A biochemical study on the effect of proteolysis of beta-thromboglobulin proteins released from activated platelets on fibroblast proliferation

Resmi Ravindran, Lissy K. Krishnan

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

β-Thromboglobulin (β-TG) proteins are a heterogeneous group released from platelet α-granules on activation and have an effect on fibroblast migration and proliferation. We have previously reported the action of a metal-dependent protease on platelet-released proteins, which generates low-molecular-weight proteins that could be inhibited by ethylenediaminetetraacetic acid (EDTA). To understand the physiological significance of the breakdown of proteins after release, their effect on fibroblast proliferation in vitro was studied. Platelet releasates were obtained without and with EDTA inhibition designated as R1 and R2, respectively, and proteins were affinity purified for testing. Cell proliferation was measured using [3H]-thymidine assay. Both R1 and R2 showed maximum activity at 100 μg/ml and R2 elicited significant proliferation compared to R1. When affinity-purified proteins were tested at 100 ng/ml, high-molecular-weight proteins showed significantly higher proliferation than low-molecular-weight proteins. We have shown that β-TG is cleaved after being released from activated platelets, thereby becoming less mitogenic for fibroblasts.

Original languageEnglish (US)
Pages (from-to)285-289
Number of pages5
JournalPathophysiology of Haemostasis and Thrombosis
Volume36
Issue number6
DOIs
StatePublished - 2007

Keywords

  • α-Granule proteins
  • β-Thromboglobulin
  • Platelet chemokines

ASJC Scopus subject areas

  • Hematology
  • Physiology (medical)

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