Inhibition of p42 and p44 MAP kinase does not alter smooth muscle contraction in swine carotid artery.
Am J Physiol
; 275(1): H131-8, 1998 07.
Article
em En
| MEDLINE
| ID: mdl-9688905
ABSTRACT
Caldesmon inhibits myosin ATPase activity; phosphorylation of caldesmon reverses the inhibition. The caldesmon kinase is believed to be mitogen-activated protein (MAP) kinase. MAP kinases are activated during vascular stimulation, but a cause-and-effect relationship between kinase activity and contraction has not been established. We examined the role of MAP kinase in contraction using PD-098059, an inhibitor of MAP kinase kinase (MEK). MAP kinase activity was assessed using an anti-active MAP kinase antibody and direct measurement of MAP kinase catalyzed phosphorylation of myelin basic protein, MBP-(95-98). MAP kinase phosphorylation, stimulated by histamine (50 microM) or phorbol 12,13-dibutyrate (PDBu, 0.1 microM), was inhibited by PD-098059 (100 microM). PD-098059 did not alter the sensitivity or the maximal level of force in smooth muscle stimulated by histamine or PDBu, nor did PD-098059 affect contraction of beta-escin-permeabilized tissue. Our data suggest that p44 and p42 MAP kinases are not involved in regulation of vascular smooth muscle contraction. These results do not, however, preclude a role for other isoforms of the MAP kinase family.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Flavonoides
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Artérias Carótidas
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Proteínas Quinases Dependentes de Cálcio-Calmodulina
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Proteína Quinase 1 Ativada por Mitógeno
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Proteínas Quinases Ativadas por Mitógeno
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Contração Isométrica
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Músculo Liso Vascular
Limite:
Animals
Idioma:
En
Ano de publicação:
1998
Tipo de documento:
Article