Please use this identifier to cite or link to this item:
|Title:||A Biochemical Study on the Effect of Proteolysis of Beta-Thromboglobulin Proteins Released from Activated Platelets on Fibroblast Proliferation|
Krishnan, Lissy K.
|Publisher:||PATHOPHYSIOLOGY OF HAEMOSTASIS AND THROMBOSIS|
|Citation:||PATHOPHYSIOLOGY OF HAEMOSTASIS AND THROMBOSIS. 36; 6; 285-289|
|Abstract:||beta-Thromboglobulin (beta-TG) proteins are a heterogeneous group released from platelet alpha-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 [(3)H]-thymidine assay. Both R1 and R2 showed maximum activity at 100 mu g/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 beta-TG is cleaved after being released from activated platelets, thereby becoming less mitogenic for fibroblasts. Copyright (C) 2010 S. Karger AG, Basel|
|Appears in Collections:||Journal Articles|
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.