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Department of Physiology, MCP/Hahnemann School of Medicine, Allegheny University of the Health Sciences, Philadelphia, Pennsylvania 19146
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 µM) or phorbol
12,13-dibutyrate (PDBu, 0.1 µM), was inhibited by PD-098059 (100 µM). 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 
-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.
mitogen-activated protein kinase kinase; PD-098059; vascular smooth muscle; phorbol ester; histamine; phosphorylation; myosin light chain
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