Tyrosine phosphorylation of paxillin may be involved in vascular smooth muscle contraction
The Korean Journal of Physiology and Pharmacology
; : 211-217, 2000.
Article
en En
| WPRIM
| ID: wpr-727737
Biblioteca responsable:
WPRO
ABSTRACT
Paxillin is a regulatory component of the complex of cytoskeletal proteins that link the actin cytoskeleton to the plasma membrane. However, the role of paxillin during smooth muscle contraction is unclear. We investigated a possible role for the membrane-associated dense plaque protein paxillin in the regulation of contraction in rat aortic vascular smooth muscle. The tyrosine phosphorylation of paxillin, which was increased by norepinephrine, reached a peak level after 1 min stimulation and then decreased with time. However, norepinephrine induced a sustained contraction that reached a steady state 30 min after application. Pretreatment with tyrphostin, an inhibitor of tyrosine kinase, inhibited the tyrosine phosphorylation of paxillin and also the contraction stimulated by norepinephrine. Both inhibitions were concentration-dependent, and the degree of correlation between them was high. These results show that, in rat aortic smooth muscle, tyrosine kinase(s) activated by norepinephrine may phosphorylate the tyrosine residues of paxillin, thereby providing a source of regulation during vascular smooth muscle contraction.
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Texto completo:
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Índice:
WPRIM
Asunto principal:
Fosforilación
/
Tirosina
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Citoesqueleto de Actina
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Proteínas Tirosina Quinasas
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Norepinefrina
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Membrana Celular
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Proteínas del Citoesqueleto
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Paxillin
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Músculo Liso
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Músculo Liso Vascular
Límite:
Animals
Idioma:
En
Revista:
The Korean Journal of Physiology and Pharmacology
Año:
2000
Tipo del documento:
Article