Collagen-platelet interaction: Type XI collagen-induced platelet aggregation

T. M. Chiang, M. Cremer, Andrew Kang

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Type XI collagen in its native fibrillar but not in soluble monomeric form mediates human platelet aggregation and release of adenosine triphosphate in a dose-dependent manner. Its action is inhibited by aspirin. Type XI collagen also increased radiolabelled phosphate incorporation into protein bands with molecular weights of 42 KDa and 22 KDa, respectively. In contract, these events were not observed in platelets incubated with type IX collagen. These results suggest that the fibrillar type XI collagen has the same ability as other types of collagen to induce human platelet aggregation.

Original languageEnglish (US)
Pages (from-to)509-520
Number of pages12
JournalThrombosis Research
Volume59
Issue number3
DOIs
StatePublished - Aug 1 1990

Fingerprint

Collagen Type XI
Platelet Aggregation
Collagen Type IX
Collagen
Blood Platelets
Fibrillar Collagens
Contracts
Aspirin
Adenosine Triphosphate
Molecular Weight
Phosphates
Proteins

All Science Journal Classification (ASJC) codes

  • Hematology

Cite this

Collagen-platelet interaction : Type XI collagen-induced platelet aggregation. / Chiang, T. M.; Cremer, M.; Kang, Andrew.

In: Thrombosis Research, Vol. 59, No. 3, 01.08.1990, p. 509-520.

Research output: Contribution to journalArticle

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