Protease action and generation of beta-thromboglobulin-like protein followed by platelet activation.

Abstract:

:Beta-thromboglobulin (beta-TG) is a platelet-specific protein present in the alpha-granules and secreted into the surrounding medium on cell activation. The sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) of platelet releasate after inhibition of metalloproteinases with ethyleneglycol-bis-(beta-aminoethyl ether) N,N'-tetra acetic acid (EGTA) showed disappearance of an 8.0-kDa band. In the absence of the cation chelators, a 48-kDa band disappeared and concurrently, the 8.0-kDa band intensity increased suggesting that the former may be the immediate precursor of the latter. The Western blot stained using specific antibodies, isolated from single-cell clones of hybridoma, against 8.0 kDa protein recognized not only 48 and 8.0 kDa bands but few others too. The data suggests that one or more high molecular weight protein is released from alpha-granules and is broken down into smaller fragments after release to form beta-thromboglobulin (beta-TG)-like proteins by the action of metal dependent proteases.

journal_name

Thromb Res

journal_title

Thrombosis research

authors

Resmi KR,Krishnan LK

doi

10.1016/s0049-3848(02)00135-4

subject

Has Abstract

pub_date

2002-05-15 00:00:00

pages

229-36

issue

4-5

eissn

0049-3848

issn

1879-2472

pii

S0049384802001354

journal_volume

106

pub_type

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