Immunochemical studies of the purified human platelet receptor for the α1(I)-chain of chick skin collagen

T. M. Chiang, Andrew Kang, James Dale, E. H. Beachey

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

The membrane receptor of human platelets that bind the α1(I)-chain of chick skin collagen was purified to homogeneity by molecular sieve chromatography, affinity chromatography, and preparative gel-electrophoresis. Rabbits that were immunized with the purified receptor emulsified in complete Freund's adjuvant produced antibody, as measured by an enzyme-linked immunosorbent assay. The antiserum was shown to be highly receptor-specific by immunoprecipitation of solubilized platelet membrane protein that had been labeled with (γ-32P)ATP and protein kinase. Platelet aggregation induced by α1(I) as well as native chick skin collagen was inhibited by both the purified receptor and antibody against the receptor in a dose-dependent fashion. In contrast, neither the receptor nor the antiserum inhibited ADP-induced aggregation. These studies provide the most definitive evidence that α1(I) and native collagen interact specifically with a cell surface receptor on human platelets to induce aggregation.

Original languageEnglish (US)
Pages (from-to)872-876
Number of pages5
JournalJournal of Immunology
Volume133
Issue number2
StatePublished - Jan 1 1984

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Collagen
Blood Platelets
Skin
Immune Sera
Freund's Adjuvant
Antibodies
Cell Surface Receptors
Platelet Aggregation
Affinity Chromatography
Immunoprecipitation
Adenosine Diphosphate
Protein Kinases
Gel Chromatography
Electrophoresis
Membrane Proteins
Adenosine Triphosphate
Gels
Enzyme-Linked Immunosorbent Assay
Rabbits
Membranes

All Science Journal Classification (ASJC) codes

  • Immunology

Cite this

Immunochemical studies of the purified human platelet receptor for the α1(I)-chain of chick skin collagen. / Chiang, T. M.; Kang, Andrew; Dale, James; Beachey, E. H.

In: Journal of Immunology, Vol. 133, No. 2, 01.01.1984, p. 872-876.

Research output: Contribution to journalArticle

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