skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Incorporation of thrombospondin into fibrin clots

Abstract

Thrombospondin is a major platelet glycoprotein which is released from platelets during blood coagulation. The authors examined the interaction of thrombospondin with polymerizing fibrin. Thrombospondin, purified from human platelets and labeled with /sup 125/I, became incorporated into clots formed from both plasma and purified fibrinogen. Plasma clots contained somewhat less thrombospondin than clots formed from equivalent concentrations of fibrinogen. In plasma clots and fibrin clots formed in the presence of factor XIII, thrombospondin was cross-linked in the clot; thrombospondin in the supernatant remained largely monomeric. Cross-linking of thrombospondin by factor XIII, however, only slightly increased the amount of thrombospondin which was incorporated into the clot. In contrast, incorporation of /sup 125/I-fibronectin into clots was dependent upon cross-linking. Most of the incorporation of /sup 125/I-thrombospondin occurred during fibrin polymerization as judged by parallel studies of the incorporation of /sup 125/I-fibrinogen. The amount of thrombospondin incorporated into a clot was directly related to thrombospondin concentration and was only weakly dependent on fibrinogen concentration. Incorporation was not saturated at thrombospondin:fibrin (mol/mol) ratios as high as 2/1. Thrombospondin, however, modified the final structure of fibrin clots in a concentration-dependent manner as monitored by opacity. When tryptic digests of /sup 125/I-thrombospondin were studied, the 270-kilodaltonmore » core became incorporated into fibrin whereas the 30-kilodalton heparin binding fragment was excluded. These results indicate that thrombospondin specifically co-polymerizes with fibrin during blood coagulation and may be an important modulator of clot structure.« less

Authors:
; ;
Publication Date:
OSTI Identifier:
6241080
Resource Type:
Journal Article
Journal Name:
J. Biol. Chem.; (United States)
Additional Journal Information:
Journal Volume: 12
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; GLUCOPROTEINS; BLOOD COAGULATION; CROSS-LINKING; BIOCHEMICAL REACTION KINETICS; BLOOD PLATELETS; FIBRIN; FIBRINOGEN; IODINE 125; TRACER TECHNIQUES; BETA DECAY RADIOISOTOPES; BIOLOGICAL MATERIALS; BLOOD; BLOOD CELLS; BLOOD COAGULATION FACTORS; BODY FLUIDS; CARBOHYDRATES; CHEMICAL REACTIONS; COAGULANTS; DAYS LIVING RADIOISOTOPES; DRUGS; ELECTRON CAPTURE RADIOISOTOPES; GLOBULINS; HEMATOLOGIC AGENTS; HEMOSTATICS; INTERMEDIATE MASS NUCLEI; IODINE ISOTOPES; ISOTOPE APPLICATIONS; ISOTOPES; KINETICS; MATERIALS; NUCLEI; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; POLYMERIZATION; PROTEINS; RADIOISOTOPES; REACTION KINETICS; SACCHARIDES; SCLEROPROTEINS; 551001* - Physiological Systems- Tracer Techniques

Citation Formats

Bale, M D, Westrick, L G, and Mosher, D F. Incorporation of thrombospondin into fibrin clots. United States: N. p., 1985. Web.
Bale, M D, Westrick, L G, & Mosher, D F. Incorporation of thrombospondin into fibrin clots. United States.
Bale, M D, Westrick, L G, and Mosher, D F. 1985. "Incorporation of thrombospondin into fibrin clots". United States.
@article{osti_6241080,
title = {Incorporation of thrombospondin into fibrin clots},
author = {Bale, M D and Westrick, L G and Mosher, D F},
abstractNote = {Thrombospondin is a major platelet glycoprotein which is released from platelets during blood coagulation. The authors examined the interaction of thrombospondin with polymerizing fibrin. Thrombospondin, purified from human platelets and labeled with /sup 125/I, became incorporated into clots formed from both plasma and purified fibrinogen. Plasma clots contained somewhat less thrombospondin than clots formed from equivalent concentrations of fibrinogen. In plasma clots and fibrin clots formed in the presence of factor XIII, thrombospondin was cross-linked in the clot; thrombospondin in the supernatant remained largely monomeric. Cross-linking of thrombospondin by factor XIII, however, only slightly increased the amount of thrombospondin which was incorporated into the clot. In contrast, incorporation of /sup 125/I-fibronectin into clots was dependent upon cross-linking. Most of the incorporation of /sup 125/I-thrombospondin occurred during fibrin polymerization as judged by parallel studies of the incorporation of /sup 125/I-fibrinogen. The amount of thrombospondin incorporated into a clot was directly related to thrombospondin concentration and was only weakly dependent on fibrinogen concentration. Incorporation was not saturated at thrombospondin:fibrin (mol/mol) ratios as high as 2/1. Thrombospondin, however, modified the final structure of fibrin clots in a concentration-dependent manner as monitored by opacity. When tryptic digests of /sup 125/I-thrombospondin were studied, the 270-kilodalton core became incorporated into fibrin whereas the 30-kilodalton heparin binding fragment was excluded. These results indicate that thrombospondin specifically co-polymerizes with fibrin during blood coagulation and may be an important modulator of clot structure.},
doi = {},
url = {https://www.osti.gov/biblio/6241080}, journal = {J. Biol. Chem.; (United States)},
number = ,
volume = 12,
place = {United States},
year = {Tue Jun 25 00:00:00 EDT 1985},
month = {Tue Jun 25 00:00:00 EDT 1985}
}