A peptide inhibitor of type I collagen-mediated platelet

T. Aggregation, M. Chiang, Andrew Kang

Research output: Contribution to journalArticle

Abstract

A synthetic peptide-1, an 18 amino acid residue peptide derived from a hydrophilic domain of a cloned platelet receptor for type I collagen, was used to study the role of the receptor on types I and III collagen-jnduced platelet aggregation and the release of ATP. The peptide inhibits the type I but not the type III collagen-induced platelet aggregation and the release of ATP in a dose dependent manner. The [125I]-peptide-l specifically binds to type I collagen-coated microtiter wells in a time- and dosedependent manner (with Kd = 10 nM). The binding of [I25l]-peptide-l can be inhibited by an excess of unlabeled peptide-1 suggesting that the binding is specific. The labeled peptide-1 does not bind to fibronectin- or type 111 collagen-coated microtiter wells. The peptide-1 also inhibits the type I collagen stimulated platelet protein phosphorylation of the 47 kDa and 22 kDa proteins. Results from an enzyme-linked immunosorbent assay show that the peptide reacts with the poly- and mono- clonal antibodies raised against the purified platelet type I collagen receptor (Mr 65 kDa). Flow cytometry data also show that peptide-1 inhibits the binding of anti-65 kDa IgG to the platelet surface. The peptide also inhibits the adhesion of platelets on type I collagen matrix and rabbit aortic segments in a dose-dependent manner. These results suggest that the reactive site of the platelet receptor for type I collagen resides in this portion of the molecule.

Original languageEnglish (US)
JournalFASEB Journal
Volume11
Issue number9
StatePublished - Dec 1 1997

Fingerprint

Collagen Type I
Platelets
Blood Platelets
Peptides
Collagen Type III
Platelet Aggregation
Agglomeration
Adenosine Triphosphate
Immunosorbents
Phosphorylation
Monoclonal antibodies
Flow cytometry
Fibronectins
Assays
Catalytic Domain
Flow Cytometry
Proteins
Collagen
Adhesion
Immunoglobulin G

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics

Cite this

A peptide inhibitor of type I collagen-mediated platelet. / Aggregation, T.; Chiang, M.; Kang, Andrew.

In: FASEB Journal, Vol. 11, No. 9, 01.12.1997.

Research output: Contribution to journalArticle

Aggregation, T, Chiang, M & Kang, A 1997, 'A peptide inhibitor of type I collagen-mediated platelet', FASEB Journal, vol. 11, no. 9.
Aggregation, T. ; Chiang, M. ; Kang, Andrew. / A peptide inhibitor of type I collagen-mediated platelet. In: FASEB Journal. 1997 ; Vol. 11, No. 9.
@article{c21eddd9e38c4787b1ac2a03a10fdf74,
title = "A peptide inhibitor of type I collagen-mediated platelet",
abstract = "A synthetic peptide-1, an 18 amino acid residue peptide derived from a hydrophilic domain of a cloned platelet receptor for type I collagen, was used to study the role of the receptor on types I and III collagen-jnduced platelet aggregation and the release of ATP. The peptide inhibits the type I but not the type III collagen-induced platelet aggregation and the release of ATP in a dose dependent manner. The [125I]-peptide-l specifically binds to type I collagen-coated microtiter wells in a time- and dosedependent manner (with Kd = 10 nM). The binding of [I25l]-peptide-l can be inhibited by an excess of unlabeled peptide-1 suggesting that the binding is specific. The labeled peptide-1 does not bind to fibronectin- or type 111 collagen-coated microtiter wells. The peptide-1 also inhibits the type I collagen stimulated platelet protein phosphorylation of the 47 kDa and 22 kDa proteins. Results from an enzyme-linked immunosorbent assay show that the peptide reacts with the poly- and mono- clonal antibodies raised against the purified platelet type I collagen receptor (Mr 65 kDa). Flow cytometry data also show that peptide-1 inhibits the binding of anti-65 kDa IgG to the platelet surface. The peptide also inhibits the adhesion of platelets on type I collagen matrix and rabbit aortic segments in a dose-dependent manner. These results suggest that the reactive site of the platelet receptor for type I collagen resides in this portion of the molecule.",
author = "T. Aggregation and M. Chiang and Andrew Kang",
year = "1997",
month = "12",
day = "1",
language = "English (US)",
volume = "11",
journal = "FASEB Journal",
issn = "0892-6638",
publisher = "FASEB",
number = "9",

}

TY - JOUR

T1 - A peptide inhibitor of type I collagen-mediated platelet

AU - Aggregation, T.

AU - Chiang, M.

AU - Kang, Andrew

PY - 1997/12/1

Y1 - 1997/12/1

N2 - A synthetic peptide-1, an 18 amino acid residue peptide derived from a hydrophilic domain of a cloned platelet receptor for type I collagen, was used to study the role of the receptor on types I and III collagen-jnduced platelet aggregation and the release of ATP. The peptide inhibits the type I but not the type III collagen-induced platelet aggregation and the release of ATP in a dose dependent manner. The [125I]-peptide-l specifically binds to type I collagen-coated microtiter wells in a time- and dosedependent manner (with Kd = 10 nM). The binding of [I25l]-peptide-l can be inhibited by an excess of unlabeled peptide-1 suggesting that the binding is specific. The labeled peptide-1 does not bind to fibronectin- or type 111 collagen-coated microtiter wells. The peptide-1 also inhibits the type I collagen stimulated platelet protein phosphorylation of the 47 kDa and 22 kDa proteins. Results from an enzyme-linked immunosorbent assay show that the peptide reacts with the poly- and mono- clonal antibodies raised against the purified platelet type I collagen receptor (Mr 65 kDa). Flow cytometry data also show that peptide-1 inhibits the binding of anti-65 kDa IgG to the platelet surface. The peptide also inhibits the adhesion of platelets on type I collagen matrix and rabbit aortic segments in a dose-dependent manner. These results suggest that the reactive site of the platelet receptor for type I collagen resides in this portion of the molecule.

AB - A synthetic peptide-1, an 18 amino acid residue peptide derived from a hydrophilic domain of a cloned platelet receptor for type I collagen, was used to study the role of the receptor on types I and III collagen-jnduced platelet aggregation and the release of ATP. The peptide inhibits the type I but not the type III collagen-induced platelet aggregation and the release of ATP in a dose dependent manner. The [125I]-peptide-l specifically binds to type I collagen-coated microtiter wells in a time- and dosedependent manner (with Kd = 10 nM). The binding of [I25l]-peptide-l can be inhibited by an excess of unlabeled peptide-1 suggesting that the binding is specific. The labeled peptide-1 does not bind to fibronectin- or type 111 collagen-coated microtiter wells. The peptide-1 also inhibits the type I collagen stimulated platelet protein phosphorylation of the 47 kDa and 22 kDa proteins. Results from an enzyme-linked immunosorbent assay show that the peptide reacts with the poly- and mono- clonal antibodies raised against the purified platelet type I collagen receptor (Mr 65 kDa). Flow cytometry data also show that peptide-1 inhibits the binding of anti-65 kDa IgG to the platelet surface. The peptide also inhibits the adhesion of platelets on type I collagen matrix and rabbit aortic segments in a dose-dependent manner. These results suggest that the reactive site of the platelet receptor for type I collagen resides in this portion of the molecule.

UR - http://www.scopus.com/inward/record.url?scp=33750157928&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33750157928&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:33750157928

VL - 11

JO - FASEB Journal

JF - FASEB Journal

SN - 0892-6638

IS - 9

ER -