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
Article
in English
| 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.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Endopeptidases
/
Peroxides
/
Cattle
/
Calcium
/
Ion Transport
/
Calcium-Transporting ATPases
/
Tert-Butylhydroperoxide
/
Enzyme Activation
/
Lung
/
Animals
Language:
English
Journal:
Indian J Biochem Biophys
Year:
1996
Type:
Article
Similar
MEDLINE
...
LILACS
LIS