Temporal relationships between isometric force, phosphorylase, and protein kinase activities in vascular smooth muscle.
Proc Soc Exp Biol Med
; 178(2): 254-60, 1985 Feb.
Article
em En
| MEDLINE
| ID: mdl-2982169
ABSTRACT
Vascular smooth muscle contractility is tightly coupled to ATP production by intermediary metabolism. To elucidate mechanisms underlying coordination of metabolism and contractility we studied the time course of isometric force, and the activation of phosphorylase and cAMP-dependent protein kinases during stimulation of bovine coronary arterial strips with KCl. Isometric force reached a maximum after 10 min of exposure to 30 mM KCl (ED90) and was sustained throughout the subsequent 20-min period of contraction. In contrast, activation of phosphorylase was biphasic enzymic activity reached a maximum (176 +/- 10% of control) after 3 min of contraction and then, though remaining above control, activity declined to a lower level (135 +/- 7% of control). However, no change occurred in the activity ratios for cAMP-dependent protein kinase assessed in either the presence (type II isozyme) or absence (type I isozyme) of 0.5 M NaCl. These data suggest that the activation of phosphorylase during K+-induced contraction is independent of the cAMP system. The biphasic activation of phosphorylase may reflect transient changes in the intracellular concentration of Ca2+ or the activation of a phosphatase(s) during the response.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosfotransferases
/
Proteínas Quinases
/
Músculo Liso Vascular
Limite:
Animals
Idioma:
En
Revista:
Proc Soc Exp Biol Med
Ano de publicação:
1985
Tipo de documento:
Article