Involvement of a protease in tert-butylhydroperoxide-mediated activation of Ca2+ ATPase in microsomes of pulmonary smooth muscle.
Indian J Biochem Biophys
;
1996 Oct; 33(5): 414-9
Artigo
em Inglês
| IMSEAR
| ID: sea-26294
ABSTRACT
Microsomes isolated from bovine pulmonary artery smooth muscle tissue treated with the oxidant t-buOOH stimulated Ca2+ ATPase activity dose-dependently as also protease activity when tested with a synthetic substrate N-benzoyl-DL-arginine p-nitroanilide. At 300 microM, t-buOOH optimally stimulated these activities. Treatment of the microsomes with t-buOOH stimulated ATP dependent Ca2+ uptake while Na+ dependent Ca2+ uptake was inhibited by t-buOOH. Pretreatment of the microsomes with vitamin E (1 mM) and aprotinin (1 mg/ml) prevented t-buOOH caused stimulation of protease activity and Ca2+ ATPase activity, and also stimulation of ATP dependent Ca2+ uptake while t-buOOH caused inhibition of Na+ dependent Ca2+ uptake was reversed by vitamin E and aprotinin. Treatment of the microsomes with trypsin (1 microgram/ml) stimulated Ca2+ ATPase and ATP dependent Ca2+ uptake while Na+ dependent Ca2+ uptake was inhibited. Pretreatment of the microsomes with aprotinin prevented trypsin caused stimulation of Ca2+ ATPase and ATP dependent Ca2+ uptake, while trypsin caused inhibition of Na+ dependent Ca2+ uptake was reversed by aprotinin.
Texto completo:
DisponíveL
Índice:
IMSEAR (Sudeste Asiático)
Assunto principal:
Endopeptidases
/
Peróxidos
/
Bovinos
/
Cálcio
/
Transporte de Íons
/
ATPases Transportadoras de Cálcio
/
Terc-Butil Hidroperóxido
/
Ativação Enzimática
/
Pulmão
/
Animais
Idioma:
Inglês
Revista:
Indian J Biochem Biophys
Ano de publicação:
1996
Tipo de documento:
Artigo
Similares
MEDLINE
...
LILACS
LIS