| Autor: |
Bernard, A., Griffiths, B., Noé, W., Wurm, F., Sinacore, Martin S., Richards, TroyZ, Francullo, Linda, Woodard, Amy, Hardy, Mark, Cornell, Richard, Koza, Steve, Davies, Monique, Ellis, Deb, Harrison, Scott |
| Zdroj: |
Animal Cell Technology: Products from Cells, Cells as Products; 2000, p229-235, 7p |
| Abstrakt: |
P-Selectin Glycoprotein Ligand-1 (PSGL-1) is a dimeric mucin-like transmembrane glycoprotein identified as a functional ligand for P-Selectin (1). Functional activity of PSGL-1 is dependent upon at least two key posttranslational modifications made to the amino terminus. Core 2 O-linked oligosaccharide structures at Thr16 bearing the sialyl-Lewisx (SLex) antigen and sulfation of one or more of the NH2-terminal tyrosine it has been shown that a polypeptide containing the NH2-terminal 47 amino acid sequence of human PSGL-1 is sufficient for high-affinity binding to P-Selectin (2). [ABSTRACT FROM AUTHOR] |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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