Mechanisms of smooth muscle contraction
A. Horowitz, C. B. Menice, R. Laporte and K. G. Morgan Boston Biomedical Research Institute, Boston, Massachusetts, USA. Work performed with differentiated contractile smooth muscle tissue over the last two decades has made clear that covalent modification of myosin by phosphorylation of the 20-kDa...
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Published in | Physiological reviews Vol. 76; no. 4; pp. 967 - 1003 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
United States
Am Physiological Soc
01.10.1996
American Physiological Society |
Subjects | |
Online Access | Get full text |
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Summary: | A. Horowitz, C. B. Menice, R. Laporte and K. G. Morgan
Boston Biomedical Research Institute, Boston, Massachusetts, USA.
Work performed with differentiated contractile smooth muscle tissue over
the last two decades has made clear that covalent modification of myosin by
phosphorylation of the 20-kDa myosin light chains is a significant mode of
regulation of contractile activity in smooth muscle, particularly in regard
to the generation of phasic contractions and the initial development of
tonic contractions. This regulatory mechanism appears to be of unique
importance in smooth muscle compared with striated muscle. It is equally
clear, however, that there is an important role for protein kinase C in the
regulation of smooth muscle tone maintenance, particularly in vascular
smooth muscle. Several possible signal transduction cascades involving
protein kinase C are outlined. Increasing evidence suggests a link between
protein kinase C and actin-based regulatory mechanisms. This review places
emphasis on relating up-to-date biochemical facts to the physiological
realities of the smooth muscle cell. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 ObjectType-Review-3 content type line 23 ObjectType-Feature-3 ObjectType-Review-1 |
ISSN: | 0031-9333 1522-1210 |
DOI: | 10.1152/physrev.1996.76.4.967 |