, as does ICAM-1. These results provide definitive evidence that selectins play a significant role at different steps of T-cell lymphoma development. (Blood. 2005;105:4800-4806)
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18

Xu, J., I. S. Grewal, G. P. Geba, and R. A. Flavell. "Impaired primary T cell responses in L-selectin-deficient mice." Journal of Experimental Medicine 183, no. 2 (February 1, 1996): 589–98. http://dx.doi.org/10.1084/jem.183.2.589.

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L-selectin is a homing receptor that mediates the selective attachment of leukocytes to specialized high endothelial venules. To study the potential role of L-selectin in immune responses in intact mice, we generated L-selectin-deficient mice by gene targeting. L-selectin-deficient mice are defective in cutaneous delayed-type hypersensitivity (DTH) responses when tested after conventional intervals of immunization (4 d). Primary T cell proliferative responses and cytokine production (interleukin [IL] 2, IL-4, and interferon gamma) were also compromised when tested after 5 d of immunization, indicating that L-selectin is important for the immune response to antigens. In contrast, after more prolonged immunization protocols (9 d), normal responses were observed, suggesting that L-selectin-independent compensatory mechanisms exist. Interestingly, humoral responses of L-selectin-deficient mice to keyhole limpet hemocyanin are indistinguishable from wild-type control mice, implying that L-selectin plays no rate-limiting role in T cell help of B cell function. Thus, our results suggest that L-selectin plays an important role in the generation of primary T cell responses but may not be essential for humoral and memory T cell responses. L-selectin does not appear to be rate limiting for the events leading to antigen-driven neutrophil recruitment, since normal DTH responses are obtained at late time points after immunization.
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19

Spertini, O., A. S. Cordey, N. Monai, L. Giuffrè, and M. Schapira. "P-selectin glycoprotein ligand 1 is a ligand for L-selectin on neutrophils, monocytes, and CD34+ hematopoietic progenitor cells." Journal of Cell Biology 135, no. 2 (October 15, 1996): 523–31. http://dx.doi.org/10.1083/jcb.135.2.523.

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Selectins play a critical role in initiating leukocyte binding to vascular endothelium. In addition, in vitro experiments have shown that neutrophils use L-selectin to roll on adherent neutrophils, suggesting that they express a nonvascular L-selectin ligand. Using a L-selectin/IgM heavy chain (mu) chimeric protein as an immunocytological probe, we show here that L-selectin can bind to neutrophils, monocytes, CD34+ hematopoietic progenitors, and HL-60 and KG-1 myeloid cells. The interaction between L-selectin and leukocytes was protease sensitive and calcium dependent, and abolished by cell treatment with neuraminidase, chlorate, or O-sialoglycoprotein endopeptidase. These results revealed common features between leukocyte L-selectin ligand and the mucin-like P-selectin glycoprotein ligand 1 (PSGL-1), which mediates neutrophil rolling on P- and E-selectin. The possibility that PSGL-1 could be a ligand for L-selectin was further supported by the ability of P-selectin/mu chimera to inhibit L-selectin/mu binding to leukocytes and by the complete inhibition of both selectin interactions with myeloid cells treated with mocarhagin, a cobra venom metalloproteinase that cleaves the amino terminus of PSGL-1 at Tyr-51. Finally, the abrogation of L- and P-selectin binding to myeloid cells treated with a polyclonal antibody, raised against a peptide corresponding to the amino acid residues 42-56 of PSGL-1, indicated that L- and P-selectin interact with a domain located at the amino-terminal end of PSGL-1. The ability of the anti-PSGL-1 mAb PL-1 to inhibit L- and P-selectin binding to KG-1 cells further supported that possibility. Thus, apart from being involved in neutrophil rolling on P- and E-selectin, PSGL-1 also plays a critical role in mediating neutrophil attachment to adherent neutrophils. Interaction between L-selectin and PSGL-1 may be of major importance for increasing leukocyte recruitment at inflammatory sites.
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20

Shigeta, Akiko, Masanori Matsumoto, Thomas F. Tedder, John B. Lowe, Masayuki Miyasaka, and Takako Hirata. "An L-selectin ligand distinct from P-selectin glycoprotein ligand-1 is expressed on endothelial cells and promotes neutrophil rolling in inflammation." Blood 112, no. 13 (December 15, 2008): 4915–23. http://dx.doi.org/10.1182/blood-2008-04-153866.

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Abstract Neutrophils recruited from the blood are key players in the innate immune response. Selectins play critical roles in neutrophil recruitment by mediating their tethering and rolling in inflamed venules. While the roles of P- and E-selectin in this process are well established, the mechanisms of L-selectin–mediated neutrophil recruitment remain elusive. One proposal is that tethering is mediated by L-selectin on flowing neutrophils interacting with P-selectin glycoprotein ligand-1 (PSGL-1) on adherent neutrophils. To clarify whether L-selectin–mediated neutrophil recruitment depends entirely on PSGL-1, we examined the impact of L-selectin deficiency in mice with a PSGL-1–deficient background. L-selectin and PSGL-1 double-knockout mice exhibited a higher increase in their peripheral blood neutrophil count and a worse defect in neutrophil recruitment into the inflamed peritoneum than PSGL-1–deficient mice. Intravital microscopy of inflamed cremaster muscle venules showed that L-selectindeficiency or antibody blockade of L-selectin reduced the residual leukocyte rolling in PSGL-1–deficient mice. Flow cytometric analyses showed that the endothelial cells from the cremaster muscle bound L-selectin in a PSGL-1–independent manner. These results provide evidence for the existence of an L-selectin ligand distinct from PSGL-1 in inflammation and indicate that such a ligand is expressed on endothelial cells, promoting neutrophil rolling in vivo.
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Corsi, M. M., D. Pagani, G. Dogliotti, F. Perona, G. Sambataro, and L. Pignataro. "Protein Biochip Array of Adhesion Molecule Expression in Peripheral Blood of Patients with Nasal Polyposis." International Journal of Biological Markers 23, no. 2 (April 2008): 115–20. http://dx.doi.org/10.1177/172460080802300208.

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Nasal polyposis is a chronic non-infectious inflammatory disease of the nasal and paranasal cavity mucosa of unknown multifactorial origin in which inflammatory cells, and in particular eosinophils, seem to play a pivotal role. Eosinophil migration from the bloodstream to nasal polyps is considered to be specific and is a complex process involving several different molecules such as ICAM-1, VCAM-1, and L-, P- and E-selectins. The aim of this study was to investigate, using a protein biochip array technology, the concentrations of these molecules in the peripheral blood of a group of patients affected by nasal polyposis. Patients exhibited a significantly higher expression of VCAM-1, E-selectin, and L-selectin compared to healthy controls, and Spearman's rank correlation test limited to the molecules with significant between-group differences demonstrated a significant correlation between VCAM-1 and E-selectin, VCAM-1 and L-selectin, and E-selectin and L-selectin. The results of this investigation are in line with those coming from various imunohistochemical analyses, and seem to confirm the role of inflammation in the pathogenesis of nasal polyposis. These molecules may also represent novel therapeutic targets in the treatment of nasal polyps, and may allow the selection of pharmacological prophylactics that would allow effective inhibition of the inflammation induced by a given allergen.
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22

von Andrian, UH, JD Chambers, EL Berg, SA Michie, DA Brown, D. Karolak, L. Ramezani, EM Berger, KE Arfors, and EC Butcher. "L-selectin mediates neutrophil rolling in inflamed venules through sialyl LewisX-dependent and -independent recognition pathways." Blood 82, no. 1 (July 1, 1993): 182–91. http://dx.doi.org/10.1182/blood.v82.1.182.bloodjournal821182.

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The glycoprotein (GP) L-selectin initiates adhesive interactions between leukocytes and endothelial cells (EC). It functions as a lymphocyte-lectin homing receptor recognizing carbohydrate determinants of the peripheral lymph node addressing on high endothelial venules. It also mediates neutrophil rolling, the earliest interaction of neutrophils with acutely inflamed venules. Neutrophil L-selectin presents sialyl-LewisX (sLe(X)) as a ligand to P- and E-selectin in vitro, and we have proposed that this is a major mechanism of L- selectin-mediated rolling in vivo. In contrast, the contribution of neutrophil L-selectin as a receptor protein recognizing one (or more) ligand(s) on inflamed EC is unclear. To address this question, an sLe(X)-negative murine pre-B cell line, L1–2, that can neither bind vascular selectins nor roll in inflamed rabbit venules, was transfected with human L-selectin cDNA. L-selectin expression in stable transfectants was sufficient to confer significant rolling in vivo. Rolling was unaffected by neuraminidase treatment but completely blocked by anti-L-selectin monoclonal antibody (MoAb) DREG-56. Thus, L- selectin can initiate leukocyte interactions with EC determinants potentially through recognition of endothelial carbohydrates. In contrast, when human neutrophils were tested, rolling was reduced, but not abolished, by MoAb DREG-56. Likewise, treatment with neuraminidase or anti-sLe(X) MoAbs decreased, but did not abrogate, neutrophil rolling, consistent with residual EC recognition via L-selectin. Combination of MoAb DREG-56 and neuraminidase resulted in almost complete loss of rolling, as did removal of glycosylated L-selectin by chymotrypsin. Together with the demonstrable rolling of L-selectin transfectants, our results support the concept of a bidirectional interaction between L-selectin bearing sLe(X) on neutrophils and activated EC in vivo. These findings also suggest that L-selectin may mediate rolling of lymphocytes that lack carbohydrate ligands for E- or P-selectin, although probably less efficiently than through bidirectional recognition.
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Thomas, Susan N., Ronald L. Schnaar, and Konstantinos Konstantopoulos. "Podocalyxin-like protein is an E-/L-selectin ligand on colon carcinoma cells: comparative biochemical properties of selectin ligands in host and tumor cells." American Journal of Physiology-Cell Physiology 296, no. 3 (March 2009): C505—C513. http://dx.doi.org/10.1152/ajpcell.00472.2008.

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Selectins facilitate metastasis and tumor cell arrest in the microvasculature by mediating binding of selectin-expressing host cells to ligands on tumor cells. We recently identified CD44 variant isoforms as functional P-, but not E-/L-, selectin ligands on colon carcinoma cells. Furthermore, a ∼180-kDa sialofucosylated glycoprotein(s) mediated selectin binding in CD44-knockdown cells. Using immunoaffinity chromatography and tandem mass spectrometry, we identify podocalyxin-like protein (PCLP) as an alternative selectin ligand. Blot rolling and cell-free flow-based adhesion assays disclose that PCLP on LS174T colon carcinoma cells possesses E-/L-, but not P-, selectin binding activity. The selectin-binding determinants on LS174T PCLP are non-MECA-79-reactive sialofucosylated structures displayed on O-linked glycans, distinct from the MECA-79-reactive O-glycans on PCLP expressed by high endothelial venules, which is an L-selectin ligand. PCLP on CD44-knockdown LS174T cells exhibits higher HECA-452 immunoreactivity than PCLP on wild-type cells, suggesting that PCLP functions as an alternative acceptor for selectin-binding glycans. The enhanced expression of HECA-452 reactivity on PCLP from CD44-knockdown cells correlates with the increased avidity of PCLP for E- but not L-selectin. The novel finding that PCLP is an E-/L-selectin ligand on carcinoma cells offers a unifying perspective on the apparent enhanced metastatic potential associated with tumor cell PCLP overexpression and the role of selectins in metastasis.
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24

Abbal, Claire, Martine Lambelet, Debora Bertaggia, Carole Gerbex, Manuel Martinez, Alexandre Arcaro, Marc Schapira, and Olivier Spertini. "Lipid raft adhesion receptors and Syk regulate selectin-dependent rolling under flow conditions." Blood 108, no. 10 (November 15, 2006): 3352–59. http://dx.doi.org/10.1182/blood-2006-04-013912.

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Abstract Selectins and their ligand P-selectin glycoprotein ligand-1 (PSGL-1) mediate leukocyte rolling along inflamed vessels. Cell rolling is modulated by selectin interactions with their ligands and by topographic requirements including L-selectin and PSGL-1 clustering on tips of leukocyte microvilli. Lipid rafts are cell membrane microdomains reported to function as signaling platforms. Here, we show that disruption of leukocyte lipid rafts with cholesterol chelating agents depleted raft-associated PSGL-1 and L-selectin and strongly reduced L-, P-, and E-selectin–dependent rolling. Cholesterol repletion reversed inhibition of cell rolling. Importantly, leukocyte rolling on P-selectin induced the recruitment of spleen tyrosine kinase (Syk), a tyrosine kinase associated to lipid raft PSGL-1. Furthermore, inhibition of Syk activity or expression, with pharmacologic inhibitors or by RNA interference, strongly reduced leukocyte rolling on P-selectin, but not on E-selectin or PSGL-1. These observations identify novel regulatory mechanisms of leukocyte rolling on selectins with a strong dependency on lipid raft integrity and Syk activity.
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25

Rosen, Steven D. "Homing in on L-Selectin." Journal of Immunology 177, no. 1 (June 19, 2006): 3–4. http://dx.doi.org/10.4049/jimmunol.177.1.3.

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26

Rosen, Steven D. "Endothelial Ligands for L-Selectin." American Journal of Pathology 155, no. 4 (October 1999): 1013–20. http://dx.doi.org/10.1016/s0002-9440(10)65201-7.

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27

Stamenkovic, Ivan. "The L-selectin adhesion system." Current Opinion in Hematology 2, no. 1 (1995): 68–75. http://dx.doi.org/10.1097/00062752-199502010-00010.

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28

Waddell, Thomas K., Lea Fialkow, Chi Kin Chan, Takashi Kei Kishimoto, and Gregory P. Downey. "Signaling Functions of L-selectin." Journal of Biological Chemistry 270, no. 25 (June 23, 1995): 15403–11. http://dx.doi.org/10.1074/jbc.270.25.15403.

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29

Martinez, Manuel, Magali Joffraud, Sylvain Giraud, Bénédicte Baïsse, Michael Pierre Bernimoulin, Marc Schapira, and Olivier Spertini. "Regulation of PSGL-1 Interactions with L-selectin, P-selectin, and E-selectin." Journal of Biological Chemistry 280, no. 7 (December 3, 2004): 5378–90. http://dx.doi.org/10.1074/jbc.m410899200.

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30

MALHOTRA, Rajneesh, Malcolm WARD, Robert B. SIM, and Michael I. BIRD. "Identification of human complement Factor H as a ligand for L-selectin." Biochemical Journal 341, no. 1 (June 24, 1999): 61–69. http://dx.doi.org/10.1042/bj3410061.

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The selectin family of adhesion molecules (E-, P- and L-selectins) is involved in leukocyte recruitment to sites of inflammation and tissue damage. Recently it has been shown that L-selectin is involved not only in leukocyte tethering and rolling, but also plays an important role in leukocyte activation. For example, glycosylation-dependent cell-adhesion molecule 1 (GlyCAM-1), a known ligand for L-selectin, has been shown to enhance β2-integrin function. GlyCAM-1 is a secreted protein and is present in mouse serum at a concentration of approx. 1.5 μg/ml. There is no obvious GlyCAM-1 homologue in man and, to date, L-selectin ligand(s) from human serum have not been characterized. Therefore we have used L-selectin affinity chromatography, followed by ion-exchange chromatography, to isolate specific ligand(s) for L-selectin. Using this procedure, we have isolated three major glycoproteins of apparent molecular masses 170 kDa, 70 kDa and 50 kDa. The 170 kDa protein band was digested with trypsin and peptides were analysed by delayed extraction matrix-assisted laser desorption ionization MS and protein database searching. The 170 kDa protein was identified as the human complement protein Factor H. Human Factor H, isolated by a different method, was shown to bind specifically to L-selectin in the presence of CaCl2, and binding was inhibited by anti-L-selectin antibodies, fucoidan and lipopolysaccharide. Only a part of the purified Factor H preparation bound to immobilized L-selectin. The interaction of Factor H with leukocyte L-selectin was shown to induce the secretion of tumour necrosis factor-α (TNF-α). Pretreatment of Factor H with sialidase reduced both the binding of L-selectin to Factor H and the Factor H-induced L-selectin-mediated TNF-α secretion by leukocytes. Taken together, these results demonstrate that a post-translationally modified form of human plasma Factor H is a potential physiological ligand for L-selectin.
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31

Berg, Ellen L., John Magnani, R. Aaron Warnock, Martyn K. Robinson, and Eugene C. Butcher. "Comparison of L-selectin and E-selectin ligand specificities: The L-selectin can bind the E-selectin ligands Sialyl Lex and Sialyl Lea." Biochemical and Biophysical Research Communications 184, no. 2 (April 1992): 1048–55. http://dx.doi.org/10.1016/0006-291x(92)90697-j.

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32

Hafezi-Moghadam, Ali, Kennard L. Thomas, Alyson J. Prorock, Yuqing Huo, and Klaus Ley. "L-Selectin Shedding Regulates Leukocyte Recruitment." Journal of Experimental Medicine 193, no. 7 (April 2, 2001): 863–72. http://dx.doi.org/10.1084/jem.193.7.863.

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The physiologic role of L-selectin shedding is unknown. Here, we investigate the effect of L-selectin shedding on firm adhesion and transmigration. In a tumor necrosis factor α–induced model of inflammation, inhibition of L-selectin shedding significantly increased firm adhesion and transmigration by a lymphocyte function–associated antigen (LFA)-1 and intercellular adhesion molecule (ICAM)-1–dependent mechanism. We examined the quality of leukocyte rolling and L-selectin–mediated signaling. Blockade of L-selectin shedding significantly reduced the “jerkiness” of leukocyte rolling, defined as the variability of velocity over time. A low level of jerkiness was also observed in the rolling of microbeads conjugated with L-selectin, a model system lacking the mechanism for L-selectin shedding. Inhibition of L-selectin shedding potentiated activation of LFA-1 and Mac-1 induced by L-selectin cross-linking as shown by activation epitope expression and binding of ICAM-1–conjugated beads. We conclude that inhibition of L-selectin shedding increases leukocyte adhesion and transmigration by (a) increasing leukocyte exposure to the inflamed endothelium by decreasing jerkiness and (b) promoting leukocyte activation by outside-in signaling. These observations help to resolve the apparent discrepancy between the minor contribution of L-selectin to rolling and the significant leukocyte recruitment defect in L-selectin knockout mice.
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33

Zoldhelyi, Pierre, Pamela J. Beck, Robert J. Bjercke, Judy C. Ober, X. Hu, Janice M. McNatt, Salman Akhtar, et al. "Inhibition of coronary thrombosis and local inflammation by a noncarbohydrate selectin inhibitor." American Journal of Physiology-Heart and Circulatory Physiology 279, no. 6 (December 1, 2000): H3065—H3075. http://dx.doi.org/10.1152/ajpheart.2000.279.6.h3065.

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We tested the hypothesis that selectin inhibition with blocking antibodies or a small-molecular-weight inhibitor of L-, P-, and E-selectin, methoxybenzoylpropionic acid (MBPA), prevents thrombus formation in a canine coronary Folts' model. Cyclic flow variations (CFVs) were induced by crush injury and constriction of the left anterior descending coronary artery in dogs. Systemic infusion of antibodies to P- and L-selectin abolished CFVs, respectively, in 50% and 17% of treated dogs [ P = not significant (NS)]. The combination of P- and L-selectin antibodies suppressed CFVs in 60% of treated dogs ( P = NS). In contrast, systemic selectin blockade by intravenous infusion or local adventitial application of MBPA markedly reduced CFVs and, in addition, reduced myocardial myeloperoxidase (MPO) activity. We conclude that inhibition of L-, P-, and E-selectin binding by a small-molecular-weight, noncarbohydrate compound markedly reduces arterial thrombosis, whereas systemic administration of antibodies to L- and P-selectin fail to reproduce this antithrombotic effect. These results underscore the role of selectins in the pathogenesis of arterial thrombosis under high shear stress and suggest that inhibition of P- and L- selectin may not suffice to prevent thrombus formation in this model. The role of E-selectin in thrombus formation in this model awaits further testing.
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34

Furie, Barbara, Bruce Furie, and Jing Yang. "The Biology of P-Selectin Glycoprotein Ligand-1: Its Role as a Selectin Counterreceptor in Leukocyte-Endothelial and Leukocyte-Platelet Interaction." Thrombosis and Haemostasis 81, no. 01 (1999): 1–7. http://dx.doi.org/10.1055/s-0037-1614407.

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SummaryCell-cell interactions mediating leukocyte trafficking, thrombogene-sis and inflammation are crucial for the host defense mechanism. The selectin family of integral membrane proteins includes E-selectin, L-selectin and P-selectin. Selectins mediate tethering and rolling of leukocytes to the vessel wall at the site of inflammation. The counter-receptor for P-selectin and possibly the other selectins is P-selectin glycoprotein ligand-1 (PSGL-1). This review focuses on the properties and biology of PSGL-1.
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35

Armstead, V. E., A. G. Minchenko, R. A. Schuhl, R. Hayward, T. O. Nossuli, and A. M. Lefer. "Regulation of P-selectin expression in human endothelial cells by nitric oxide." American Journal of Physiology-Heart and Circulatory Physiology 273, no. 2 (August 1, 1997): H740—H746. http://dx.doi.org/10.1152/ajpheart.1997.273.2.h740.

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P-selectin translocation to the surface of endothelial cells is increased after exposure to the nitric oxide (NO) synthase inhibitor NG-nitro-L-arginine methyl ester (L-NAME), resulting in increased endothelial adhesiveness. L-NAME (3 mM) was added to human cultured iliac vein endothelial cells for 1, 2, 4, and 6 h, and P-selectin mRNA expression was quantified by a ribonuclease protection assay. In parallel experiments, the NO donor, SPM-5185 (10 microM), was added to human iliac venous endothelial cells, and P-selectin mRNA expression quantified. P-selectin protein synthesis was quantified by Western blot analysis. L-NAME caused increased expression of P-selection RNA at 2-4 h, whereas D-NAME, the stereoisomer lacking NO synthase-inhibitory activity, had no effect. The stimulatory effect of L-NAME was reversed by addition of 3 mM L-arginine. SPM-5185 decreased P-selectin mRNA over the same time period (P < 0.02). The increased P-selectin mRNA expression induced by L-NAME was paralleled by an increase in P-selectin protein synthesis. The effects of SPM-5185 and L-arginine were also paralleled by decreases in P-selectin protein synthesis and in decreased adherence of human neutrophils to human iliac venous endothelial cells. The peak effect of inhibition of NO synthesis or addition of exogenous NO occurred at 2-4 h. These results suggest a regulatory effect of NO on endothelial P-selectin expression that modulates early leukocyte-endothelial cell interactions to preserve vascular homeostasis.
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36

Crockett-Torabi, E., and J. C. Fantone. "L-selectin stimulation of canine neutrophil initiates calcium signal secondary to tyrosine kinase activation." American Journal of Physiology-Heart and Circulatory Physiology 272, no. 3 (March 1, 1997): H1302—H1308. http://dx.doi.org/10.1152/ajpheart.1997.272.3.h1302.

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Neutrophils play an important role in myocardial ischemia-reperfusion injury. Neutrophil adhesion to the vascular endothelium is one of the important early mechanisms that lead to reperfusion injury. The leukocyte adhesion molecule, L-selectin, plays a major role in the initial interaction between neutrophils and endothelial cells. Intervention aimed at blocking selectins or their associated ligands can exert cardioprotective effects. The purpose of this study was to examine the role of L-selectin in the initiation of transmembrane signaling and regulation of canine neutrophil responses. Cross-linking of canine neutrophil L-selectin using anti-L-selectin antibody induced a rapid and transient increase in intracellular Ca2+ levels and superoxide anion generation that were dependent on the extent of L-selectin cross-linking. The responses were significantly inhibited by the protein tyrosine kinase inhibitor, genistein. The results demonstrate that ligation of canine neutrophil L-selectin is coupled to intracellular signal transduction pathways and the generation of second messengers, which may independently play important regulatory roles in modulating neutrophil-endothelial cell interactions.
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37

Darwish, Iman, Yevgeniy Brailovsky, Amir Darki, Debra Hoppensteadt, Brett Slajus, Emily Bontekoe, Frank De Stefano, and Jawed Fareed. "Dysregulation of Hemostatic Biomarkers, Inflammatory Biomarkers, and Alteration of Cellular Indices As Predictors of Adverse Outcomes in Pulmonary Embolism Patients." Blood 134, Supplement_1 (November 13, 2019): 2408. http://dx.doi.org/10.1182/blood-2019-126876.

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Background: Pulmonary Embolism (PE) is a condition that affects a multitude of individuals worldwide. The pathophysiology of PE is multifactorial and complex. Measuring levels of biomarkers in PE patient plasma may be predictive of patient outcomes in terms of survival, and such biomarkers could be correlated to other parameters such as white cell counts and their ratios. Adhesion molecules, such as selectins, have been predicted to play a role in the pathophysiology of PE, however their relationship to other cellular parameters is not fully explored. P-selectin is found on platelets, and is involved in the gathering of platelets in thrombotic states. Meanwhile, E and L-selectin contribute to cellular rolling that occurs in states of inflammation. White blood cell counts are routinely obtained from patient blood analysis. Selectins, including Platelet (P), Endothelial (E), and Leukocyte (L) Selectins may possess relationships to the white cell profiles including neutrophil-lymphocyte ratio (NLR), platelet-lymphocyte ratio (PLR), platelet-neutrophil ratio (PNR), lymphocyte-monocyte ratio (LMR), and monocyte-neutrophil ratio (MNR). Selectins can also be correlated to total platelet and white cell counts. Mortality outcomes in PE patients may be associated with altered levels of hemostatic and inflammatory biomarkers such as selectins. Materials and Methods: Blood samples were acquired from 100 patients diagnosed with acute PE between March 2016 and June 2019 at Loyola University Medical Center in Maywood, IL. Enzyme Linked Immunosorbent Assays (ELISA) were used to quantify levels of P, E, and L selectins in the plasma of PE patients. Other coagulation and inflammatory biomarkers, including Tumor Necrosis Factor Alpha (TNFa), D-dimer, Plasminogen Activating Inhibitor-1 (PAI-1), Matrix Metalloprotease-9 (MMP-9), C-Reactive Protein (CRP), micro particles, and alpha-2-antiplasmin were also quantified. Patient chart review was conducted assessing for levels of platelets, neutrophils, lymphocytes, and monocytes. Appropriate cellular ratios were calculated. Patient outcomes in the form of mortality were noted. Spearman non-parametric analysis and Wilcoxon-Mann-Whitney Tests were conducted using Graphpad PRISM software. Results: All of the biomarkers studied exhibited an increase in PE patient plasma, ranging from 2 fold to 34.6 fold increase, with the exception of alpha-2-antiplasmin, E-selectin, and L-selectin, as shown in Table 1. D-dimer, MMP-9, and CRP show the most pronounced increase in PE patients. No statistically significant correlations were noted between P, E, and L-selectins and NLR, PLR, PNR, LMR, or MNR. P-selectin was positively correlated with platelet count (r=.22, p=.032, 95% CI=0.01293 to 0.4084, n=95). L-selectin was not found to be significantly correlated with white count, but a positive trend was still evident (r=.13, p=.22, CI= -0.08329 to 0.3250, n=95). Within the patient pool, 12% of patients were deceased, while 88% survived. L-selectin and all-cause mortality were significantly correlated at an alpha level of .05 (p=.04). Conclusion: These studies demonstrate the marked dysregulation of hemostatic and inflammatory biomarkers associated with alterations of cellular indices. In particular, P and L selectin demonstrated some relationship to platelets and white count. L-selectin levels are significantly correlated to all-cause mortality. Measuring levels of L-selectin in PE patients may provide insight into mortality outcomes for pulmonary embolism patients. Our results are suggestive of the positive predictive value of L-selectin in PE patients. Profiling of various biomarkers, in particular selectins, may be helpful in the risk stratification of PE patients. Adding such a parameter to patient analysis may provide better prognostic information, which may be helpful in their clinical management. Disclosures No relevant conflicts of interest to declare.
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Lawrence, Michael B., Geoffrey S. Kansas, Eric J. Kunkel, and Klaus Ley. "Threshold Levels of Fluid Shear Promote Leukocyte Adhesion through Selectins (CD62L,P,E)." Journal of Cell Biology 136, no. 3 (February 10, 1997): 717–27. http://dx.doi.org/10.1083/jcb.136.3.717.

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Leukocyte adhesion through L-selectin to peripheral node addressin (PNAd, also known as MECA-79 antigen), an L-selectin ligand expressed on high endothelial venules, has been shown to require a minimum level of fluid shear stress to sustain rolling interactions (Finger, E.B., K.D. Puri, R. Alon, M.B. Lawrence, V.H. von Andrian, and T.A. Springer. 1996. Nature (Lond.). 379:266–269). Here, we show that fluid shear above a threshold of 0.5 dyn/cm2 wall shear stress significantly enhances HL-60 myelocyte rolling on P- and E-selectin at site densities of 200/μm2 and below. In addition, gravitational force is sufficient to detach HL60 cells from P- and E-selectin substrates in the absence, but not in the presence, of flow. It appears that fluid shear–induced torque is critical for the maintenance of leukocyte rolling. K562 cells transfected with P-selectin glycoprotein ligand-1, a ligand for P-selectin, showed a similar reduction in rolling on P-selectin as the wall shear stress was lowered below 0.5 dyn/cm2. Similarly, 300.19 cells transfected with L-selectin failed to roll on PNAd below this level of wall shear stress, indicating that the requirement for minimum levels of shear force is not cell type specific. Rolling of leukocytes mediated by the selectins could be reinitiated within seconds by increasing the level of wall shear stress, suggesting that fluid shear did not modulate receptor avidity. Intravital microscopy of cremaster muscle venules indicated that the leukocyte rolling flux fraction was reduced at blood centerline velocities less than 1 mm/s in a model in which rolling is mediated by L- and P-selectin. Similar observations were made in L-selectin–deficient mice in which leukocyte rolling is entirely P-selectin dependent. Leukocyte adhesion through all three selectins appears to be significantly enhanced by a threshold level of fluid shear stress.
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39

Houshmand, B., A. Rafiei, M. Hajilooi, K. Mani-Kashani, and L. Gholami. "E-selectin and L-selectin polymorphisms in patients with periodontitis." Journal of Periodontal Research 44, no. 1 (February 2009): 88–93. http://dx.doi.org/10.1111/j.1600-0765.2008.01092.x.

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40

Dimitroff, Charles J., Jack Y. Lee, Kenneth S. Schor, Brenda M. Sandmaier, and Robert Sackstein. "Differential L-Selectin Binding Activities of Human Hematopoietic Cell L-Selectin Ligands, HCELL and PSGL-1." Journal of Biological Chemistry 276, no. 50 (October 8, 2001): 47623–31. http://dx.doi.org/10.1074/jbc.m105997200.

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Expression of L-selectin on human hematopoietic cells (HC) is associated with a higher proliferative activity and a more rapid engraftment after hematopoietic stem cell transplantation. Two L-selectin ligands are expressed on human HCs, P-selectin glycoprotein ligand-1 (PSGL-1) and a specialized glycoform of CD44 (hematopoietic cell E- and L-selectin ligand, HCELL). Although the structural biochemistry of HCELL and PSGL-1 is well characterized, the relative capacity of these molecules to mediate L-selectin-dependent adhesion has not been explored. In this study, we examined under shear stress conditions L-selectin-dependent leukocyte adhesive interactions mediated by HCELL and PSGL-1, both as naturally expressed on human HC membranes and as purified molecules. By utilizing both Stamper-Woodruff and parallel-plate flow chamber assays, we found that HCELL displayed a 5-fold greater capacity to support L-selectin-dependent leukocyte adherence across a broad range of shear stresses compared with that of PSGL-1. Moreover, L-selectin-mediated leukocyte binding to immunopurified HCELL was consistently >5-fold higher than leukocyte binding to equivalent amounts of PSGL-1. Taken together, these data indicate that HCELL is a more avid L-selectin ligand than PSGL-1 and may be the preferential mediator of L-selectin-dependent adhesive interactions among human HCs in the bone marrow.
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41

Nolte, D., P. Schmid, U. Jager, A. Botzlar, F. Roesken, R. Hecht, E. Uhl, K. Messmer, and D. Vestweber. "Leukocyte rolling in venules of striated muscle and skin is mediated by P-selectin, not by L-selectin." American Journal of Physiology-Heart and Circulatory Physiology 267, no. 4 (October 1, 1994): H1637—H1642. http://dx.doi.org/10.1152/ajpheart.1994.267.4.h1637.

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Leukocyte rolling in post-capillary venules is mediated by adhesion molecules of the selectin family expressed on both leukocytes (L-selectin) and endothelial cells (E- and P-selectin). With the use of intravital fluorescence microscopy, the effects of antibodies against these selectins were analyzed in the skinfold chamber model of BALB/c mice and the ear model of homozygous hairless mice (hr/hr) that permit chronic observation of striated muscle and skin microcirculation in awake animals, respectively. Mice were injected intravenously with monoclonal antibodies (MAb) to murine L-selectin and E-selectin and affinity-purified polyclonal antibodies to P-selectin. The antibodies, which are known to block cell adhesion, were tested by immunoprecipitation to selectively bind to L-, E-, or P-selectin. Leukocyte rolling was a constant finding in both microcirculation models in the absence of inflammatory stimuli. In both models, injection of anti-P-selectin antibodies completely prevented baseline leukocyte rolling over an observation period of 2 h (P < 0.01 vs. baseline), while no effects were seen after administration of either anti-L-selectin or anti-E-selectin MAb. Treatment with the isotype-matched control antibodies did not affect leukocyte rolling in either model. We conclude that leukocyte rolling in postcapillary venules of murine striated muscle and skin is a physiological process mediated via P-selectin, whereas L- and E-selectin appear not to play a significant role under these circumstances.
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42

Collins, Robert G., Unsu Jung, Maricela Ramirez, Daniel C. Bullard, M. John Hicks, C. Wayne Smith, Klaus Ley, and Arthur L. Beaudet. "Dermal and pulmonary inflammatory disease in E-selectin and P-selectin double-null mice is reduced in triple-selectin–null mice." Blood 98, no. 3 (August 1, 2001): 727–35. http://dx.doi.org/10.1182/blood.v98.3.727.

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Abstract In the initial phase of an inflammatory response, leukocytes marginate and roll along the endothelial surface as a result of adhesive interactions between molecules on the endothelial cells and leukocytes. To evaluate the role of the 3 selectins (E, L, and P) in leukocyte rolling and emigration, a null mutation for L-selectin was introduced into previously described embryonic stem cells with null mutations in the genes for both E-selectin and P-selectin (E/P double mutants) to produce triple-selectin–null mice (E-selectin, L-selectin, and P-selectin [E/L/P] triple mutants). Triple-selectin homozygous mutant mice are viable and fertile and only rarely develop the severe mucocutaneous infections or pulmonary inflammation characteristic of E/P double-mutant mice. Surface expression of L-selectin was undetectable in triple-mutant mice on fluorescence-activated cell-sorter analysis of peripheral neutrophils. Pathological studies revealed moderate cervical lymphadenopathy and lymphoplasmacytic infiltrate, but these were less extensive than in E/P double-mutant mice. Neutrophil emigration during thioglycolate-induced peritonitis was significantly reduced at 4, 8, and 24 hours (35%, 65%, and 46% of wild-type values, respectively). Intravital microscopy of the cremaster muscle revealed almost no rolling at times up to 6 hours after exteriorization, with or without addition of tumor necrosis factor α. The small amount of residual rolling was dependent on α4-integrin. The occurrence of skin and pulmonary disease in E/P double-mutant mice but not E/L/P triple-mutant mice suggests that deficiency of L-selectin alters the inflammatory response in E/P mutants.
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43

Collins, Robert G., Unsu Jung, Maricela Ramirez, Daniel C. Bullard, M. John Hicks, C. Wayne Smith, Klaus Ley, and Arthur L. Beaudet. "Dermal and pulmonary inflammatory disease in E-selectin and P-selectin double-null mice is reduced in triple-selectin–null mice." Blood 98, no. 3 (August 1, 2001): 727–35. http://dx.doi.org/10.1182/blood.v98.3.727.h8000727_727_735.

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In the initial phase of an inflammatory response, leukocytes marginate and roll along the endothelial surface as a result of adhesive interactions between molecules on the endothelial cells and leukocytes. To evaluate the role of the 3 selectins (E, L, and P) in leukocyte rolling and emigration, a null mutation for L-selectin was introduced into previously described embryonic stem cells with null mutations in the genes for both E-selectin and P-selectin (E/P double mutants) to produce triple-selectin–null mice (E-selectin, L-selectin, and P-selectin [E/L/P] triple mutants). Triple-selectin homozygous mutant mice are viable and fertile and only rarely develop the severe mucocutaneous infections or pulmonary inflammation characteristic of E/P double-mutant mice. Surface expression of L-selectin was undetectable in triple-mutant mice on fluorescence-activated cell-sorter analysis of peripheral neutrophils. Pathological studies revealed moderate cervical lymphadenopathy and lymphoplasmacytic infiltrate, but these were less extensive than in E/P double-mutant mice. Neutrophil emigration during thioglycolate-induced peritonitis was significantly reduced at 4, 8, and 24 hours (35%, 65%, and 46% of wild-type values, respectively). Intravital microscopy of the cremaster muscle revealed almost no rolling at times up to 6 hours after exteriorization, with or without addition of tumor necrosis factor α. The small amount of residual rolling was dependent on α4-integrin. The occurrence of skin and pulmonary disease in E/P double-mutant mice but not E/L/P triple-mutant mice suggests that deficiency of L-selectin alters the inflammatory response in E/P mutants.
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44

Kansas, GS, KB Saunders, K. Ley, A. Zakrzewicz, RM Gibson, BC Furie, B. Furie, and TF Tedder. "A role for the epidermal growth factor-like domain of P-selectin in ligand recognition and cell adhesion." Journal of Cell Biology 124, no. 4 (February 15, 1994): 609–18. http://dx.doi.org/10.1083/jcb.124.4.609.

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The selectin family of adhesion molecules mediates the initial interactions of leukocytes with endothelium. The extracellular region of each selectin contains an amino-terminal C-type lectin domain, followed by an EGF-like domain and multiple short consensus repeat units (SCR). Previous studies have indirectly suggested a role for each of the extracellular domains of the selectins in cell adhesion. In this study, a panel of chimeric selectins created by exchange of domains between L- and P-selectin was used to directly examine the role of the extracellular domains in cell adhesion. Exchange of only the lectin domains between L- and P-selectin conferred the adhesive and ligand recognition functions of the lectin domain of the parent molecule. However, chimeric selectins which contained both the lectin domain of L-selectin and the EGF-like domain of P-selectin exhibited dual ligand-binding specificity. These chimeric proteins supported adhesion both to myeloid cells and to high endothelial venules (HEV) of lymph nodes and mesenteric venules in vivo. Exchange of the SCR domains had no detectable effect on receptor function or specificity. Thus, the EGF-like domain of P-selectin may play a direct role in ligand recognition and leukocyte adhesion mediated by P-selectin, with the lectin plus EGF-like domains collectively forming a functional ligand recognition unit.
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45

Ivetic, A., and A. J. Ridley. "The telling tail of L-selectin." Biochemical Society Transactions 32, no. 6 (October 26, 2004): 1118–21. http://dx.doi.org/10.1042/bst0321118.

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L-selectin is constitutively expressed on the surface of most leucocytes and is important for tethering and subsequent rolling of leucocytes on endothelial cells, facilitating their migration into secondary lymphoid organs (e.g. naive T cells) and sites of inflammation (e.g. neutrophils). Previous studies have shown that the 17-amino-acid L-selectin cytoplasmic tail is important for its function in cell adhesion and, hence, identifying binding partners will provide insight into how L-selectin is regulated in leucocytes. This review describes currently known binding partners of the L-selectin tail and how their associations affect L-selectin function.
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46

Evans, Sharon S., Wan-Chao Wang, Mark D. Bain, Randy Burd, Julie R. Ostberg, and Elizabeth A. Repasky. "Fever-range hyperthermia dynamically regulates lymphocyte delivery to high endothelial venules." Blood 97, no. 9 (May 1, 2001): 2727–33. http://dx.doi.org/10.1182/blood.v97.9.2727.

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Abstract Fever is associated with increased survival during acute infection, although its mechanism of action is largely unknown. This study found evidence of an unexpectedly integrated mechanism by which fever-range temperatures stimulate lymphocyte homing to secondary lymphoid tissues by increasing L-selectin and α4β7 integrin–dependent adhesive interactions between circulating lymphocytes and specialized high endothelial venules (HEV). Exposure of splenic lymphocytes in vivo to fever-like whole-body hyperthermia (WBH; 39.8 ± 0.2°C for 6 hours) stimulated both L-selectin and α4β7 integrin–dependent adhesion of lymphocytes to HEV under shear conditions in lymph nodes and Peyer patches. The adhesiveness of HEV ligands for L-selectin and α4β7 integrin (ie, peripheral lymph node addressin and mucosal addressin cell adhesion molecule-1) also increased during WBH or febrile responses associated with lipopolysaccharide-induced or turpentine-induced inflammation. Similar increases in HEV adhesion occurred during hyperthermia treatment of lymph node and Peyer patch organ cultures in vitro, indicating that the local lymphoid tissue microenvironment is sufficient for the hyperthermia response. In contrast, WBH did not augment adhesion in squamous endothelium of nonlymphoid tissues. Analysis of homing of α4β7hi L-selectinlo murine TK1 cells and L-selectinhi α4β7 integrin-negative 300.19/L-selectin transfectant cells showed that fever-range temperatures caused a 3- to 4-fold increase in L-selectin and α4β7 integrin–dependent trafficking to secondary lymphoid tissues. Thus, enhanced lymphocyte delivery to HEV by febrile temperatures through bimodal regulation of lymphocyte and endothelial adhesion provides a novel mechanism to promote immune surveillance.
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47

Ramos, Carroll L., McRae J. Smith, Karen R. Snapp, Geoffrey S. Kansas, George W. Stickney, Klaus Ley, and Michael B. Lawrence. "Functional Characterization of L-Selectin Ligands on Human Neutrophils and Leukemia Cell Lines: Evidence for Mucinlike Ligand Activity Distinct From P-Selectin Glycoprotein Ligand-1." Blood 91, no. 3 (February 1, 1998): 1067–75. http://dx.doi.org/10.1182/blood.v91.3.1067.

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Abstract Recent reports have shown that leukocyte-leukocyte adhesion is dependent on L-selectin and that leukocyte recognition of L-selectin may be mediated by P-selectin glycoprotein ligand-1 (PSGL-1). We show that the specific attachment and rolling of human neutrophils and the leukemia cell lines HL-60 and U937 on immobilized, purified L-selectin under continuous shear stress is only partially inhibited by treatment with the PSGL-1 monoclonal antibody (MoAb), KPL1 (41% to 53% inhibition), suggesting that L-selectin ligand activity in addition to PSGL-1 may mediate myeloid cell rolling on L-selectin. K562 cells cotransfected with cDNAs encoding α(1,3)fucosyltransferase-VII (FucT-VII) and PSGL-1 rolled on L-selectin. Adhesion of FucT-VII-PSGL-1 transfectants to L-selectin was completely blocked by MoAb KPL1, indicating that both L-selectin and P-selectin bind similar sites on PSGL-1. In support of existence of a non–PSGL-1 L-selectin ligand activity on leukocytes, an HL-60 membrane preparation immunodepleted of PSGL-1 supported rolling of L-selectin, but not P-selectin transfectants. Treatment of HL-60 cells with O-sialoglycoprotein endopeptidase inhibited attachment and rolling on L-selectin and P-selectin. However, neuraminidase treatment completely blocked HL-60 rolling on L-selectin, but not P-selectin, suggesting L-selectin and P-selectin ligand activities have different contributions of sialic acid. These findings indicate that myeloid cells express sialylated, O-linked glycoprotein ligand activity independent of PSGL-1 that supports L-selectin–mediated rolling.
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48

Ramos, Carroll L., McRae J. Smith, Karen R. Snapp, Geoffrey S. Kansas, George W. Stickney, Klaus Ley, and Michael B. Lawrence. "Functional Characterization of L-Selectin Ligands on Human Neutrophils and Leukemia Cell Lines: Evidence for Mucinlike Ligand Activity Distinct From P-Selectin Glycoprotein Ligand-1." Blood 91, no. 3 (February 1, 1998): 1067–75. http://dx.doi.org/10.1182/blood.v91.3.1067.1067_1067_1075.

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Recent reports have shown that leukocyte-leukocyte adhesion is dependent on L-selectin and that leukocyte recognition of L-selectin may be mediated by P-selectin glycoprotein ligand-1 (PSGL-1). We show that the specific attachment and rolling of human neutrophils and the leukemia cell lines HL-60 and U937 on immobilized, purified L-selectin under continuous shear stress is only partially inhibited by treatment with the PSGL-1 monoclonal antibody (MoAb), KPL1 (41% to 53% inhibition), suggesting that L-selectin ligand activity in addition to PSGL-1 may mediate myeloid cell rolling on L-selectin. K562 cells cotransfected with cDNAs encoding α(1,3)fucosyltransferase-VII (FucT-VII) and PSGL-1 rolled on L-selectin. Adhesion of FucT-VII-PSGL-1 transfectants to L-selectin was completely blocked by MoAb KPL1, indicating that both L-selectin and P-selectin bind similar sites on PSGL-1. In support of existence of a non–PSGL-1 L-selectin ligand activity on leukocytes, an HL-60 membrane preparation immunodepleted of PSGL-1 supported rolling of L-selectin, but not P-selectin transfectants. Treatment of HL-60 cells with O-sialoglycoprotein endopeptidase inhibited attachment and rolling on L-selectin and P-selectin. However, neuraminidase treatment completely blocked HL-60 rolling on L-selectin, but not P-selectin, suggesting L-selectin and P-selectin ligand activities have different contributions of sialic acid. These findings indicate that myeloid cells express sialylated, O-linked glycoprotein ligand activity independent of PSGL-1 that supports L-selectin–mediated rolling.
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49

Zöllner, Olaf, Martin C. Lenter, James E. Blanks, Eric Borges, Martin Steegmaier, Hans-Günther Zerwes, and Dietmar Vestweber. "L-Selectin from Human, but Not from Mouse Neutrophils Binds Directly to E-Selectin." Journal of Cell Biology 136, no. 3 (February 10, 1997): 707–16. http://dx.doi.org/10.1083/jcb.136.3.707.

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L-Selectin on neutrophils as well as inducible E- and P-selectin on endothelium are involved in the recruitment of neutrophils into inflamed tissue. Based on cell attachment assays, L-selectin was suggested to function as a carbohydrate presenting ligand for E- and P-selectin. However, previous affinity isolation experiments with an E-selectin–Ig fusion protein had failed to detect L-selectin among the isolated E-selectin ligands from mouse neutrophils. We show here that L-selectin from human neutrophils, in contrast to mouse neutrophils, can be affinity-isolated as a major ligand from total cell extracts using E-selectin–Ig as affinity probe. Binding of human L-selectin to E-selectin was direct, since purified L-selectin could be reprecipitated with E-selectin–Ig. Recognition of L-selectin was abolished by sialidase-treatment, required Ca2+, and was resistant to treatment with endoglycosidase F. Binding of L-selectin to a P-selectin–Ig fusion protein was not observed. In agreement with the biochemical data, the anti–Lselectin mAb DREG56 inhibited rolling of human neutrophils on immobilized E-selectin–Ig but not on P-selectin–Ig. No such inhibitory effect was seen with the anti–mouse L-selectin mAb MEL14 on mouse neutrophils. Rolling of E-selectin transfectants on purified and immobilized human L-selectin was inhibited by mAb DREG56. We conclude that L-selectin on human neutrophils is a major glycoprotein ligand among very few glycoproteins that can be isolated by an E-selectin affinity matrix. The clear difference between human and mouse L-selectin suggests that E-selectin–binding carbohydrate moieties are attached to different protein scaffolds in different species.
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50

Shimada, Yuka, Shinichi Sato, Minoru Hasegawa, Thomas F. Tedder, and Kazuhiko Takehara. "Elevated serum L-selectin levels and abnormal regulation of L-selectin expression on leukocytes in atopic dermatitis: Soluble L-selectin levels indicate disease severity☆☆☆★." Journal of Allergy and Clinical Immunology 104, no. 1 (July 1999): 163–68. http://dx.doi.org/10.1016/s0091-6749(99)70128-4.

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