Expression cloning of a functional glycoprotein ligand for P-selectin.

Autor: Sako D; Genetics Institute, Small Molecule Drug Discovery Group, Cambridge, Massachusetts 02140., Chang XJ, Barone KM, Vachino G, White HM, Shaw G, Veldman GM, Bean KM, Ahern TJ, Furie B, et. al.
Jazyk: angličtina
Zdroj: Cell [Cell] 1993 Dec 17; Vol. 75 (6), pp. 1179-86.
DOI: 10.1016/0092-8674(93)90327-m
Abstrakt: The initial adhesive interactions between circulating leukocytes and endothelia are mediated, in part, by P-selectin. We now report the expression cloning of a functional ligand for P-selectin from an HL-60 cDNA library. The predicted amino acid sequence reveals a novel mucin-like transmembrane protein. Significant binding of transfected COS cells to P-selectin requires coexpression of both the protein ligand and a fucosyltransferase. This binding is calcium dependent and can be inhibited by a neutralizing monoclonal antibody to P-selectin. Cotransfected COS cells express the ligand as a homodimer of 220 kd. A soluble ligand construct, when coexpressed with fucosyltransferase in COS cells, also mediates P-selectin binding and is immunocrossreactive with the major HL-60 glycoprotein that specifically binds P-selectin.
Databáze: MEDLINE