The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
A carbohydrate domain common to both sialyl Le(a) and sialyl Le(X) is recognized by the endothelial cell leukocyte adhesion molecule ELAM-1
Open accessAbstract
The specificity of endothelial cell leukocyte adhesion molecule-1, ELAM-1, for binding to a panel of carbohydrate structures was determined by a sensitive cell binding assay with immobilized synthetic glycoconjugates. ELAM-1 cDNA transfectants were found to bind Sialyl Lea (sialylated lacto-N-fucopentaose II) or sialylated Lewis a antigen (NeuAc alpha 2-3Gal beta 1-3(Fuc alpha 1-4)GlcNAc), as well as or slightly better than Sialyl Lex (sialylated lacto-N-fucopentaose III) or sialylated Lewis X antigen (NeuAc alpha 2-3 Gal beta 1-4(Fuc alpha 1-3)GlcNAc). A monoclonal antibody, HECA-452, which has been identified recently as recognizing ELAM-1 ligands in addition to those containing Sialyl Lex, was also found to bind both Sialyl Lex and Sialyl Lea. Hard sphere exo-anomeric (HSEA) calculations were performed on these two hexasaccharides. The conformations indicate that Sialyl Lea and Sialyl Lex show a high degree of similarity in both the nonreducing and reducing termini. As Lea and Lex show much weaker reactivity, the determinants recognized by ELAM-1 and HECA-452 probably involve neuraminic acid and fucose residues which on one face of both Sialyl Lex and Sialyl Lea can be similarly positioned. The finding that Sialyl Lea is a potent ligand for ELAM-1 is important, as circulating Sialyl Lea and Sialyl Lex containing mucins which are elevated in the serum of many cancer patients may block leukocyte interactions with ELAM-1 and may contribute to the pathological immunodepression observed in these patients.
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Cites
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Self-citationELAM-1 Mediates Cell Adhesion by Recognition of a Carbohydrate Ligand, Sialyl-Le x
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Cited by
Varki, A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.16.7390 · Cited by 946
Mechanisms That Regulate the Function of the Selectins and Their Ligands
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Guvench, O., Mallajosyula, S. S., Raman, E. P., Hatcher, E., Vanommeslaeghe, K., Foster, T. J., Jamison, F. W., & MacKerell, A. D. (2011) · Journal of Chemical Theory and Computation · doi:10.1021/ct200328p · Cited by 699
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Metadata
- Authors
- Berg, E. L., Robinson, M. K., Mansson, O., Butcher, E. C., & Magnani, J. L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1991-08
- Volume
- 266
- Issue
- 23
- Pages
- 14869-14872
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1546312651
- Cited by
- 473
- References
- 28
- FWCI
- 20.17
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: A carbohydrate domain common to both sialyl Le(a) and sialyl Le(X) is recognized by the endothelial cell leukocyte adhesion molecule ELAM-1. https://app.cochat.ai/papers/10.1016/s0021-9258(18)98555-8
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- Berg, E. L., Robinson, M. K., Mansson, O., Butcher, E. C., & Magnani, J. L. (1991). A carbohydrate domain common to both sialyl Le(a) and sialyl Le(X) is recognized by the endothelial cell leukocyte adhesion molecule ELAM-1. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)98555-8
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