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Journal articles on the topic 'P-selectin ligand protein'

Author: Grafiati

Published: 4 May 2024

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1

Lenter, M., A. Levinovitz, S. Isenmann, and D. Vestweber. "Monospecific and common glycoprotein ligands for E- and P-selectin on myeloid cells." Journal of Cell Biology 125, no. 2 (1994): 471–81. http://dx.doi.org/10.1083/jcb.125.2.471.

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E- and P-selectin are inducible cell adhesion molecules on endothelial cells, which function as Ca(2+)-dependent lectins and mediate the binding of neutrophils and monocytes. We have recently identified a 150-kD glycoprotein ligand for E-selectin on mouse myeloid cells, using a recombinant antibody-like form of mouse E-selectin. Here, we report that this ligand does not bind to an analogous P-selectin fusion protein. Instead, the chimeric P-selectin-IgG protein recognizes a 160-kD glycoprotein on the mouse neutrophil progenitor 32D cl 3, on mature mouse neutrophils and on human HL60 cells. The

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2

Frenette, Paul S., Cécile V. Denis, Linnea Weiss, et al. "P-Selectin Glycoprotein Ligand 1 (Psgl-1) Is Expressed on Platelets and Can Mediate Platelet–Endothelial Interactions in Vivo." Journal of Experimental Medicine 191, no. 8 (2000): 1413–22. http://dx.doi.org/10.1084/jem.191.8.1413.

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The platelet plays a pivotal role in maintaining vascular integrity. In a manner similar to leukocytes, platelets interact with selectins expressed on activated endothelium. P-selectin glycoprotein ligand 1 (PSGL-1) is the main P-selectin ligand expressed on leukocytes. Searching for platelet ligand(s), we used a P-selectin–immunoglobulin G (IgG) chimera to affinity purify surface-biotinylated proteins from platelet lysates. P-selectin–bound ligands were eluted with ethylenediaminetetraacetic acid. An ∼210-kD biotinylated protein was isolated from both human neutrophil and platelet preparation

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3

HARMS, Gesche, Regine KRAFT, Gerlinde GRELLE, Bärbel VOLZ, Jens DERNEDDE, and Rudolf TAUBER. "Identification of nucleolin as a new L-selectin ligand." Biochemical Journal 360, no. 3 (2001): 531–38. http://dx.doi.org/10.1042/bj3600531.

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Apart from leucocyte–endothelial interactions, the adhesion molecule L-selectin mediates the homotypic adhesion of leucocytes during recruitment at sites of acute inflammation, as well as intercellular adhesion of haematopoietic progenitor cells during haematopoiesis. There is evidence that, in addition to P-selectin glycoprotein ligand-1, other as-yet-unidentified proteins function as L-selectin ligands on human leucocytes and haematopoietic progenitor cells. In the present study, we show: (i) by affinity chromatography on L-selectin–agarose; (ii) by protein identification using MS; and (iii)

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4

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 (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 tha

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5

Guyer, DA, KL Moore, EB Lynam, et al. "P-selectin glycoprotein ligand-1 (PSGL-1) is a ligand for L-selectin in neutrophil aggregation." Blood 88, no. 7 (1996): 2415–21. http://dx.doi.org/10.1182/blood.v88.7.2415.bloodjournal8872415.

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In inflammation, activated neutrophils adhere to endothelial cells and aggregate with one another. While beta 2-integrin and L-selectin are essential for aggregation, their ligands remain to be identified. We have previously shown that L-selectin mediates a carbohydrate-dependent interaction in aggregation (Simon et al: J Immunol 149:2765, 1992; Rochon et al: J Immunol 152:1385, 1994). We have suggested that the L-selectin counter-structure is a mucinlike protein and proposed that aggregation occurs through a two-step process involving L-selectin, beta 2-integrin, and their distinct counter-st

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6

Moore, K. L., N. L. Stults, S. Diaz, et al. "Identification of a specific glycoprotein ligand for P-selectin (CD62) on myeloid cells." Journal of Cell Biology 118, no. 2 (1992): 445–56. http://dx.doi.org/10.1083/jcb.118.2.445.

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P-selectin (CD62, GMP-140, PADGEM), a Ca(2+)-dependent lectin on activated platelets and endothelium, functions as a receptor for myeloid cells by interacting with sialylated, fucosylated lactosaminoglycans. P-selectin binds to a limited number of protease-sensitive sites on myeloid cells, but the protein(s) that carry the glycans recognized by P-selectin are unknown. Blotting of neutrophil or HL-60 cell membrane extracts with [125I]P-selectin and affinity chromatography of [3H]glucosamine-labeled HL-60 cell extracts were used to identify P-selectin ligands. A major ligand was identified with

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7

Zöllner, Olaf, Martin C. Lenter, James E. Blanks, et al. "L-Selectin from Human, but Not from Mouse Neutrophils Binds Directly to E-Selectin." Journal of Cell Biology 136, no. 3 (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 c

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8

Moore, K. L., K. D. Patel, R. E. Bruehl, et al. "P-selectin glycoprotein ligand-1 mediates rolling of human neutrophils on P-selectin." Journal of Cell Biology 128, no. 4 (1995): 661–71. http://dx.doi.org/10.1083/jcb.128.4.661.

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Neutrophils roll on P-selectin expressed by activated platelets or endothelial cells under the shear stresses in the microcirculation. P-selectin glycoprotein ligand-1 (PSGL-1) is a high affinity ligand for P-selectin on myeloid cells. However, it has not been demonstrated that PSGL-1 contributes to the rolling of neutrophils on P-selectin. We developed two IgG mAbs, PL1 and PL2, that appear to recognize protein-dependent epitopes on human PSGL-1. The mAbs bound to PSGL-1 on all leukocytes as well as on heterologous cells transfected with PSGL-1 cDNA. PL1, but not PL2, blocked binding of 125-I

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9

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 (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 tr

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10

Evangelista, Virgilio, Stefano Manarini, Rita Sideri, et al. "Platelet/Polymorphonuclear Leukocyte Interaction: P-Selectin Triggers Protein-Tyrosine Phosphorylation–Dependent CD11b/CD18 Adhesion: Role of PSGL-1 as a Signaling Molecule." Blood 93, no. 3 (1999): 876–85. http://dx.doi.org/10.1182/blood.v93.3.876.

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Abstract Polymorphonuclear leukocyte (PMN) adhesion to activated platelets is important for the recruitment of PMN at sites of vascular damage and thrombus formation. We have recently shown that binding of activated platelets to PMN in mixed cell suspensions under shear involves P-selectin and the activated β2-integrin CD11b/CD18. Integrin activation required signaling mechanisms that were sensitive to tyrosine kinase inhibitors.1 Here we show that mixing activated, paraformaldehyde (PFA)-fixed platelets with PMNs under shear conditions leads to rapid and fully reversible tyrosine phosphorylat

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11

Evangelista, Virgilio, Stefano Manarini, Rita Sideri, et al. "Platelet/Polymorphonuclear Leukocyte Interaction: P-Selectin Triggers Protein-Tyrosine Phosphorylation–Dependent CD11b/CD18 Adhesion: Role of PSGL-1 as a Signaling Molecule." Blood 93, no. 3 (1999): 876–85. http://dx.doi.org/10.1182/blood.v93.3.876.403k25_876_885.

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Polymorphonuclear leukocyte (PMN) adhesion to activated platelets is important for the recruitment of PMN at sites of vascular damage and thrombus formation. We have recently shown that binding of activated platelets to PMN in mixed cell suspensions under shear involves P-selectin and the activated β2-integrin CD11b/CD18. Integrin activation required signaling mechanisms that were sensitive to tyrosine kinase inhibitors.1 Here we show that mixing activated, paraformaldehyde (PFA)-fixed platelets with PMNs under shear conditions leads to rapid and fully reversible tyrosine phosphorylation of a

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12

Snapp, Karen R., Amy J. Wagers, Ron Craig, Lloyd M. Stoolman, and Geoffrey S. Kansas. "P-Selectin Glycoprotein Ligand-1 Is Essential for Adhesion to P-Selectin But Not E-Selectin in Stably Transfected Hematopoietic Cell Lines." Blood 89, no. 3 (1997): 896–901. http://dx.doi.org/10.1182/blood.v89.3.896.

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Abstract P-selectin (CD62P) is a member of the selectin family of adhesion molecules involved in the regulation of leukocyte traffic. P-selectin glycoprotein ligand-1 (PSGL-1) is a mucin-like molecule that is thought to be a primary ligand for P-selectin. The interaction of P-selectin with PSGL-1 results in leukocyte rolling and recruitment of leukocytes to sites of inflammation and tissue injury. However, expression of PSGL-1 protein alone is insufficient for binding to P-selectin. Several posttranslational modifications of PSGL-1, including sialylation, sulfation, and fucosylation by α1,3-fu

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13

Kappelmayer, János, and Béla Nagy. "The Interaction of Selectins and PSGL-1 as a Key Component in Thrombus Formation and Cancer Progression." BioMed Research International 2017 (2017): 1–18. http://dx.doi.org/10.1155/2017/6138145.

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Cellular interaction is inevitable in the pathomechanism of human disease. Formation of heterotypic cellular aggregates, between distinct cells of hematopoietic and nonhematopoietic origin, may be involved in events leading to inflammation and the complex process of cancer progression. Among adhesion receptors, the family of selectins with their ligands have been considered as one of the major contributors to cell-cell interactions. Consequently, the inhibition of the interplay between selectins and their ligands may have potential therapeutic benefits. In this review, we focus on the current

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14

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 (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

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15

Geng, Jian-Guo, Hai-Bo Wang, Ming Chen, et al. "P-Selectin Activates Leukocyte Integrin alphaMbeta2 by Recruiting Phosphatidylinositol-3 Kinase to P-Selectin Glycoprotein Ligand-1 Cytoplasmic Domain through Adaptor Protein Naf1." Blood 104, no. 11 (2004): 652. http://dx.doi.org/10.1182/blood.v104.11.652.652.

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Abstract The interaction of endothelial P-selectin (CD62P) with neutrophil PSGL-1 (P-selectin glycoprotein ligand-1, CD162) mediates neutrophil rolling, which acts in concert with cytokines and chemoattractants for integrin-mediated firm adhesion of neutrophils to vascular endothelial cells. Numerous studies have established that this sequence of events is critical to the extravasation of neutrophils during an inflammatory response. We have recently shown that cross-linking of PSGL-1 with P-selectin acts cooperatively with extracellular stimuli, such as cytokines and chemoattractants released

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16

Gardiner, Elizabeth E., Mariagrazia De Luca, Tracy McNally, Alan D. Michelson, Robert K. Andrews, and Michael C. Berndt. "Regulation of P-selectin binding to the neutrophil P-selectin counter-receptor P-selectin glycoprotein ligand-1 by neutrophil elastase and cathepsin G." Blood 98, no. 5 (2001): 1440–47. http://dx.doi.org/10.1182/blood.v98.5.1440.

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In the inflammatory response, leukocyte rolling before adhesion and transmigration through the blood vessel wall is mediated by specific cell surface adhesion receptors. Neutrophil rolling involves the interaction of P-selectin expressed on activated endothelium and its counter-receptor on neutrophils, P-selectin glycoprotein ligand-1 (PSGL-1). Here, it is reported that P-selectin binding to neutrophils is lost under conditions that cause the release of proteinases from neutrophil primary granules. Treatment of neutrophils with the purified neutrophil granule proteinases, cathepsin G and elast

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17

Lo, Chi Y., Aristotelis Antonopoulos, Rohitesh Gupta, et al. "Competition between Core-2 GlcNAc-transferase and ST6GalNAc-transferase Regulates the Synthesis of the Leukocyte Selectin Ligand on Human P-selectin Glycoprotein Ligand-1." Journal of Biological Chemistry 288, no. 20 (2013): 13974–87. http://dx.doi.org/10.1074/jbc.m113.463653.

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The binding of selectins to carbohydrate ligands expressed on leukocytes regulates immunity and inflammation. Among the human selectin ligands, the O-linked glycans at the N-terminus of the leukocyte cell-surface molecule P-selectin glycoprotein ligand-1 (PSGL-1, CD162) are important because they bind all selectins (L-, E-, and P-selectin) with high affinity under hydrodynamic shear conditions. Analysis of glycan microheterogeneity at this site is complicated by the presence of 72 additional potential O-linked glycosylation sites on this mucinous protein. To overcome this limitation, truncated

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18

Thomas, Wendy. "For catch bonds, it all hinges on the interdomain region." Journal of Cell Biology 174, no. 7 (2006): 911–13. http://dx.doi.org/10.1083/jcb.200609029.

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Tensile mechanical force was long assumed to increase the detachment rates of biological adhesive bonds (Bell, 1978). However, in the last few years, several receptor–ligand pairs were shown to form “catch bonds,” whose lifetimes are enhanced by moderate amounts of force. These include the bacterial adhesive protein FimH binding to its ligand mannose (Thomas et al., 2002; Thomas et al., 2006), blood cell adhesion proteins P- and L-selectin binding to sialyl Lewis X (sLeX)–containing ligands (Marshall et al., 2003; Evans et al., 2004; Sarangapani et al., 2004), and the myosin–actin motor protei

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19

Bestebroer, Jovanka, Miriam J. J. G. Poppelier, Laurien H. Ulfman, et al. "Staphylococcal superantigen-like 5 binds PSGL-1 and inhibits P-selectin–mediated neutrophil rolling." Blood 109, no. 7 (2006): 2936–43. http://dx.doi.org/10.1182/blood-2006-06-015461.

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Abstract Staphylococcus aureus secretes several virulence factors interfering with host-cell functions. Staphylococcal superantigen-like (SSL) proteins are a family of 11 exotoxins with structural homology to superantigens but with generally unknown functions. Recently, we described that chemotaxis inhibitory protein of Staphylococcus aureus (CHIPS31-121), a potent inhibitor of C5a-induced responses, is structurally homologous to the C-terminal domain of SSL5. Here, we identify P-selectin glycoprotein ligand-1 (PSGL-1), involved in the initial rolling of neutrophils along the endothelium, as a

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20

Torgersen, Dawn, Nicholas P. Mullin, and Kurt Drickamer. "Mechanism of Ligand Binding to E- and P-selectin Analyzed Using Selectin/Mannose-binding Protein Chimeras." Journal of Biological Chemistry 273, no. 11 (1998): 6254–61. http://dx.doi.org/10.1074/jbc.273.11.6254.

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21

Musser, John H., Mark B. Anderson, and Daniel E. Levy. "Glycomimetics as Selectin Inhibitors." Current Pharmaceutical Design 1, no. 2 (1995): 221–32. http://dx.doi.org/10.2174/1381612801666220918090305.

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The selectins are a family of cell adhesion molecules involved in the rolling stage of the transendothelial migration of leukocytes and their principal interaction is with cell-surface carbohydrates such as sialyl Lewis X (sLex). The selectin family currently consists of E-selectin, found on cytokine-activated endothelial cells, L selectin, identified by reaction with the monoclonal antibody MEL-14, and P-selectin, characterized utilizing antibodies differentiating between activated and resting platelets. The structural motifs of the selectins consist of a lectin binding domain succeeded by a

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22

Yang, J., J. Galipeau, CA Kozak, BC Furie, and B. Furie. "Mouse P-selectin glycoprotein ligand-1: molecular cloning, chromosomal localization, and expression of a functional P-selectin receptor." Blood 87, no. 10 (1996): 4176–86. http://dx.doi.org/10.1182/blood.v87.10.4176.bloodjournal87104176.

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A mouse homolog of P-selectin glycoprotein ligand-1 (PSGL-1), a P- selectin receptor on myeloid cells, has been cloned using the human cDNA sequence to probe a cDNA library prepared from the mouse WEHI-3 monocytic cell line and a genomic DNA library prepared from 129/SvJ mouse tissue. The gene flanking the entire open reading frame of 397 amino acids is composed of a single exon. Mouse and human PSGL-1 show an overall similarity of 67% and an identity of 50% and contain a similar domain organization. However, there are 10 threonine/serine- rich decameric repeats in mouse PSGL-1 as compared wit

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Rivera-Nieves, Jesús, Tracy L. Burcin, Timothy S. Olson, et al. "Critical role of endothelial P-selectin glycoprotein ligand 1 in chronic murine ileitis." Journal of Experimental Medicine 203, no. 4 (2006): 907–17. http://dx.doi.org/10.1084/jem.20052530.

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L-selectin ligands might be relevant for inflammatory cell trafficking into the small intestine in a spontaneous model of chronic ileitis (i.e., SAMP1/YitFc mice). Immunoblockade of peripheral node addressin or mucosal addressin cell adhesion molecule 1 failed to ameliorate ileitis, whereas P-selectin glycoprotein ligand 1 (PSGL-1) neutralization attenuated both the adoptively transferred and spontaneous disease. PSGL-1 was detected in venules of mesenteric lymph node and small intestine by immunohistochemistry and confirmed by real-time reverse transcription polymerase chain reaction and flow

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Snapp, Karen R., Christine E. Heitzig, and Geoffrey S. Kansas. "Attachment of the PSGL-1 cytoplasmic domain to the actin cytoskeleton is essential for leukocyte rolling on P-selectin." Blood 99, no. 12 (2002): 4494–502. http://dx.doi.org/10.1182/blood.v99.12.4494.

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P-selectin glycoprotein ligand–1 (PSGL-1) serves as the leukocyte ligand for P-selectin, and many of the structural features of its ectodomain required for interactions with P-selectin have been uncovered. In contrast, the function of the highly conserved PSGL-1 cytoplasmic domain has not been explored. Stable transfectants expressing similar levels of either wild-type PSGL-1 or truncated PSGL-1 in which only 4 cytoplasmic residues were retained (designated PSGL-1Δcyto), were analyzed. Transfectants expressing full-length PSGL-1 rolled well on P-selectin. In contrast, rolling was almost comple

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Senczuk, Anna M., John C. Reeder, Magda M. Kosmala, and May Ho. "Plasmodium falciparum erythrocyte membrane protein 1 functions as a ligand for P-selectin." Blood 98, no. 10 (2001): 3132–35. http://dx.doi.org/10.1182/blood.v98.10.3132.

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Abstract The malarial protein Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) is a parasite protein that is exported to the surface of the infected erythrocyte, where it is inserted into the red cell cytoskeleton in the second half of the parasite life cycle. The surface expression of PfEMP1 coincides with the occurrence of the adhesion of infected erythrocytes to vascular endothelium. This protein has been shown to interact with CD36, intercellular adhesion molecule-1 (ICAM-1) and chondroitin sulfate A (CSA). In this study, it is demonstrated by affinity purification and western

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26

von Andrian, UH, JD Chambers, EL Berg, et al. "L-selectin mediates neutrophil rolling in inflamed venules through sialyl LewisX-dependent and -independent recognition pathways." Blood 82, no. 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 o

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27

Borges, Eric, Wolfgang Tietz, Martin Steegmaier, et al. "P-Selectin Glycoprotein Ligand-1 (PSGL-1) on T Helper 1 but Not on T Helper 2 Cells Binds to P-Selectin and Supports Migration into Inflamed Skin." Journal of Experimental Medicine 185, no. 3 (1997): 573–78. http://dx.doi.org/10.1084/jem.185.3.573.

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We have shown recently that mouse Th1 cells but not Th2 cells are selectively recruited into inflamed sites of a delayed-type hypersensitivity (DTH) reaction of the skin. This migration was blocked by monoclonal antibodies (mAb) against P- and E-selectin. Here we show that Th1 cells bind to P-selectin via the P-selectin glycoprotein ligand-1 (PSGL-1). This is the only glycoprotein ligand that was detectable by affinity isolation with a P-selectin–Ig fusion protein. Binding of Th1 cells to P-selectin, as analyzed by flow cytometry and in cell adhesion assays, was completely blocked by antibodie

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Salmi, Marko, Sami Tohka, Ellen L. Berg, Eugene C. Butcher, and Sirpa Jalkanen. "Vascular Adhesion Protein 1 (VAP-1) Mediates Lymphocyte Subtype-specific, Selectin-independent Recognition of Vascular Endothelium in Human Lymph Nodes." Journal of Experimental Medicine 186, no. 4 (1997): 589–600. http://dx.doi.org/10.1084/jem.186.4.589.

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Interactions between lymphocyte surface receptors and their ligands on vascular endothelial cells regulate the exit of lymphocytes from the circulation. Distinct subsets of mononuclear cells bind to high endothelial venules (HEVs) in different lymphoid organs to a different extent, but the molecular mechanisms behind this selectivity have remained poorly characterized. Here we show that vascular adhesion protein-1 (VAP-1) mediates subtype-specific binding of CD8-positive T cells and natural killer cells to human endothelium. VAP-1–dependent, oligosaccharide-dependent peripheral lymph node (PLN

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29

Mehta, Padmaja, Kamala D. Patel, Thomas M. Laue, Harold P. Erickson, and Rodger P. McEver. "Soluble Monomeric P-Selectin Containing Only the Lectin and Epidermal Growth Factor Domains Binds to P-Selectin Glycoprotein Ligand-1 on Leukocytes." Blood 90, no. 6 (1997): 2381–89. http://dx.doi.org/10.1182/blood.v90.6.2381.

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Abstract Under shear stress, leukocytes use P-selectin glycoprotein ligand-1 (PSGL-1) to tether to and roll on P-selectin expressed on activated platelets or endothelial cells. P-selectin has an NH2-terminal lectin domain, an epidermal growth factor (EGF)-like motif, nine consensus repeats (CRs), a transmembrane domain, and a cytoplasmic tail. To determine whether the CRs are required for P-selectin to bind PSGL-1, we expressed a soluble protein (Lec-EGF) that contained only the lectin and EGF domains, plus a short C-terminal epitope tag. Electron microscopy and hydrodynamic analysis confirmed

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30

Mehta, Padmaja, Kamala D. Patel, Thomas M. Laue, Harold P. Erickson, and Rodger P. McEver. "Soluble Monomeric P-Selectin Containing Only the Lectin and Epidermal Growth Factor Domains Binds to P-Selectin Glycoprotein Ligand-1 on Leukocytes." Blood 90, no. 6 (1997): 2381–89. http://dx.doi.org/10.1182/blood.v90.6.2381.2381_2381_2389.

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Under shear stress, leukocytes use P-selectin glycoprotein ligand-1 (PSGL-1) to tether to and roll on P-selectin expressed on activated platelets or endothelial cells. P-selectin has an NH2-terminal lectin domain, an epidermal growth factor (EGF)-like motif, nine consensus repeats (CRs), a transmembrane domain, and a cytoplasmic tail. To determine whether the CRs are required for P-selectin to bind PSGL-1, we expressed a soluble protein (Lec-EGF) that contained only the lectin and EGF domains, plus a short C-terminal epitope tag. Electron microscopy and hydrodynamic analysis confirmed that Lec

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Cappenberg, Anika, Marina Kardell, and Alexander Zarbock. "Selectin-Mediated Signaling—Shedding Light on the Regulation of Integrin Activity in Neutrophils." Cells 11, no. 8 (2022): 1310. http://dx.doi.org/10.3390/cells11081310.

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As a consequence of tissue injury or infection, neutrophils are recruited in a stepwise recruitment process from the bloodstream into the surrounding tissue. Selectins are a family of adhesion molecules comprised of L-, E-, and P-selectin. Differences in expression patterns, protein structure, and ligand binding characteristics mediate distinct functions of each selectin. Interactions of selectins and their counter-receptors mediate the first contact of neutrophils with the endothelium, as well as subsequent neutrophil rolling along the endothelial surface. For efficient neutrophil recruitment

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Cano-Mendez, Alan, Nallely García-Larragoiti, Maria Damian-Vazquez, et al. "Platelet Reactivity and Inflammatory Phenotype Induced by Full-Length Spike SARS-CoV-2 Protein and Its RBD Domain." International Journal of Molecular Sciences 23, no. 23 (2022): 15191. http://dx.doi.org/10.3390/ijms232315191.

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A state of immunothrombosis has been reported in COVID-19. Platelets actively participate in this process. However, little is known about the ability of SARS-CoV-2 virus proteins to induce platelet activity. Platelet-rich plasma (PRP) was incubated with spike full-length protein and the RBD domain in independent assays. We evaluated platelet activation through the expression of P-selectin and activation of glicoprotein IIbIIIa (GP IIbIIIa), determined by flow cytometry and the ability of the proteins to induce platelet aggregation. We determined concentrations of immunothrombotic biomarkers in

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Maugeri, Norma, Patrizia Rovere-Querini, Virgilio Evangelista та ін. "Neutrophils phagocytose activated platelets in vivo: a phosphatidylserine, P-selectin, and β2 integrin–dependent cell clearance program". Blood 113, № 21 (2009): 5254–65. http://dx.doi.org/10.1182/blood-2008-09-180794.

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Abstract Activated platelets express ligands, which are recognized by counterreceptors on neutrophils. Here, we show that the ensuing cell-to-cell interaction programs neutrophil phagocytic function, resulting in activated platelet clearance. Neutrophils that have internalized platelets circulate in the blood of patients with acute myocardial infarction, and the extent of platelet clearance correlates with expression of platelet activation, including P-selectin. Activated platelets injected intravenously in experimental animals are detectable in circulating neutrophils 60 minutes after, and wi

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Lu, Sydney X., Maria Lia Palomba, Il-Kang Na, et al. "P-Selectin in Recipients of Allogeneic Bone Marrow Transplantation Regulates Experimental Graft-Versus-Host-Disease." Blood 114, no. 22 (2009): 1335. http://dx.doi.org/10.1182/blood.v114.22.1335.1335.

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Abstract Abstract 1335 Poster Board I-357 Alloreactive T cells are crucial for graft-versus-host-disease (GVHD) pathophysiology, and we hypothesized that controlling their trafficking can ameliorate GVHD. P-selectin is a dimeric glycoprotein found on most inflamed endothelium, which interacts with multiple lectin-type molecules on leukocytes, including T cells. We used murine allogenienc BMT models to study GVHD and found that P-selectin−/− recipients exhibited significantly less GVHD mortality and morbidity, as well as decreased GVHD of the skin, liver and small bowels. However, WT and P-sele

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Chien, Sylvia S., Jin Dai, John L. Magnani, et al. "E-Selectin Ligand Expression By Leukemic Blasts Is Associated with Prognosis in Patients with AML." Blood 132, Supplement 1 (2018): 1513. http://dx.doi.org/10.1182/blood-2018-99-119449.

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Abstract Introduction. The E-selectin ligand is a carbohydrate structure (sialyl Lewis x) expressed on myeloid cells and plays a role in cell adhesion and activation by binding specifically to E-selectin on endothelial cells. Acute myeloid leukemia (AML) blasts express the E-selectin ligand on glycoforms of CD44, CD62L and CD65. Interaction of AML blasts in the marrow microenvironment is believed to involve a number of receptors, including CXCR4, VLA4, and CD44. E-selectin in the vascular niche regulates dormancy for hematopoietic stem cells (Winkler IG et al. 2012), and chemoresistance and su

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Barkalow, Fern J., Kurt L. Barkalow, and Tanya N. Mayadas. "Dimerization of P-selectin in platelets and endothelial cells." Blood 96, no. 9 (2000): 3070–77. http://dx.doi.org/10.1182/blood.v96.9.3070.

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Abstract P-selectin is a leukocyte adhesion receptor stored in platelets and endothelial cells and is translocated to the surface upon cell activation. Purified P-selectin is oligomeric and has increased avidity for its ligand relative to the monomeric form, but whether P-selectin self-associates in the membrane of intact cells is not known. A chemical cross-linking approach was used to show that P-selectin is present as noncovalent dimers in resting platelets, human umbilical vein endothelial cells, and heterologous RIN5F cells expressing P-selectin. The results of 2-dimensional isoelectric f

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Barkalow, Fern J., Kurt L. Barkalow, and Tanya N. Mayadas. "Dimerization of P-selectin in platelets and endothelial cells." Blood 96, no. 9 (2000): 3070–77. http://dx.doi.org/10.1182/blood.v96.9.3070.h8003070_3070_3077.

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P-selectin is a leukocyte adhesion receptor stored in platelets and endothelial cells and is translocated to the surface upon cell activation. Purified P-selectin is oligomeric and has increased avidity for its ligand relative to the monomeric form, but whether P-selectin self-associates in the membrane of intact cells is not known. A chemical cross-linking approach was used to show that P-selectin is present as noncovalent dimers in resting platelets, human umbilical vein endothelial cells, and heterologous RIN5F cells expressing P-selectin. The results of 2-dimensional isoelectric focusing a

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Park, Jinho, Kyoung Seong Choi, and J. Stephen Dumler. "Major Surface Protein 2 of Anaplasma phagocytophilum Facilitates Adherence to Granulocytes." Infection and Immunity 71, no. 7 (2003): 4018–25. http://dx.doi.org/10.1128/iai.71.7.4018-4025.2003.

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ABSTRACT Anaplasma phagocytophilum is an obligate intracellular bacterium that infects myeloid cells in the mammalian host. Msp2 (p44) is the major immunodominant outer-membrane protein of these bacteria. We hypothesized that Msp2 acts as an adhesin for A. phagocytophilum entry into granulocytes. This potential role was investigated by blocking binding with Msp2 monoclonal antibodies and by antagonizing binding and propagation with recombinant Msp2 (rMsp2) in vitro. With HL-60 cells, fresh human peripheral blood neutrophils, and a cell line devoid of the fucosylated platelet selectin glycoprot

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Volcik, Kelly A., Diane Catellier, Aaron R. Folsom, Nena Matijevic, Bruce Wasserman, and Eric Boerwinkle. "SELP and SELPLG Genetic Variation Is Associated with Cell Surface Measures of SELP and SELPLG: The Atherosclerosis Risk in Communities Carotid MRI Study." Clinical Chemistry 55, no. 6 (2009): 1076–82. http://dx.doi.org/10.1373/clinchem.2008.119487.

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Abstract Background: P-selectin (SELP) and its ligand, P-selectin glycoprotein ligand 1 (SELPLG), play key roles in both the inflammatory response and the atherosclerotic process. Previous studies have shown genetic variation in the SELP gene [selectin P (granule membrane protein 140kDa, antigen CD62)] to be associated with plasma SELP concentrations; however, the major biological function of SELP (and SELPLG) is at the cell surface. We therefore investigated the association of SELP polymorphisms with platelet SELP measures and polymorphisms in the SELPLG gene (selectin P ligand) with lymphocy

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Pierce, Elizabeth, Sung Choi, Krystyna Olkiewicz, et al. "Critical role for selectin receptor:ligand interactions in the development of IPS following allogeneic BMT (145.32)." Journal of Immunology 184, no. 1_Supplement (2010): 145.32. http://dx.doi.org/10.4049/jimmunol.184.supp.145.32.

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Abstract Idiopathic pneumonia syndrome (IPS) is a frequently fatal complication of allogeneic BMT and limits successful outcomes. The pathophysiology of IPS involves the release of soluble inflammatory proteins and the recruitment of donor lymphoid and myeloid effectors into the lung. The entry of leukocytes into inflamed tissue is mediated by several molecules that are orchestrated in a sequential manner. We used well-established mouse BMT models to investigate the role of selectin (sel) receptor:ligand interactions in the development of IPS. Firstly, E and P sel ligands are up-regulated on d

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Underhill, Gregory H., Heather A. Minges-Wols, Jamie L. Fornek, Pamela L. Witte, and Geoffrey S. Kansas. "IgG plasma cells display a unique spectrum of leukocyte adhesion and homing molecules." Blood 99, no. 8 (2002): 2905–12. http://dx.doi.org/10.1182/blood.v99.8.2905.

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Abstract Long-lived antibody-secreting plasma cells are formed in the secondary lymphoid organs and subsequently home to the bone marrow, although the mechanisms that control this migration remain primarily unknown. In this study, we show that IgG plasma cells constitute a significant fraction of cervical lymph node cells from older mice deficient in both E- and P-selectin (E/P−/−), and that these cells can be prospectively isolated by phenotype. These IgG plasma cells were polyclonal, cytoplasmic Ig+, spontaneously secreted antibody, were in the G0/G1 phase of the cell cycle, and failed to ex

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Xie, Huijuan, Yaw-Chyn Lim, Francis W. Luscinskas, and Andrew H. Lichtman. "Acquisition of Selectin Binding and Peripheral Homing Properties by CD4+ and CD8+ T Cells." Journal of Experimental Medicine 189, no. 11 (1999): 1765–76. http://dx.doi.org/10.1084/jem.189.11.1765.

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Different T cell subsets exhibit distinct capacities to migrate into peripheral sites of inflammation, and this may in part reflect differential expression of homing receptors and chemokine receptors. Using an adoptive transfer approach, we examined the ability of functionally distinct subsets of T cells to home to a peripheral inflammatory site. The data directly demonstrate the inability of naive T cells and the ability of effector cells to home to inflamed peritoneum. Furthermore, interleukin (IL)-12 directs the differentiation of either CD4+ or CD8+ T cells into effector populations that e

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Scalia, Rosario, Valerie E. Armstead, Alexander G. Minchenko, and Allan M. Lefer. "Essential Role of P-Selectin in the Initiation of the Inflammatory Response Induced by Hemorrhage and Reinfusion." Journal of Experimental Medicine 189, no. 6 (1999): 931–38. http://dx.doi.org/10.1084/jem.189.6.931.

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Resuscitation from hemorrhage induces profound pathophysiologic alterations and activates inflammatory cascades able to initiate neutrophil accumulation in a variety of tissues. This process is accompanied by acute organ damage (e.g., lungs and liver). We have previously demonstrated that significant leukocyte–endothelium interactions occur very early in other forms of ischemia/reperfusion (i.e., splanchnic ischemia/reperfusion and traumatic shock) which are largely mediated by increased expression of the adhesion molecule, P-selectin, on the vascular endothelium. Here we postulated that incre

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Lichtenthaler, Stefan F., Diana-ines Dominguez, Gil G. Westmeyer, et al. "The Cell Adhesion Protein P-selectin Glycoprotein Ligand-1 Is a Substrate for the Aspartyl Protease BACE1." Journal of Biological Chemistry 278, no. 49 (2003): 48713–19. http://dx.doi.org/10.1074/jbc.m303861200.

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Guan, Jun, Sundee Dees, Tony Chadderton, and Alejandro Amador Arjona. "Abstract 6373: P-selectin glycoprotein ligand-1 modulates the functions of human T cells and macrophages in vitro." Cancer Research 83, no. 7_Supplement (2023): 6373. http://dx.doi.org/10.1158/1538-7445.am2023-6373.

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Abstract P-selectin glycoprotein ligand-1 (PSGL-1) is a type I transmembrane protein expressed on the surface of most hematopoietic cells. PSGL-1 can engage multiple ligands (e.g., selectins, VISTA, Siglec-5, versican, CCL19, and CCL21). Apart from being a key adhesion molecule involved in immune cell trafficking, PSGL-1 has been shown to function as a negative immune checkpoint receptor in both T cells and macrophages. PSGL-1 is highly expressed in tumor-infiltrating T cells (TILs) and in tumor-associated macrophages (TAMs) in the tumor microenvironment (TME). PSGL-1 signaling in TILs induces

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Mueller, Helena, Mari Tenno, Hugo Van Aken, Jamey D. Marth, Klaus Ley, and Alexander Zarbock. "Severe impairment of leukocyte recruitment into inflamed tissue of ppGalNAcT1-deficient mice (94.1)." Journal of Immunology 182, no. 1_Supplement (2009): 94.1. http://dx.doi.org/10.4049/jimmunol.182.supp.94.1.

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Abstract P-selectin glycoprotein ligand-1 (PSGL-1) plays an important role in leukocyte recruitment. Its binding affinity to selectins is modulated by posttranslational modifications. The polypeptide N-acetylgalactosamine transferase-1 (ppGalNAcT1) initiates core-type protein O-glycosylation. To address whether the glycosylation of PSGL-1 by ppGalNAcT1 is important for leukocyte recruitment, we investigated leukocyte rolling and velocity in untreated and TNF-α treated cremaster muscles and autoperfused flow chambers comparing ppGalNAcT1-/-(Galnt1-/-) with WT mice. In untreated and TNF-α treate

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Kyriakides, Constantinos, William Austen, Yong Wang, et al. "Skeletal muscle reperfusion injury is mediated by neutrophils and the complement membrane attack complex." American Journal of Physiology-Cell Physiology 277, no. 6 (1999): C1263—C1268. http://dx.doi.org/10.1152/ajpcell.1999.277.6.c1263.

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The relative inflammatory roles of neutrophils, selectins, and terminal complement components are investigated in this study of skeletal muscle reperfusion injury. Mice underwent 2 h of hindlimb ischemia followed by 3 h of reperfusion. The role of neutrophils was defined by immunodepletion, which reduced injury by 38%, as did anti-selectin therapy with recombinant soluble P-selectin glycoprotein ligand-immunoglobulin (Ig) fusion protein. Injury in C5-deficient and soluble complement receptor type 1-treated wild-type mice was 48% less than that of untreated wild-type animals. Injury was restore

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Bestebroer, Jovanka, Kok P. M. van Kessel, Hafida Azouagh, et al. "Staphylococcal SSL5 inhibits leukocyte activation by chemokines and anaphylatoxins." Blood 113, no. 2 (2009): 328–37. http://dx.doi.org/10.1182/blood-2008-04-153882.

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Abstract Staphylococcus aureus secretes several virulence factors modulating immune responses. Staphylococcal superantigen-like (SSL) proteins are a family of 14 exotoxins with homology to superantigens, but with generally unknown function. Recently, we showed that SSL5 binds to P-selectin glycoprotein ligand 1 dependently of sialyl Lewis X and inhibits P-selectin–dependent neutrophil rolling. Here, we show that SSL5 potently and specifically inhibits leukocyte activation by anaphylatoxins and all classes of chemokines. SSL5 inhibited calcium mobilization, actin polymerization, and chemotaxis

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Remmler, Jill, Dorothea Zucker-Franklin, and Claire Philipp. "The Effects of MPL-Ligand, Interleukin-6 and Interleukin-11 on Megakaryocyte and Platelet Alpha-granule Proteins." Thrombosis and Haemostasis 80, no. 12 (1998): 968–75. http://dx.doi.org/10.1055/s-0037-1615397.

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SummaryThrombopoietin (Mpl ligand), interleukin-6 (IL-6), and interleukin-11 (IL-11) differ in their effects on megakaryocyte maturation and development. In the present study, the impact of these thrombocytopoietic cytokines on biochemical and structural granule and membrane components was examined. Western blotting was performed on equivalent amounts of isolated megakaryocyte or platelet protein and the relative intensities of the enhanced chemiluminescent-visualized bands were quantitated by densitometry. Megakaryocyte growth and development factor (MGDF), a recombinant thrombopoietin-relate

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Piccardoni, Paola, Rita Sideri, Stefano Manarini, et al. "Platelet/polymorphonuclear leukocyte adhesion: a new role for SRC kinases in Mac-1 adhesive function triggered by P-selectin." Blood 98, no. 1 (2001): 108–16. http://dx.doi.org/10.1182/blood.v98.1.108.

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Abstract Adhesion of polymorphonuclear leukocytes (PMNLs) to activated platelets requires a P-selectin–triggered, tyrosine kinase–dependent adhesiveness of Mac-1 and is accompanied by tyrosine phosphorylation of a 110-kd protein (P-110) in PMNLs. Inhibitors of SRC tyrosine kinases were found to inhibit PMNL adhesion to activated platelets or to P-selectin expressing Chinese hamster ovary (CHO-P) cells and the tyrosine phosphorylation of P-110. Adhesion of PMNLs to activated platelets or to CHO-P cells stimulated activity of LYN and HCK. Monoclonal antibody blockade of P-selectin or β2-integrin

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