Endothelial-selectin ligands sialyl Lewisx and sialyl Lewisa are differentiation antigens immunogenic in human melanoma

Cancer ◽  
1997 ◽  
Vol 79 (9) ◽  
pp. 1686-1697 ◽  
Author(s):  
Mepur H. Ravindranath ◽  
Amir A. Amiri ◽  
Philip M. Bauer ◽  
Mark C. Kelley ◽  
Richard Essner ◽  
...  
Keyword(s):  
Human Melanoma ◽  
Sialyl Lewisx ◽  
Differentiation Antigens ◽  
Selectin Ligands ◽  
Sialyl Lewisa

scholarly journals Targeting Selectins Mediated Biological Activities With Multivalent Probes

2021 ◽  
Vol 9 ◽  
Author(s):  
Deepak Ganesh ◽  
Prashant Jain ◽  
Chethan Devanur Shanthamurthy ◽  
Suraj Toraskar ◽  
Raghavendra Kikkeri
Keyword(s):  
Tumor Metastasis ◽  
Inflammatory Diseases ◽  
Biological Activities ◽  
Type I ◽  
Blood Capillaries ◽  
Activated Platelets ◽  
Selectin Ligands ◽  
Different Types ◽  
Selectin Binding ◽  
Sialyl Lewisa

Selectins are type-I transmembrane glycoproteins that are ubiquitously expressed on activated platelets, endothelial cells, and leukocytes. They bind to cell surface glycoproteins and extracellular matrix ligands, regulate the rolling of leukocytes in the blood capillaries, and recruit them to inflammatory sites. Hence, they are potential markers for the early detection and inhibition of inflammatory diseases, thrombosis, cardiovascular disorders, and tumor metastasis. Fucosylated and sialylated glycans, such as sialyl Lewisx, its isoform sialyl Lewisa, and heparan sulfate, are primary selectin ligands. Functionalization of these selectin-binding ligands on multivalent probes, such as nanoparticles, liposomes, and polymers, not only inhibits selectin-mediated biological activity but is also involved in direct imaging of the inflammation site. This review briefly summarizes the selectin-mediated various diseases such as thrombosis, cancer and recent progress in the different types of multivalent probes used to target selectins.

Substrate specificity of fucosyl transferase III: An efficient synthesis of sialyl Lewisx-, sialyl Lewisa-derivatives and mimetics thereof

2000 ◽  
Vol 78 (6) ◽  
pp. 892-904 ◽  
Author(s):  
Beat Ernst ◽  
Bea Wagner ◽  
Gabi Baisch ◽  
Andreas Katopodis ◽  
Tammo Winkler ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Enzymatic Synthesis ◽  
Reaction Rates ◽  
Efficient Synthesis ◽  
Natural Substrate ◽  
Sialyl Lewisx ◽  
Sialyl Lewis ◽  
Sialyl Lewisa

Fucosyl transferase III (FucT III) has previously been characterized as the most general enzyme of the FucT family, as judged from its ability to catalyze the transfer of fucose to both Galβ(1-3)GlcNAc and Galβ(1-4)GlcNAc. In order to explore the synthetic potential of FucT III for the enzymatic synthesis of sialyl Lewisx and sialyl Lewisa derivatives, its substrate specificity has been probed using a number of natural substrate mimetics. A remarkable range of acceptor substrates was found when N-acetyl glucosamine was replaced by D-glucal, (R,R)-1,2-cyclohexanediol and (R,R)-butan-2,3-diol. Although the reaction rates were low compared to the reaction with the natural substrates, they proved to be sufficient for the synthesis of preparative amounts.Key words: fucosyl transferase III, sialyl Lewisa, sialyl Lewisx, carbohydrate mimetics.

scholarly journals L-Selectin Ligands That Are O-glycoprotease Resistant and Distinct from MECA-79 Antigen are Sufficient for Tethering and Rolling of Lymphocytes on Human High Endothelial Venules

1998 ◽  
Vol 140 (3) ◽  
pp. 721-731 ◽  
Author(s):  
Rachael A. Clark ◽  
Robert C. Fuhlbrigge ◽  
Timothy A. Springer
Keyword(s):  
In Vitro Assay ◽  
Lymphoid Tissues ◽  
Sialyl Lewisx ◽  
High Endothelial Venules ◽  
Vitro Assay ◽  
Tissue Sections ◽  
High Affinity ◽  
Selectin Ligands ◽  
Carbohydrate Ligands

During the process of lymphocyte recirculation, lymphocytes bind via L-selectin to sulfated sialyl-Lewisx (sLex)–containing carbohydrate ligands expressed on the surface of high endothelial venules (HEV). We have examined the expression of sLex on HEV using a panel of mAbs specific for sLex and sLex-related structures, and have examined the function of different sLex-bearing structures using an in vitro assay of lymphocyte rolling on HEV. We report that three sLex mAbs, 2F3, 2H5, and CSLEX-1, previously noted to bind with high affinity to glycolipid-linked sLex, vary in their ability to stain HEV in different lymphoid tissues and bind differentially to O-linked versus N-linked sLex on glycoproteins. Treatment of tissue sections with neuraminidase abolished staining with all three mAbs but slightly increased staining with MECA-79, a mAb to a sulfation-dependent HEV-associated carbohydrate determinant. Treatment of tissue sections with O-sialoglycoprotease under conditions that removed the vast majority of MECA-79 staining, only partially reduced staining with the 2F3 and 2H5 mAbs. Using a novel rolling assay in which cells bind under flow to HEV of frozen tissue sections, we demonstrate that a pool of O-sialoglycoprotease–resistant molecules is present on HEV that is sufficient for attachment and rolling of lymphocytes via L-selectin. This interaction is not inhibited by the mAb MECA-79. Furthermore, MECA-79 mAb blocks binding to untreated sections by only 30%, whereas the sLex mAb 2H5 blocks binding by ∼60% and a combination of MECA-79 and 2H5 mAb blocks binding by 75%. We conclude that a pool of O-glycoprotease-resistant sLex-like L-selectin ligands exist on human HEV that is distinct from the mucin-associated moieties recognized by MECA-79 mAb. We postulate that these ligands may participate in lymphocyte binding to HEV.

Selectin ligands on human melanoma cells

1996 ◽  
Vol 13 (1) ◽  
pp. 33-43 ◽  
Author(s):  
Nicholas Miller ◽  
Richard G. Vile ◽  
Ian R. Hart
Keyword(s):  
Melanoma Cells ◽  
Human Melanoma ◽  
Human Melanoma Cells ◽  
Selectin Ligands

Comparative evaluation of the prognostic value of MUC1, MUC2, sialyl-Lewisa and sialyl-Lewisx antigens in colorectal adenocarcinoma

2002 ◽  
Vol 40 (5) ◽  
pp. 440-449 ◽  
Author(s):  
S E Baldus ◽  
S P Monig ◽  
F-G Hanisch ◽  
T K Zirbes ◽  
U Flucke ◽  
...  
Keyword(s):  
Comparative Evaluation ◽  
Prognostic Value ◽  
Colorectal Adenocarcinoma ◽  
Sialyl Lewisx ◽  
Sialyl Lewisa

scholarly journals Anti–Sia-lb (Anti-Gd) Cold Agglutinins Bind the Domain NeuNAcα2-3Gal in Sialyl Lewisx, Sialyl Lewisa, and Related Carbohydrates on Nucleated Cells and in Soluble Cancer-Associated Mucins

Blood ◽  
1997 ◽  
Vol 90 (4) ◽  
pp. 1576-1587
Author(s):  
Teresa Gallart ◽  
Dieter Roelcke ◽  
Maite Blay ◽  
Arturo Pereira ◽  
Antonio Martı́nez ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Red Blood Cells ◽  
Adhesion Molecules ◽  
Blood Cells ◽  
Malignant Cells ◽  
Sialyl Lewisx ◽  
Cold Agglutinins ◽  
Activity Inhibition ◽  
Carbohydrate Ligands ◽  
Sialyl Lewisa

Anti–Sia-lb (formerly anti-Gd) cold agglutinins (CAs) recognize sialylated carbohydrates on both adult and neonate red blood cells (RBCs). RBC CA activity inhibition experiments reported here indicate that the domain NeuNAcα2-3Gal, as found in sialyllactose, synthetic sialyl(s) Lewis(Le)x and sLea, sialyllactosamine, sialyl-fucosyllactose, and nonfucosylated sLea, constitutes the minimal epitope for these CAs, implicating that these autoantibodies could be able to bind this domain in sLex and sLea and related carbohydrates expressed on nucleated cells and in soluble cancer-related mucins. The following data obtained with the previously characterized monoclonal IgMk anti-Sia-lb CA, GAS, show that this is the case. GAS epitope expression among leukocytes that lack sLea parallels that of sLex determinant as detected by mouse monoclonal antibodies (MoAbs), especially MoAb KM-93. It is also found on epithelial malignant cells bearing both sLex and sLea. GAS epitope on these nucleated cells, (1) like that present on RBC, is abolished by sialidase, unaffected by proteases, and inhibited by sialyllactose; and (2) is overlapping and/or proximal to that recognized by anti-sLex MoAb, CSLEX-1, and KM-93. Moreover, CAGAS binds soluble cancer-associated mucins bearing sLex and sLea determinants. This binding is inhibited by sialyllactose and these mucins inhibit the RBC CA activity of CAGAS. The possible significance of anti–Sia-lb (anti-Gd) CAs as autoantibodies directed to carbohydrate ligands of host adhesion molecules that might be receptors of microbial adhesins of some CA-inducing pathogens is discussed.

Difference in Prognostic Value Between Sialyl Lewisa and Sialyl Lewisx Antigen Levels in the Preoperative Serum of Gastric Cancer Patients

2002 ◽  
Vol 34 (4) ◽  
pp. 408-415 ◽  
Author(s):  
Tohru Nakagoe ◽  
Terumitsu Sawai ◽  
Takashi Tsuji ◽  
Masa-aki Jibiki ◽  
Atsushi Nanashima ◽  
...  
Keyword(s):  
Gastric Cancer ◽  
Cancer Patients ◽  
Prognostic Value ◽  
Sialyl Lewisx ◽  
Preoperative Serum ◽  
Gastric Cancer Patients ◽  
Sialyl Lewisa

scholarly journals Anti–Sia-lb (Anti-Gd) Cold Agglutinins Bind the Domain NeuNAcα2-3Gal in Sialyl Lewisx, Sialyl Lewisa, and Related Carbohydrates on Nucleated Cells and in Soluble Cancer-Associated Mucins

Blood ◽  
1997 ◽  
Vol 90 (4) ◽  
pp. 1576-1587 ◽  
Author(s):  
Teresa Gallart ◽  
Dieter Roelcke ◽  
Maite Blay ◽  
Arturo Pereira ◽  
Antonio Martı́nez ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Red Blood Cells ◽  
Adhesion Molecules ◽  
Blood Cells ◽  
Malignant Cells ◽  
Sialyl Lewisx ◽  
Cold Agglutinins ◽  
Activity Inhibition ◽  
Carbohydrate Ligands ◽  
Sialyl Lewisa

Abstract Anti–Sia-lb (formerly anti-Gd) cold agglutinins (CAs) recognize sialylated carbohydrates on both adult and neonate red blood cells (RBCs). RBC CA activity inhibition experiments reported here indicate that the domain NeuNAcα2-3Gal, as found in sialyllactose, synthetic sialyl(s) Lewis(Le)x and sLea, sialyllactosamine, sialyl-fucosyllactose, and nonfucosylated sLea, constitutes the minimal epitope for these CAs, implicating that these autoantibodies could be able to bind this domain in sLex and sLea and related carbohydrates expressed on nucleated cells and in soluble cancer-related mucins. The following data obtained with the previously characterized monoclonal IgMk anti-Sia-lb CA, GAS, show that this is the case. GAS epitope expression among leukocytes that lack sLea parallels that of sLex determinant as detected by mouse monoclonal antibodies (MoAbs), especially MoAb KM-93. It is also found on epithelial malignant cells bearing both sLex and sLea. GAS epitope on these nucleated cells, (1) like that present on RBC, is abolished by sialidase, unaffected by proteases, and inhibited by sialyllactose; and (2) is overlapping and/or proximal to that recognized by anti-sLex MoAb, CSLEX-1, and KM-93. Moreover, CAGAS binds soluble cancer-associated mucins bearing sLex and sLea determinants. This binding is inhibited by sialyllactose and these mucins inhibit the RBC CA activity of CAGAS. The possible significance of anti–Sia-lb (anti-Gd) CAs as autoantibodies directed to carbohydrate ligands of host adhesion molecules that might be receptors of microbial adhesins of some CA-inducing pathogens is discussed.

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