Isolation and characterization of a bovine cDNA encoding a functional homolog of human P-selectin.

Journal Article

A cDNA encoding a homologue of human P-selectin has been isolated from a bovine capillary endothelial cDNA library. The 2.7 kb cDNA encodes a 646 amino acid polypeptide with 77% identity to the human P-selectin except that it lacks three of the consensus repeat domains found in human P-selectin. Human P-selectin, expressed in platelets and endothelium, is a Ca(2+)-dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. To determine if bovine P-selectin exhibits a similar binding activity, its cDNA was expressed in COS cells and the ability of the transfectants to bind HL-60 human myelogenous leukemia cells was examined. The bovine P-selectin bound the myeloid cells in a manner similar to human P-selectin, indicating that the altered domain structure of bovine P-selectin does not affect P-selectin function in this in vitro cell adhesion assay.

Full Text

Duke Authors

Cited Authors

  • Strubel, NA; Nguyen, M; Kansas, GS; Tedder, TF; Bischoff, J

Published Date

  • April 30, 1993

Published In

Volume / Issue

  • 192 / 2

Start / End Page

  • 338 - 344

PubMed ID

  • 7683458

International Standard Serial Number (ISSN)

  • 0006-291X

Digital Object Identifier (DOI)

  • 10.1006/bbrc.1993.1420

Language

  • eng

Conference Location

  • United States