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Journal articles on the topic 'Lactosamine'

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Published: 9 March 2023
Last updated: 10 March 2023

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1

Misra, Anup Kumar, Geetanjali Agnihotri, Soni Kamlesh Madhusudan, and Pallavi Tiwari. "Practical Synthesis of Sulfated Analogs of Lactosamine and Sialylated Lactosamine Derivatives." Journal of Carbohydrate Chemistry 23, no. 4 (December 29, 2004): 191–99. http://dx.doi.org/10.1081/car-200030027.

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2

Yan, Fengyang, Seema Mehta, Eva Eichler, Warren W. Wakarchuk, Michel Gilbert, Melissa J. Schur, and Dennis M. Whitfield. "Simplifying Oligosaccharide Synthesis: Efficient Synthesis of Lactosamine and Siaylated Lactosamine Oligosaccharide Donors." Journal of Organic Chemistry 68, no. 6 (March 2003): 2426–31. http://dx.doi.org/10.1021/jo026569v.

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3

MELCHER, Ralph, Alexandra HILLEBRAND, Ute BAHR, Bernd SCHRÖDER, Michael KARAS, and Andrej HASILIK. "Glycosylation-site-selective synthesis of N-acetyl-lactosamine repeats in bis-glycosylated human lysozyme." Biochemical Journal 348, no. 3 (June 7, 2000): 507–15. http://dx.doi.org/10.1042/bj3480507.

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We have studied the elongation of oligosaccharides containing N-acetyl-lactosamine repeats using glycosylated human lysozyme mutants as a model. We reported previously that a combination of glycosylation sites at the 49th (site IV) and 68th (site II) amino acid residues of the protein particularly stimulates the synthesis of N-acetyl-lactosamine repeats [Melcher, Grosch, Grosse and Hasilik (1998) Glycoconjugate J. 15, 987-993]. In the present study we show that it is the carbohydrate attached to site IV that is selectively affected. It contains more N-acetyl-lactosamine repeats when site II is glycosylated in the same molecule. As a corollary of the glycosylation at site II, the synthesis of a third antenna at site IV is increased. The triantennary oligosaccharides at site IV contain more N-acetyl-lactosamine repeats than the biantennary ones. Thus placing a carbohydrate at site II stimulates the branching and the elongation of the carbohydrate at the other site.
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4

Dall'Olio, F., N. Malagolini, G. Di Stefano, M. Ciambella, and F. Serafini-Cessi. "Postnatal development of rat colon epithelial cells is associated with changes in the expression of the β1,4-N-acetylgalactosaminyltransferase involved in the synthesis of Sda antigen of α2,6-sialyltransferase activity towards N-acetyl-lactosamine." Biochemical Journal 270, no. 2 (September 1, 1990): 519–24. http://dx.doi.org/10.1042/bj2700519.

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beta 1,4-N-Acetylgalactosaminyltransferase (beta 1,4GalNAc-transferase) and alpha 2,3-sialyltransferase are both involved in the biosynthesis of the Sda blood group antigen, which is also present in cells of large intestine. The expression of these enzymes and of alpha 2,6-sialyltransferase activity towards N-acetyl-lactosamine was investigated in rat intestinal cells and correlated with both cell differentiation and extent of postnatal maturation. The beta 1,4GalNAc-transferase activity was exclusively found in epithelial cells of the large intestine, preferentially in the proximal segments suggesting a proximal-distal gradient of expression. The beta 1,4GalNAc-transferase and alpha 2,3-sialyltransferase activity towards N-acetyl-lactosamine were expressed in all cell fractions of the colonic crypt, with a maximum activity in the deeply located cells; therefore Sda antigen biosynthesis appears to occur preferentially at a specific stage of cell differentiation. By using N-acetyl-lactosamine as an acceptor, the predominant sialyltransferase in the colon cells was that capable of adding sialic acid in the alpha 2,3- linkage, whereas in the ileum cells the major enzyme was that forming the alpha 2,6-isomer. There were dramatic changes in the expression of colonic beta 1,4GalNac-transferase and of alpha 2,6-sialyltransferase activity towards N-acetyl-lactosamine during postnatal maturation. The former enzyme, practically absent at birth, increased slowly in the first days of life and then rapidly after weaning; by contrast, the latter enzyme was largely expressed only in newborn animals. As the colonic alpha 2,3-sialyltransferase activity towards N-acetyl-lactosamine did not change during the postnatal period, the ratio between the alpha 2,6- and alpha 2,3-sialyltransferase activities was reversed after weaning.
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5

Gyuricza, Barbara, Ágnes Szűcs, Judit P. Szabó, Viktória Arató, Zita Képes, Dániel Szücs, Dezső Szikra, György Trencsényi, and Anikó Fekete. "The Synthesis and Preclinical Investigation of Lactosamine-Based Radiopharmaceuticals for the Detection of Galectin-3-Expressing Melanoma Cells." Pharmaceutics 14, no. 11 (November 18, 2022): 2504. http://dx.doi.org/10.3390/pharmaceutics14112504.

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Given that galectin-3 (Gal-3) is a β-galactoside-binding lectin promoting tumor growth and metastatis, it could be a valuable target for the treatment of Gal-3-expressing neoplasms. An aromatic group introduced to the C-3′ position of lactosamine increased its affinity for Gal-3. Herein, we aimed at developing a radiopharmaceutical for the detection of Gal-3 positive malignancies. To enhance tumor specificity, a heterodimeric radiotracer capable of binding to both Gal-3 and αvβ3 integrin was also synthetized. Arginine-glycine-asparagine (RGD) peptide is the ligand of angiogenesis- and metastasis-associated αvβ3 integrin. Following the synthesis of the chelator-conjugated (2-naphthyl)methylated lactosamine, the obtained compound was applied as a precursor for radiolabeling and was conjugated to the RGD peptide by click reaction as well. Both synthetized precursors were radiolabeled with 68Ga, resulting in high labeling yield (>97). The biological studies were carried out using B16F10 melanoma tumor-bearing C57BL6 mice. High tumor accumulation of both labeled lactosamine derivatives—detected by in vivo PET and ex vivo biodistribution studies—indicated their potential for melanoma detection. However, the heterodimer radiotracer showed high hepatic uptake, while low liver accumulation characterized chelator-conjugated lactosamine, resulting in PET images with excellent contrast. Therefore, this novel carbohydrate-based radiotracer is suitable for the highly selective determination of Gal-3-expressing melanoma cells.
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6

Guardado-Calvo, Pablo, Eva M. Muñoz, Antonio L. Llamas-Saiz, Gavin C. Fox, Richard Kahn, David T. Curiel, Joel N. Glasgow, and Mark J. van Raaij. "Crystallographic Structure of Porcine Adenovirus Type 4 Fiber Head and Galectin Domains." Journal of Virology 84, no. 20 (August 4, 2010): 10558–68. http://dx.doi.org/10.1128/jvi.00997-10.

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ABSTRACT Adenovirus isolate NADC-1, a strain of porcine adenovirus type 4, has a fiber containing an N-terminal virus attachment region, shaft and head domains, and a C-terminal galectin domain connected to the head by an RGD-containing sequence. The crystal structure of the head domain is similar to previously solved adenovirus fiber head domains, but specific residues for binding the coxsackievirus and adenovirus receptor (CAR), CD46, or sialic acid are not conserved. The structure of the galectin domain reveals an interaction interface between its two carbohydrate recognition domains, locating both sugar binding sites face to face. Sequence evidence suggests other tandem-repeat galectins have the same arrangement. We show that the galectin domain binds carbohydrates containing lactose and N-acetyl-lactosamine units, and we present structures of the galectin domain with lactose, N-acetyl-lactosamine, 3-aminopropyl-lacto-N-neotetraose, and 2-aminoethyl-tri(N-acetyl-lactosamine), confirming the domain as a bona fide galectin domain.
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7

Vanmaele, Rosa P., Louis D. Heerze, and Glen D. Armstrong. "Role of Lactosyl Glycan Sequences in Inhibiting Enteropathogenic Escherichia coli Attachment." Infection and Immunity 67, no. 7 (July 1, 1999): 3302–7. http://dx.doi.org/10.1128/iai.67.7.3302-3307.1999.

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ABSTRACT Previously, we found that asialo-lactosamine sequences served as receptors for enteropathogenic Escherichia coli (EPEC) binding to Chinese hamster ovary (CHO) cells. In the present report, we have extended these earlier results by examining the ability of lactosamine- or fucosylated lactosamine-bovine serum albumin (BSA) glycoconjugates to inhibit EPEC, strain E2348/69, binding to HEp-2 cells. We found that, consistent with our previous findings with CHO cells, N-acetyllactosamine-BSA was the most effective inhibitor of EPEC localized adherence to HEp-2 cells, with Lewis X-BSA being the next best inhibitor. Further investigation revealed that coincubating EPEC E2348/69 with these BSA glycoconjugates alone caused a decrease in the expression of the bundle-forming pilus structural subunit (BfpA) and intimin by the bacteria. BfpA and intimin expression were reduced to the greatest extent byN-acetyllactosamine–BSA and Lewis X-BSA, respectively. These results suggest that the glycoconjugate inhibition of EPEC binding to HEp-2 cells might be achieved, wholly or in part, by an active mechanism that is distinct from simple competitive antagonism of receptor-adhesin interactions.
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8

Holschbach, C., J. Schneider, and H. Geyer. "Glycosylation of the envelope glycoprotein gp130 of simian immunodeficiency virus from sooty mangabey (Cercocebus atys)." Biochemical Journal 267, no. 3 (May 1, 1990): 759–66. http://dx.doi.org/10.1042/bj2670759.

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The envelope glycoprotein 130 (‘130’ referring to an Mr of 130,000) of simian immunodeficiency virus from sooty mangabey (Cercocebus atys) (SIVSM) was isolated from the cell-free supernatant of the SIVSM-infected human T-cell line H9, metabolically labelled with D-[6-3H]glucosamine. After digestion with Staphylococcus aureus V8 proteinase, radiolabelled N-glycans were liberated from resulting glycopeptides by sequential treatment with endo-beta-N-acetylglucosaminidase H and peptide:N-glycosidase F and fractionated by h.p.l.c. and gel filtration. Individual oligosaccharide species were characterized by enzymic microsequencing, chromatographic analyses and, in part, by acetolysis. The oligosaccharide structures thus established include oligomannosidic glycans with five to nine mannose residues as well as fucosylated and partially sialylated bi-, tri- and tetra-antennary N-acetyl-lactosaminic oligosaccharide species, the latter of which carry, in part, additional galactose residues or N-acetyl-lactosamine repeats. In comparison with the corresponding envelope glycoprotein 120 from human immunodeficiency virus type 1 (HIV-1), propagated in the same cell line [Geyer, Holschbach, Hunsmann and Schneider (1988) J. Biol. Chem. 263, 11760-11767], carbohydrates of the simian glycoprotein were found to consist of decreased amounts of oligomannosidic glycans and increased quantities of higher-branched N-acetyl-lactosaminic species.
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9

Vierbuchen, M., G. Uhlenbruck, M. Ortmann, G. Dufhues, and R. Fischer. "Occurrence and distribution of glycoconjugates in human tissues as detected by the Erythrina cristagalli lectin." Journal of Histochemistry & Cytochemistry 36, no. 4 (April 1988): 367–76. http://dx.doi.org/10.1177/36.4.3346539.

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We applied a horseradish peroxidase-Erythrina cristagalli agglutinin (HRP-ECA) conjugate for histochemical staining of tissue sections from various formalin-fixed, paraffin-embedded human tissue specimens. The HRP-ECA conjugate showed broad reactivity, but there was a distinct distribution of native (not masked by sialic acid) and sialic acid-masked ECA binding sites in the various organs. Free ECA binding sites could be detected on red blood cells, lymphocytes of thymus, tonsil, lymph node, and in mucous substances of different organs. Independent of blood group type, the vascular endothelium exhibited strong ECA reactivity. Free ECA binding sites occurred in the cytoplasm of Kupffer's cells in liver, in histiocytic cells of thymus, lymph node, tonsil, and in bone marrow. Podocytes of kidney glomerulus, syncytiotrophoblasts of placenta, megakaryocytes in bone marrow, myelin sheath of nerve, medullary thymocytes, and hepatocytes, as well as islet cells of pancreas, contained only sialic acid-capped ECA binding sites. Inhibiting studies with galactose, lactose, and N-acetyl-lactosamine, as well as other sugars, revealed that this lectin is specific for galactosyl residues. In comparison to galactose and lactose, N-acetyl-lactosamine exhibited the highest inhibitory activity on lectin binding, supporting the concept that this lectin is most reactive with N-acetyl-lactosamine-type (type 2 chain) glycoconjugates.
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10

Hara, Yoshihiro, and Kyozo Suyama. "Biosynthesis of lactosamine in bovine mammary gland." Carbohydrate Research 330, no. 1 (January 2001): 65–71. http://dx.doi.org/10.1016/s0008-6215(00)00270-6.

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11

Pospís̆il, M., J. Kubrycht, K. Bezous̆ka, O. Táborský, M. Novák, and J. Kocourek. "Lactosamine type asialooligosaccharide recognition in NK cytotoxicity." Immunology Letters 12, no. 2-3 (March 1986): 83–90. http://dx.doi.org/10.1016/0165-2478(86)90087-8.

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12

Gyuricza, Barbara, Judit P. Szabó, Viktória Arató, Dániel Szücs, Adrienn Vágner, Dezső Szikra, and Anikó Fekete. "Synthesis of Novel, Dual-Targeting 68Ga-NODAGA-LacN-E[c(RGDfK)]2 Glycopeptide as a PET Imaging Agent for Cancer Diagnosis." Pharmaceutics 13, no. 6 (May 26, 2021): 796. http://dx.doi.org/10.3390/pharmaceutics13060796.

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Radiolabeled peptides possessing an Arg-Gly-Asp (RGD) motif are widely used radiopharmaceuticals for PET imaging of tumor angiogenesis due to their high affinity and selectivity to αvβ3 integrin. This receptor is overexpressed in tumor and tumor endothelial cells in the case of numerous cancer cell lines, therefore, it is an excellent biomarker for cancer diagnosis. The galectin-3 protein is also highly expressed in tumor cells and N-acetyllactosamine is a well-established ligand of this receptor. We have developed a synthetic method to prepare a lactosamine-containing radiotracer, namely 68Ga-NODAGA-LacN-E[c(RGDfK)]2, for cancer diagnosis. First, a lactosamine derivative with azido-propyl aglycone was synthetized. Then, NODAGA-NHS was attached to the amino group of this lactosamine derivative. The obtained compound was conjugated to an E[c(RGDfK)]2 peptide with a strain-promoted click reaction. We have accomplished the radiolabeling of the synthetized NODAGA-LacN-E[c(RGDfK)]2 precursor with a positron-emitting 68Ga isotope (radiochemical yield of >95%). The purification of the labeled compound with solid-phase extraction resulted in a radiochemical purity of >99%. Subsequently, the octanol–water partition coefficient (log P) of the labeled complex was determined to be −2.58. In addition, the in vitro stability of 68Ga-NODAGA-LacN-E[c(RGDfK)]2 was investigated and it was found that it was stable under the examined conditions.
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13

Zhi-Guang, W. "Stereocontrolled syntheses of O-glycans of core class 2 with a linear tetrameric lactosamine chain and with three lactosamine branches." Carbohydrate Research 295, no. 1-4 (December 13, 1996): 25–39. http://dx.doi.org/10.1016/s0008-6215(96)00209-1.

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14

Wang, Zhi-Guang, Xu-Fang Zhang, Yukishige Ito, Yoshiaki Nakahara, and Tomoya Ogawa. "Stereocontrolled syntheses of O-glycans of core class 2 with a linear tetrameric lactosamine chain and with three lactosamine branches." Carbohydrate Research 295 (December 1996): 25–39. http://dx.doi.org/10.1016/s0008-6215(96)90116-0.

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15

Habuchi, Osami, Yoshimi Suzuki, and Masakazu Fukuta. "Sulfation of sialyl lactosamine oligosaccharides by chondroitin 6-sulfotransferase." Glycobiology 7, no. 3 (1997): 405–12. http://dx.doi.org/10.1093/glycob/7.3.405.

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16

Eisele, Thomas, Hideharu Ishida, Gerd Hummel, and Richard R. Schmidt. "Synthesis of carbon-bridgedN-acetyl-c-lactosamine and derivatives." Liebigs Annalen 1995, no. 12 (December 1995): 2113–21. http://dx.doi.org/10.1002/jlac.1995199512297.

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17

WANG, Z. G., X. F. ZHANG, Y. ITO, Y. NAKAHARA, and T. OGAWA. "ChemInform Abstract: Stereocontrolled Syntheses of O-Glycans of Core Class 2 with a Linear Tetrameric Lactosamine Chain and with Three Lactosamine Branches." ChemInform 28, no. 17 (August 4, 2010): no. http://dx.doi.org/10.1002/chin.199717203.

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18

Acarin, L., J. M. Vela, B. González, and B. Castellano. "Demonstration of poly-N-acetyl lactosamine residues in ameboid and ramified microglial cells in rat brain by tomato lectin binding." Journal of Histochemistry & Cytochemistry 42, no. 8 (August 1994): 1033–41. http://dx.doi.org/10.1177/42.8.8027523.

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This study was designed to demonstrate the localization of poly-N-acetyl lactosamine residues in postnatal and adult rat brain, visualized by their specific binding to a lectin obtained from Lycopersicon esculentum (tomato). Lectin histochemistry was carried out on cryostat, paraffin, and vibratome sections and was examined by light microscopy. Selected vibratome sections were processed for electron microscopy. Our results showed that tomato lectin histochemistry was found in relation to blood vessels and glial cells in both postnatal and adult rat brain. Since tomato lectin-positive glial cells did not show GFAP immunoreactivity and displayed the same morphological features and overall distribution as nucleoside diphosphatase (NDPase)-positive cells, they were consequently identified as microglial cells. At the electron microscopic level, both ameboid and ramified microglial cells displayed intracytoplasmic and plasma membrane lectin reactivity. In postnatal brain, ameboid microglial cells always showed stronger binding of tomato lectin compared with ramified microglial cells in the adult brain. The putative significance of this decrease in poly-N-acetyl lactosamine from ameboid to ramified microglial cells and the possible role(s) of this sugar residue are discussed.
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19

Hounsell, E. F., J. Feeney, and P. Scudder. "500 MHz 1 H n.m.r. of oligosaccharides of N-acetyl-lactosamine-type released from human erythrocyte glycopeptides by endo-β-galactosidase." Biochemical Journal 250, no. 1 (February 15, 1988): 9–13. http://dx.doi.org/10.1042/bj2500009.

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500 MHz 1H n.m.r. spectroscopy has been used in structural studies of three linear and five branched oligosaccharides of N-acetyl-lactosamine-type that were released from desialylated blood group O erythrocyte glycopeptides by treatment with the endo-beta-galactosidase of Bacteroides fragilis followed by reduction. The following oligosaccharide alditols were characterized: (formula; see book)
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20

Mahanthappa, N. K., D. N. Cooper, S. H. Barondes, and G. A. Schwarting. "Rat olfactory neurons can utilize the endogenous lectin, L-14, in a novel adhesion mechanism." Development 120, no. 6 (June 1, 1994): 1373–84. http://dx.doi.org/10.1242/dev.120.6.1373.

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L-14 is a divalent, lactosamine-binding lectin expressed in many vertebrate tissues. In the rat nervous system, L-14 expression has been observed previously in restricted neuronal subsets within the dorsal root ganglia and spinal cord. In this study we report that L-14 is expressed by nonneuronal cells in the rat olfactory nerve. We demonstrate that L-14 binds and co-localizes with two ligands in the rat olfactory system: a beta-lactosamine-containing glycolipid, and a putative member of the laminin family. The former is expressed on the surfaces of nascent olfactory axons originating from neuron cell bodies in the olfactory epithelium. The latter is present in the extracellular matrix of the axonal path leading to synaptic targets in the olfactory bulb. In vitro, we find that recombinant L-14 promotes primary olfactory neuron adhesion to two laminin family members, and promotes intercellular adhesion. Both activities are dose-dependent, and are independent of integrin-mediated mechanisms. We have thus found that L-14 can serve two distinct adhesive functions in vitro, and propose that L-14 in vivo can promote olfactory axon fasciculation by crosslinking adjacent axons and promote axonal adhesion to the extracellular matrix.
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21

Goso, Y., and K. Hotta. "Types of oligosaccharide sulphation, depending on mucus glycoprotein source, corpus or antral, in rat stomach." Biochemical Journal 264, no. 3 (December 15, 1989): 805–12. http://dx.doi.org/10.1042/bj2640805.

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Radiolabelled mucus glycoprotein was obtained from tissue and a culture medium each of the corpus and antrum of rat stomach incubated with [35S]sulphate in vitro. Gel-filtration analysis of oligosaccharides liberated by alkaline-borohydride treatment from glycoproteins indicated that 35S-labelled oligosaccharides from the corpus vary considerably with respect to chain length whereas those from antral mucus glycoprotein are composed of small oligosaccharides. Examination of the reduced radiolabelled products obtained by HNO2 cleavage of the hydrazine-treated oligosaccharides indicated sulphate esters of N-acetylglucosamine to be present at three locations on a carbohydrate unit: [35S]sulphated monosaccharide (2,5-anhydromannitol 6-sulphate), [35S]sulphated disaccharide [galactosyl(beta 1-4)-2,5-anhydromannitol 6-sulphate] and [35S]sulphated trisaccharide [fucosyl(alpha 1-2)-galactosyl(beta 1-4)-2,5-anhydromannitol 6-sulphate]. Sulphated disaccharide and trisaccharide, possibly originating from the N-acetyl-lactosamine and fucosyl-N-acetyl-lactosamine sequences respectively, were detected in the corpus, especially as large oligosaccharides, but were present in the antrum in only very small amounts. The sulphated monosaccharide, however, most probably originating from 6-sulphated N-acetylglucosamine residues at non-reducing termini, was present in all oligosaccharide fractions in both the corpus and antrum.
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22

Gilbert, C. W., M. H. Zaroukian, and W. J. Esselman. "Poly-N-acetyllactosamine structures on murine cell surface T200 glycoprotein participate in natural killer cell binding to YAC-1 targets." Journal of Immunology 140, no. 8 (April 15, 1988): 2821–28. http://dx.doi.org/10.4049/jimmunol.140.8.2821.

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Abstract Cell-surface murine T200 glycoprotein has been implicated in the binding of NK cells to certain susceptible tumor targets. The existence of poly-N-acetyllactosamine structures on T200 glycoprotein and the ability of lactosamine-type oligosaccharides to inhibit NK cell-mediated cytotoxicity suggest that these structures may also be important in NK-target binding. To further identify and characterize these structures, relevant saccharides and reconstituted membrane liposomes containing fractionated effector cell membrane proteins were tested for their ability to block conjugate formation. Under base line conditions, the majority of plastic-non-adherent, Percoll-fractionated, NK-enriched splenocytes that formed conjugates with NK-susceptible YAC-1 targets functioned as lytic effectors in a single-cell cytotoxicity assay. These effectors were blocked in their ability to bind to YAC-1 targets by the addition of N-acetyllactosamine [Gal(beta 1,4)-GlcNAc] and chitobiose [GlcNAc(beta 1,4)GlcNAc], but not by saccharides lacking lactosamine-type linkages. Liposomes prepared from octyl-beta-D-glucopyranoside-extracted YAC-1 and NK-enriched effector cell membranes interfered with conjugate formation, whereas liposomes prepared from NK-insensitive P815 cells were inconsequential. Surface radiolabeled effector cell membrane proteins were fractionated by tomato lectin-Sepharose 4B (poly-N-acetyllactosamine-specific) column chromatography. Tomato lectin-bound material was enriched in a glycoprotein identical with T200, which, when incorporated into liposomes, was a potent inhibitor of effector-target binding. This inhibitory capacity was abrogated by treatment of liposomes with Ly-5 mAb (T200 mAb) or the lactosamine-specific enzyme endo-beta-galactosidase. When T200 was purified by mAb affinity chromatography and incorporated into liposomes, it was a potent inhibitor of conjugate formation, an effect that was blocked by pretreatment of T200-containing liposomes with Ly-5 mAb or endo-beta-galactosidase. These data provide additional evidence that T200 can mediate binding of NK cells to YAC-1 targets, and that poly-N-acetyllactosamine-type structures on NK cell surface T200 glycoprotein are important in the binding process.
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23

Shan, Yulong, Farah Oulaidi, and Martina Lahmann. "Lactosamine from lactulose via the Heyns rearrangement: a practical protocol." Tetrahedron Letters 54, no. 30 (July 2013): 3960–61. http://dx.doi.org/10.1016/j.tetlet.2013.05.086.

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24

Sasaki, Norihiko, Yoko Itakura, Sadia Mohsin, Tomoaki Ishigami, Hajime Kubo, and Yumi Chiba. "Cell Surface and Functional Features of Cortical Bone Stem Cells." International Journal of Molecular Sciences 22, no. 21 (October 31, 2021): 11849. http://dx.doi.org/10.3390/ijms222111849.

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The newly established mouse cortical-bone-derived stem cells (mCBSCs) are unique stem cells compared to mouse mesenchymal stem cells (mMSCs). The mCBSC-treated hearts after myocardial infarction have been reported to have greater improvement in myocardial structure and functions. In this study, we examined the stemness features, cell surface glycan profiles, and paracrine functions of mCBSCs compared with mMSCs. The stemness analysis revealed that the self-renewing capacity of mCBSCs was greater than mMSCs; however, the differentiation capacity of mCBSCs was limited to the chondrogenic lineage among three types of cells (adipocyte, osteoblast, chondrocyte). The cell surface glycan profiles by lectin array analysis revealed that α2-6sialic acid is expressed at very low levels on the cell surface of mCBSCs compared with that on mMSCs. In contrast, the lactosamine (Galβ1-4GlcNAc) structure, poly lactosamine- or poly N-acetylglucosamine structure, and α2-3sialic acid on both N- and O-glycans were more highly expressed in mCBSCs. Moreover, we found that mCBSCs secrete a greater amount of TGF-β1 compared to mMSCs, and that the TGF-β1 contributed to the self-migration of mCBSCs and activation of fibroblasts. Together, these results suggest that unique characteristics in mCBSCs compared to mMSCs may lead to advanced utility of mCBSCs for cardiac and noncardiac repair.
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25

PINGEL, Sabine, Uta RHEINWEILER, Volker KOLB, and Michael DUSZENKO. "Purification and characterization of an α-galactosyltransferase from Trypanosoma brucei." Biochemical Journal 338, no. 2 (February 22, 1999): 545–51. http://dx.doi.org/10.1042/bj3380545.

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A membrane-associated galactosyltransferase from Trypanosoma brucei was purified 34000-fold by affinity chromatography on UDP-hexanolamine–Sepharose™. Using SDS/PAGE under reducing conditions, the isolated enzyme ran as a relatively broad band with apparent molecular masses of 53 kDa and 52 kDa, indicative of glycosylation and the existence of two isoforms. N-Glycosylation of the enzyme was subsequently confirmed using Western blotting and either specific binding of concanavalin A or peptide-N4-(N-acetylglucosaminyl)asparagine amidase digestion. The de-N-glycosylated enzyme ran with apparent molecular masses of 51 kDa and 50 kDa, indicative of a single N-glycosylation site. The galactosyltransferase exhibited a pH optimum at 7.2 and had a pronounced requirement for Mn2+ ions (KM = 2.5 mM) for its action. The transferase activity was independent of the concentration of Triton X-100. The enzyme was capable of transferring galactose from UDP-galactose to a variety of galactose-based acceptors in α-glycosidic linkages. The apparent KM values for UDP-galactose and for the preferred acceptor substrate N-acetyl-lactosamine are 46 µM and 4.5 mM respectively. From these results we would like to suggest that the galactosyltransferase functions in the processing of terminal N-acetyl-lactosamine structures of trypanosomal glycoproteins.
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26

Asano, Masahide, Susumu Nakae, Norihiro Kotani, Naoki Shirafuji, Aya Nambu, Noriyoshi Hashimoto, Hiroto Kawashima, et al. "Impaired selectin-ligand biosynthesis and reduced inflammatory responses in β-1,4-galactosyltransferase-I–deficient mice." Blood 102, no. 5 (September 1, 2003): 1678–85. http://dx.doi.org/10.1182/blood-2003-03-0836.

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Abstract Selectins recognize ligands containing carbohydrate chains such as sialyl Lewis x (sLex) that are mainly presented at the terminus of N-acetyl lactosamine repeats on core 2 O-glycans. Several glycosyltransferases act successively to extend the N-acetyl lactosamine repeats and to synthesize sLex, and β-1,4-galactosyltransferase (β4GalT) plays a key role in these processes. Recently isolated 6 β4GalT genes are candidates, but their individual roles, including those in selectin-ligand biosynthesis, remain to be elucidated. More than 80% of the core 2 O-glycans on the leukocyte membrane glycoproteins of β4GalT-I–deficient mice lacked galactose residues in β-1,4 linkage, and soluble P-selectin binding to neutrophils and monocytes of these mice was significantly reduced, indicating an impairment of selectin-ligand biosynthesis. β4GalT-I–deficient mice exhibited blood leukocytosis but normal lymphocyte homing to peripheral lymph nodes. Acute and chronic inflammatory responses, including the contact hypersensitivity (CHS) and delayed-type hypersensitivity (DTH) responses, were suppressed, and neutrophil infiltration into inflammatory sites was largely reduced in these mice. Our results demonstrate that β4GalT-I is a major galactosyltransferase responsible for selectin-ligand biosynthesis and that inflammatory responses of β4GalT-I–deficient mice are impaired because of the defect in selectin-ligand biosynthesis.
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27

Ferens-Sieczkowska, M., M. Orczyk-Pawiłowicz, and B. Morawiecka. "The N-acetylgalactosamine and lactosamine specific lectin from Iris hybrida leaves." Acta Biochimica Polonica 44, no. 2 (June 30, 1997): 301–7. http://dx.doi.org/10.18388/abp.1997_4425.

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The lectin isolated from the leaves of Iris hybrida binds specifically N-acetyl-galactosamine and lactose. Its molecule consists of two identical subunits bound by disulfide bonds. The lectin is a glycoprotein containing about 12% of sugars. It binds asialoglycoproteins containing complex type sugar chains. The binding is reduced by half at the concentration of 0.15 to 0.40 mM of the galactose containing disaccharides irrespectively to a type of galactose isomer. This indicates rather broad specificity of I. hybrida leaf lectin.
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28

Ágoston, Károly, Gyula Dékány, István Bajza, and Markus Hederos. "Synthesis of lactosamine from lactulose: scalable approach for the Heyns rearrangement." Tetrahedron Letters 57, no. 24 (June 2016): 2595–97. http://dx.doi.org/10.1016/j.tetlet.2016.04.119.

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29

Lattová, Erika, and Ladislav Petruš. "Synthesis of N-acetyl-lactosamine via ozonolysis of a nitro derivative." Carbohydrate Research 235 (November 1992): 289–93. http://dx.doi.org/10.1016/0008-6215(92)80097-k.

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30

Takayama, Shuichi, Makoto Shimazaki, Lei Qiao, and Chi-Huey Wong. "Synthesis of lactosamine derivatives using β-d-galactosidase from Bacillus circulans." Bioorganic & Medicinal Chemistry Letters 6, no. 10 (May 1996): 1123–26. http://dx.doi.org/10.1016/0960-894x(96)00184-9.

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31

Böttcher, Stephan, and Joachim Thiem. "Facile preparation of indoxyl- and nitrophenyl glycosides of lactosamine and isolactosamine." RSC Advances 4, no. 21 (2014): 10856. http://dx.doi.org/10.1039/c3ra47128d.

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32

Schwarting, Gerald A., and Timothy R. Henion. "Lactosamine differentially affects olfactory sensory neuron projections to the olfactory bulb." Developmental Neurobiology 67, no. 12 (2007): 1627–40. http://dx.doi.org/10.1002/dneu.20536.

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33

SHARMA, Shalini, Satish BHARADWAJ, Avadhesha SUROLIA, and Sunil Kumar PODDER. "Evaluation of the stoichiometry and energetics of carbohydrate binding to Ricinus communis agglutinin: a calorimetric study." Biochemical Journal 333, no. 3 (August 1, 1998): 539–42. http://dx.doi.org/10.1042/bj3330539.

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High-sensitivity isothermal titration calorimetry has been used to investigate the thermodynamics of binding of Ricinus communis agglutinin to galactose, lactose and their derivatives in the temperature range 280.5–298 K. The present study unequivocally establishes the carbohydrate-binding stoichiometry of the tetrameric agglutinin from castor bean as two, i.e. the (As–sB)2-type tetramer of the agglutinin has two equivalent sites that are non-interacting and independent. The site binding constants range from 2.2×103 M-1 at 282 K for galactose to 4.84×104 M-1 at 281 K for N-acetyl-lactosamine. The binding enthalpies range from -21.9 kJ·mol-1 at 293 K for 4-methylumbelliferyl-β-galactoside to -50.2 kJ·mol-1 at 292.9 K for thiodigalactoside. The observation of limited entropy–enthalpy compensation for binding of the sugars to the lectin indicates that reorganization of water molecules plays an important role in binding. As the slope of the compensation plot is greater than unity, the reactions are largely enthalpically driven. These studies show that the stronger binding of N-acetyl-lactosamine than lactose is due to a favourable interaction between the acetamido group of the reducing-end N-acetylglucosamine of the former and the corresponding loci in the agglutinin molecule. Preferential binding of methyl-β-galactoside over methyl-α-galactoside also indicates the apolar nature of the interaction with the methyl group of the former sugar.
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34

Cockin, G. H., T. N. Huckerby, and I. A. Nieduszynski. "High-field n.m.r. studies of keratan sulphates. 1H and 13C assignments of keratan sulphate from shark cartilage." Biochemical Journal 236, no. 3 (June 15, 1986): 921–24. http://dx.doi.org/10.1042/bj2360921.

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Keratan sulphate was extracted from a shark/whale cartilage preparation and examined by 400 MHz 1H- and 100 MHz 13C-n.m.r. spectroscopy. Assignment of the majority of the resonances was facilitated by two-dimensional 13C-1H correlation by using a modified COLOC procedure and a COSY-45 experiment. The spectra are consistent with an N-acetyl-lactosamine repeating unit that is predominantly sulphated at C-6 of both galactose and N-acetylglucosamine. Gel chromatography of a keratanase digest of the shark keratan sulphate confirmed the high degree of galactose sulphation.
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35

Bless, Elizabeth, Denitza Raitcheva, Timothy R. Henion, Stuart Tobet, and Gerald A. Schwarting. "Lactosamine modulates the rate of migration of GnRH neurons during mouse development." European Journal of Neuroscience 24, no. 3 (August 2006): 654–60. http://dx.doi.org/10.1111/j.1460-9568.2006.04955.x.

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36

Sherman, Andrei A., Olga N. Yudina, Alexander S. Shashkov, Vladimir M. Menshov, and Nikolay E. Nifant'ev. "Synthesis of Neu5Ac- and Neu5Gc-α-(2→6′)-lactosamine 3-aminopropyl glycosides." Carbohydrate Research 330, no. 4 (February 2001): 445–58. http://dx.doi.org/10.1016/s0008-6215(01)00002-7.

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37

Machado, Sergio A., Kadirvel Govindasamy, Claudia Korneli, Emily Collins, Paul Miller, Kelsey N. Bess, and David J. Miller. "Porcine Sperm Bind to Specific Sialylated Lactosamine-Containing Glycans in the Oviduct." Biology of Reproduction 85, Suppl_1 (July 1, 2011): 528. http://dx.doi.org/10.1093/biolreprod/85.s1.528.

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38

EISELE, T., H. ISHIDA, G. HUMMEL, and R. R. SCHMIDT. "ChemInform Abstract: Synthesis of Carbon-Bridged N-Acetyl-C-lactosamine and Derivatives." ChemInform 27, no. 14 (August 12, 2010): no. http://dx.doi.org/10.1002/chin.199614238.

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39

Klisch, K., A. Boos, M. Friedrich, K. Herzog, M. Feldmann, NM Sousa, JF Beckers, R. Leiser, and G. Schuler. "The glycosylation of pregnancy-associated glycoproteins and prolactin-related protein-I in bovine binucleate trophoblast giant cells changes before parturition." Reproduction 132, no. 5 (November 2006): 791–98. http://dx.doi.org/10.1530/rep-06-0040.

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Binucleate trophoblast giant cells (BNC) in the bovine placenta produce glycoproteins, which are delivered into the mother after fusion of BNC with uterine epithelial cells. During most time of pregnancy, BNC produce pregnancy-associated glycoproteins (PAGs) and prolactin-related protein-I (PRP-I) with asparagine-linked lactosamine-type glycans terminating withN-acetyl-galactosamine. We show by lectin histochemistry that terminalN-acetyl-galactosamine (detected byDolichos biflorusagglutinin, DBA) in placentomal BNC is greatly reduced prior to parturition, while lactosamine-typeN-glycans (detected byPhaseolus vulgarisleucoagglutinin, PHA-L) remain unaltered. The change in DBA-staining showed no statistically significant differences between placentomes of cows with and without retention of fetal membranes. Western blots revealed that, at parturition the apparent molecular mass of PAGs and PRP-I is 1–2 kDa lower than in late pregnancy. These changes are due to alterations of asparagine-linked glycans, since the molecular weight of the peptide backbones after enzymatical release of asparagine-linked glycans is identical at late pregnancy and parturition. Lectin western blots showed a reduction of terminalN-acetyl-galactosamine on PAGs at parturition. A lectin sandwich-ELISAwas used to differentiate DBA- and PHA-L-binding PAGs in sera of pregnant and non-pregnant cows. The values for DBA-binding PAGs at parturition were not significantly different from non-pregnancy, while the values for PHA-L-binding PAGs were significantly higher at parturition. The peripartal changes of PAG- and PRP-I-glycosylation could alter functional properties of these proteins and might therefore be considered for functional studies. The differentiation of PAG glycoforms in maternal serum could be valuable for a further optimization of PAG-based pregnancy diagnosis in cattle.
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40

Ramkumar, R., A. Surolia, and S. K. Podder. "Energetics of carbohydrate binding by a 14 kDa S-type mammalian lectin." Biochemical Journal 308, no. 1 (May 15, 1995): 237–41. http://dx.doi.org/10.1042/bj3080237.

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The thermodynamics of the binding of derivatives of galactose and lactose to a 14 kDa beta-galactoside-binding lectin (L-14) from sheep spleen has been studied in 10 nM phosphate/150 mM NaCl/10 mM beta-mercaptoethanol buffer, pH 7.4, and in the temperature range 285-300 K using titration calorimetry. The single-site binding constants of various sugars for the lectin were in the following order: N-acetyl-lactosamine thiodigalactoside > 4-methylumbelliferyl lactoside > lactose > 4-methylumbelliferyl alpha-D-galactoside > methyl-alpha-galactose > methyl-beta-galactose. Reactions were essentially enthalpically driven with the binding enthalpies ranging from -53.8 kJ/mol for thiodigalactoside at 301 K to -2.2 kJ/mol for galactose at 300 K, indicating that hydrogen-bonding and van der Waals interactions provide the major stabilization for these reactions. However, the binding of 4-methylumbelliferyl-alpha-D-galactose displays relatively favourable entropic contributions, indicating the existence of a non-polar site adjacent to the galactose-binding subsite. From the increments in the enthalpies for the binding of lactose, N-acetyl-lactosamine and thiodigalactoside relative to methyl-beta-galactose, the contribution of glucose binding in the subsite adjacent to that for galactose shows that glucose makes a major contribution to the stability of L-14 disaccharide complexes. Observation of enthalpy-entropy compensation for the recognition of saccharides such as lactose by L-14 and the absence of it for monosaccharides such as galactose, together with the lack of appreciable changes in the heat capacity (delta Cp), indicate that reorganization of water plays an important role in these reactions.
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41

FLEMING, S., and G. BROWN. "The expression of 3-fucosylated-N-acetyl lactosamine carbohydrate determinants in renal tumours." Histopathology 11, no. 2 (February 1987): 171–82. http://dx.doi.org/10.1111/j.1365-2559.1987.tb02620.x.

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42

Loka, Ravi S., Christopher M. Sadek, Nikolas A. Romaniuk, and Christopher W. Cairo. "Conjugation of SyntheticN-Acetyl-Lactosamine to Azide-Containing Proteins Using the Staudinger Ligation." Bioconjugate Chemistry 21, no. 10 (October 20, 2010): 1842–49. http://dx.doi.org/10.1021/bc100209r.

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43

Kobayashi, Kazukiyo, Naohito Kakishita, Masahiko Okada, Toshihiro Akaike, and Taichi Usui. "Chemo-Enzymatic Synthesis of a Glycopolymer Carrying Clustered-N-ACETYL-β-lactosamine Moieties." Journal of Carbohydrate Chemistry 13, no. 5 (July 1994): 753–66. http://dx.doi.org/10.1080/07328309408011678.

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44

TAKAYAMA, S., M. SHIMAZAKI, L. QIAO, and C. H. WONG. "ChemInform Abstract: Synthesis of Lactosamine Derivatives Using β-D-Galactosidase from Bacillus circulans." ChemInform 27, no. 37 (August 5, 2010): no. http://dx.doi.org/10.1002/chin.199637285.

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45

Tai, G. H., G. M. Brown, H. G. Morris, T. N. Huckerby, and I. A. Nieduszynski. "Fucose content of keratan sulphates from bovine articular cartilage." Biochemical Journal 273, no. 2 (January 15, 1991): 307–10. http://dx.doi.org/10.1042/bj2730307.

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Alkaline-borohydride-reduced keratan sulphate chains were isolated from bovine articular cartilage (6-8-year-old animals). Nine keratan sulphate fractions of increasing molecular weight were prepared by gel-permeation chromatography on a calibrated column of TSK 30 XL. The samples were analysed for fucose and galactose contents (% by wt. of keratan sulphate) and fucose/galactose ratio. The fucose content increased with molecular size, but the galactose content remained constant. It was concluded that the alpha(1→3)-linked fucose [Thornton, Morris, Cockin, Huckerby, Nieduszynski, Carlstedt, Hardingham & Ratcliffe (1989) Biochem. J. 260, 277-282] was located within the poly-N-acetyl-lactosamine repeat sequence of articular-cartilage keratan sulphate.
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46

Vivier, E., J. M. Sorrell, M. Ackerly, M. J. Robertson, R. A. Rasmussen, H. Levine, and P. Anderson. "Developmental regulation of a mucinlike glycoprotein selectively expressed on natural killer cells." Journal of Experimental Medicine 178, no. 6 (December 1, 1993): 2023–33. http://dx.doi.org/10.1084/jem.178.6.2023.

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Natural killer (NK) cells are CD3:TCR-, CD16+, CD56+ large granular lymphocytes capable of recognizing and eliminating a variety of virus-infected, malignant, and antibody-coated target cells. Two functionally distinct populations of peripheral blood NK cells can be differentiated by their surface expression of an isoform of the neural cell adhesion molecule (CD56). CD56bright NK cells have the attributes of an undifferentiated cell, in that they proliferate in response to exogenous cytokines, but exert poor cytolytic activity. CD56dim NK cells have the attributes of a more differentiated cell, in that they proliferate poorly in response to exogenous cytokines, but are potent cytolytic effector cells. Here we describe the molecular characterization of a NK cell restricted epitope (PEN5) that is selectively expressed on the functionally differentiated CD56dim NK cells. PEN5+ NK cells proliferate poorly in response to interleukin 2 (IL-2), but are potent cytolytic effectors, whereas PEN5- NK cells proliferate in response to IL-2, but are poor cytolytic effectors. Biochemical and immunochemical analyses reveal the PEN5 epitope to be an unusual sulfated poly-N-lactosamine carbohydrate related to keratan sulfate glycosaminoglycans. Immunoprecipitates prepared using a monoclonal antibody reactive with PEN5 include two polydisperse membrane-bound glycoproteins, PEN5 alpha (120-170 kD) and PEN5 beta (210-245 kD). Enzymatic deglycosylation reduces the apparent molecular weight of both PEN5 isoforms by 80-90%, and classifies PEN5 beta as a mucinlike glycoprotein. The surface expression of the PEN5 epitope is downmodulated by stimuli that induce NK cell proliferation, and it is absent from leukemic NK cells of patients with granular lymphocyte proliferative disorder. Taken together, these results indicate that PEN5 is a developmentally regulated poly-N-lactosamine epitope associated with a mucin-type glycoprotein, whose expression is restricted to the population of nonproliferative NK cells fully committed to cytolytic effector function.
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47

Overdijk, B., E. P. Beem, G. J. van Steijn, L. A. Trippelvitz, J. J. Lisman, J. Paz Parente, P. Cardon, Y. Leroy, B. Fournet, and H. van Halbeek. "Structural analysis of the carbohydrate chains of β-N-acetylhexosaminidases from bovine brain." Biochemical Journal 232, no. 3 (December 15, 1985): 637–41. http://dx.doi.org/10.1042/bj2320637.

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The oligosaccharide structures of bovine brain beta-N-acetylhexosaminidases A and B (EC 3.2.1.30) were studied at the glycopeptide level by employing 500 MHz 1H-n.m.r. spectroscopy and methylation analysis involving g.l.c.-m.s. More than 90% of the chains were found to be of the oligomannoside type, containing, on average, five to six mannose residues. Biantennary N-acetyl-lactosamine-type chains terminated in N-acetylneuraminic acid were found to comprise the remaining 5-10% of the total carbohydrate. The isoenzyme forms A and B do not differ from each other in the structure of their carbohydrate moiety, but do deviate in carbohydrate content and, in consequence, in the number of carbohydrate chains per molecule.
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48

Kaji, Eisuke, Yumiko Osa, Naomi Shinohara, Chiho Yanagi, Masae Sekine, and Takashi Nishino. "Alternative Access to Lactosamine-derived Oxazoline via 2-Ulose Oxime as a Key Intermediate." HETEROCYCLES 64, no. 1 (2004): 317. http://dx.doi.org/10.3987/com-04-s(p)28.

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49

MELCHER, Ralph, Alexandra HILLEBRAND, Ute BAHR, Bernd SCHRÖDER, Michael KARAS, and Andrej HASILIK. "Glycosylation-site-selective synthesis of N-acetyl-lactosamine repeats in bis-glycosylated human lysozyme." Biochemical Journal 348, no. 3 (June 15, 2000): 507. http://dx.doi.org/10.1042/0264-6021:3480507.

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50

Sumiyoshi, Wataru, Shin-ichi Nakakita, Nobumitsu Miyanishi, Keita Yamada, Kayo Hasehira, Yukari Nakakita, and Jun Hirabayashi. "Hypersialylated type-I lactosamine-containing N-glycans found in Artiodactyla sera are potential xenoantigens." Glycobiology 22, no. 8 (April 4, 2012): 1031–41. http://dx.doi.org/10.1093/glycob/cws069.

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