Collagen-platelet interaction

Separate receptor sites for types I and III collagen

Thomas M. Chiang, Jerome M. Seyer, Andrew Kang

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

We have isolated a platelet membrane protein of Mr47 kDa which is responsible for the interaction of platelets with type III collagen. The 47 kDa protein was purified to apparent homogeneity by type III collagen-Sepharose 2B column chromatography and preparative slab gel electrophoreses. The 47 kDa protein blocked the adhesion of platelets to type III but not to type I collagen. Polyclonal antibodies were obtained from rabbits immunized with the purified 47 kDa protein emulsified in complete Freund's adjuvant. The polyclonal antibodies inhibited the type III collagen but not type I collagen-induced platelet aggregation. The inhibitory effect of the antibodies on type III collagen-induced platelet aggregation was dose-dependent. Cross-inhibition on platelet aggregation studies showed that type I collagen receptor antibodies (Mr65 kDa) did not inhibit type III collagen-induced platelet aggregation and type III collagen receptor antibodies did not inhibit type I collagen induced platelet aggregation. These results suggest that type I and type III collagens interact with platelets at separate sites.

Original languageEnglish (US)
Pages (from-to)443-456
Number of pages14
JournalThrombosis Research
Volume71
Issue number6
DOIs
StatePublished - Sep 15 1993

Fingerprint

Collagen Type III
Platelet Aggregation
Collagen Type I
Collagen
Blood Platelets
Antibodies
Collagen Receptors
Proteins
Freund's Adjuvant
Sepharose
Chromatography
Membrane Proteins
Gels
type I collagen receptor
Rabbits

All Science Journal Classification (ASJC) codes

  • Hematology

Cite this

Collagen-platelet interaction : Separate receptor sites for types I and III collagen. / Chiang, Thomas M.; Seyer, Jerome M.; Kang, Andrew.

In: Thrombosis Research, Vol. 71, No. 6, 15.09.1993, p. 443-456.

Research output: Contribution to journalArticle

Chiang, Thomas M. ; Seyer, Jerome M. ; Kang, Andrew. / Collagen-platelet interaction : Separate receptor sites for types I and III collagen. In: Thrombosis Research. 1993 ; Vol. 71, No. 6. pp. 443-456.
@article{7cf78c7adda541fa890a696aa9f487b7,
title = "Collagen-platelet interaction: Separate receptor sites for types I and III collagen",
abstract = "We have isolated a platelet membrane protein of Mr47 kDa which is responsible for the interaction of platelets with type III collagen. The 47 kDa protein was purified to apparent homogeneity by type III collagen-Sepharose 2B column chromatography and preparative slab gel electrophoreses. The 47 kDa protein blocked the adhesion of platelets to type III but not to type I collagen. Polyclonal antibodies were obtained from rabbits immunized with the purified 47 kDa protein emulsified in complete Freund's adjuvant. The polyclonal antibodies inhibited the type III collagen but not type I collagen-induced platelet aggregation. The inhibitory effect of the antibodies on type III collagen-induced platelet aggregation was dose-dependent. Cross-inhibition on platelet aggregation studies showed that type I collagen receptor antibodies (Mr65 kDa) did not inhibit type III collagen-induced platelet aggregation and type III collagen receptor antibodies did not inhibit type I collagen induced platelet aggregation. These results suggest that type I and type III collagens interact with platelets at separate sites.",
author = "Chiang, {Thomas M.} and Seyer, {Jerome M.} and Andrew Kang",
year = "1993",
month = "9",
day = "15",
doi = "10.1016/0049-3848(93)90118-8",
language = "English (US)",
volume = "71",
pages = "443--456",
journal = "Thrombosis Research",
issn = "0049-3848",
publisher = "Elsevier Limited",
number = "6",

}

TY - JOUR

T1 - Collagen-platelet interaction

T2 - Separate receptor sites for types I and III collagen

AU - Chiang, Thomas M.

AU - Seyer, Jerome M.

AU - Kang, Andrew

PY - 1993/9/15

Y1 - 1993/9/15

N2 - We have isolated a platelet membrane protein of Mr47 kDa which is responsible for the interaction of platelets with type III collagen. The 47 kDa protein was purified to apparent homogeneity by type III collagen-Sepharose 2B column chromatography and preparative slab gel electrophoreses. The 47 kDa protein blocked the adhesion of platelets to type III but not to type I collagen. Polyclonal antibodies were obtained from rabbits immunized with the purified 47 kDa protein emulsified in complete Freund's adjuvant. The polyclonal antibodies inhibited the type III collagen but not type I collagen-induced platelet aggregation. The inhibitory effect of the antibodies on type III collagen-induced platelet aggregation was dose-dependent. Cross-inhibition on platelet aggregation studies showed that type I collagen receptor antibodies (Mr65 kDa) did not inhibit type III collagen-induced platelet aggregation and type III collagen receptor antibodies did not inhibit type I collagen induced platelet aggregation. These results suggest that type I and type III collagens interact with platelets at separate sites.

AB - We have isolated a platelet membrane protein of Mr47 kDa which is responsible for the interaction of platelets with type III collagen. The 47 kDa protein was purified to apparent homogeneity by type III collagen-Sepharose 2B column chromatography and preparative slab gel electrophoreses. The 47 kDa protein blocked the adhesion of platelets to type III but not to type I collagen. Polyclonal antibodies were obtained from rabbits immunized with the purified 47 kDa protein emulsified in complete Freund's adjuvant. The polyclonal antibodies inhibited the type III collagen but not type I collagen-induced platelet aggregation. The inhibitory effect of the antibodies on type III collagen-induced platelet aggregation was dose-dependent. Cross-inhibition on platelet aggregation studies showed that type I collagen receptor antibodies (Mr65 kDa) did not inhibit type III collagen-induced platelet aggregation and type III collagen receptor antibodies did not inhibit type I collagen induced platelet aggregation. These results suggest that type I and type III collagens interact with platelets at separate sites.

UR - http://www.scopus.com/inward/record.url?scp=0027316934&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027316934&partnerID=8YFLogxK

U2 - 10.1016/0049-3848(93)90118-8

DO - 10.1016/0049-3848(93)90118-8

M3 - Article

VL - 71

SP - 443

EP - 456

JO - Thrombosis Research

JF - Thrombosis Research

SN - 0049-3848

IS - 6

ER -