Protease action and generation of beta-thromboglobulin-like protein followed by platelet activation.
Thromb Res
; 106(4-5): 229-36, 2002 May 15.
Article
em En
| MEDLINE
| ID: mdl-12297130
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.
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Base de dados:
MEDLINE
Assunto principal:
Endopeptidases
/
Precursores de Proteínas
/
Beta-Tromboglobulina
/
Ativação Plaquetária
Limite:
Humans
Idioma:
En
Revista:
Thromb Res
Ano de publicação:
2002
Tipo de documento:
Article
País de afiliação:
Índia