P-selectin and E-selectin. Distinct but overlapping leukocyte ligand specificities - PubMed (original) (raw)
. 1992 Jun 5;267(16):11104-10.
Affiliations
- PMID: 1375936
Free article
P-selectin and E-selectin. Distinct but overlapping leukocyte ligand specificities
G R Larsen et al. J Biol Chem. 1992.
Free article
Abstract
P-selectin on platelets and endothelial cells and E-selectin on endothelial cells are leukocyte receptors that recognize lineage-specific carbohydrates on neutrophils and monocytes. The proposed ligands for these receptors contain the Le(x) core and sialic acid. Since other investigators have shown that both E-selectin and P-selectin bind to sialylated Le(x), we evaluated whether E-selectin and P-selectin recognize the same counter-receptor on leukocytes. The interaction of HL60 cells with Chinese hamster ovary (CHO) cells expressing P-selectin or E-selectin was studied. To determine whether a protein component is required in addition to sialyl Le(x) for either P-selectin or E-selectin recognition, HL60 cells or neutrophils were digested with proteases, including chymotrypsin, elastase, proteinase Glu-C, ficin, papain, or thermolysin. Cells treated with these proteases bound E-selectin but not P-selectin. Fucosidase or neuraminidase treatment of HL60 cells markedly decreased binding to both E-selectin- and P-selectin-expressing CHO cells. Growth of HL60 cells in tunicamycin inhibited the ability of these cells to support P-selectin-mediated binding and, to a lesser extent, E-selectin-mediated binding. Purified P-selectin inhibited CHO:P-selectin binding to HL60 cells, but incompletely inhibited CHO:E-selectin binding to HL60 cells. However, purified soluble E-selectin inhibited CHO:P-selectin and CHO:E-selectin binding to HL60 cells equivalently and completely. COS cells, unable to bind to E-selectin or P-selectin, bound E-selectin but not P-selectin upon transfection with alpha-1,3-fucosyltransferase or alpha-1,3/1,4-fucosyltransferase. Similarly, LEC 11 cells expressing sialyl Le(x) bound E-selectin- but not P-selectin-expressing CHO cells. Sambucus nigra lectin, specific for the sialyl-2,6 beta Gal/GalNAc linkage, inhibited P-selectin but not E-selectin binding to HL60 cells. Although sialic acid and Le(x) are components of the P-selectin ligand and the E-selectin ligand, these results indicate that the ligands are related, having overlapping specificities, but are structurally distinct. A protein component containing sialyl Le(x) in proximity to sialyl-2,6 beta Gal structures on the P-selectin ligand may contribute to its specificity for P-selectin.
Similar articles
- Human myeloid alpha 3-fucosyltransferase is involved in the expression of the sialyl-Lewis(x) determinant, a ligand for E- and P-selectin.
Easton EW, Schiphorst WE, van Drunen E, van der Schoot CE, van den Eijnden DH. Easton EW, et al. Blood. 1993 Jun 1;81(11):2978-86. Blood. 1993. PMID: 7684623 - The selectin GMP-140 binds to sialylated, fucosylated lactosaminoglycans on both myeloid and nonmyeloid cells.
Zhou Q, Moore KL, Smith DF, Varki A, McEver RP, Cummings RD. Zhou Q, et al. J Cell Biol. 1991 Oct;115(2):557-64. doi: 10.1083/jcb.115.2.557. J Cell Biol. 1991. PMID: 1717488 Free PMC article. - P-selectin mediates Ca(2+)-dependent adhesion of activated platelets to many different types of leukocytes: detection by flow cytometry.
de Bruijne-Admiraal LG, Modderman PW, Von dem Borne AE, Sonnenberg A. de Bruijne-Admiraal LG, et al. Blood. 1992 Jul 1;80(1):134-42. Blood. 1992. PMID: 1377047 - The selectin family of carbohydrate-binding proteins: structure and importance of carbohydrate ligands for cell adhesion.
Cummings RD, Smith DF. Cummings RD, et al. Bioessays. 1992 Dec;14(12):849-56. doi: 10.1002/bies.950141210. Bioessays. 1992. PMID: 1285423 Review. - Carbohydrate ligands of the LEC cell adhesion molecules.
Brandley BK, Swiedler SJ, Robbins PW. Brandley BK, et al. Cell. 1990 Nov 30;63(5):861-3. doi: 10.1016/0092-8674(90)90487-y. Cell. 1990. PMID: 1701693 Review. No abstract available.
Cited by
- TRAIL in the Treatment of Cancer: From Soluble Cytokine to Nanosystems.
Alizadeh Zeinabad H, Szegezdi E. Alizadeh Zeinabad H, et al. Cancers (Basel). 2022 Oct 19;14(20):5125. doi: 10.3390/cancers14205125. Cancers (Basel). 2022. PMID: 36291908 Free PMC article. Review. - Role of NO and S-nitrosylation in the Expression of Endothelial Adhesion Proteins That Regulate Leukocyte and Tumor Cell Adhesion.
Aguilar G, Koning T, Ehrenfeld P, Sánchez FA. Aguilar G, et al. Front Physiol. 2020 Nov 13;11:595526. doi: 10.3389/fphys.2020.595526. eCollection 2020. Front Physiol. 2020. PMID: 33281627 Free PMC article. Review. - Abnormal Peripheral Neutrophil Transcriptome in Newly Diagnosed Type 2 Diabetes Patients.
Lin Q, Zhou W, Wang Y, Huang J, Hui X, Zhou Z, Xiao Y. Lin Q, et al. J Diabetes Res. 2020 Apr 22;2020:9519072. doi: 10.1155/2020/9519072. eCollection 2020. J Diabetes Res. 2020. PMID: 32377527 Free PMC article. - Biological roles of glycans.
Varki A. Varki A. Glycobiology. 2017 Jan;27(1):3-49. doi: 10.1093/glycob/cww086. Epub 2016 Aug 24. Glycobiology. 2017. PMID: 27558841 Free PMC article. Review. - Glycosphingolipids on Human Myeloid Cells Stabilize E-Selectin-Dependent Rolling in the Multistep Leukocyte Adhesion Cascade.
Mondal N, Stolfa G, Antonopoulos A, Zhu Y, Wang SS, Buffone A Jr, Atilla-Gokcumen GE, Haslam SM, Dell A, Neelamegham S. Mondal N, et al. Arterioscler Thromb Vasc Biol. 2016 Apr;36(4):718-27. doi: 10.1161/ATVBAHA.115.306748. Epub 2016 Feb 11. Arterioscler Thromb Vasc Biol. 2016. PMID: 26868209 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources