An aortic spontaneously active phosphatase dephosphorylates myosin and inhibits actin-myosin interaction.

Abstract:

:Actin-myosin interaction in aortic actomyosin reportedly requires phosphorylation of the 20,000 dalton myosin light chains. A spontaneously active phosphatase which dephosphorylates phosphorylase a and isolated phosphorylated cardiac myosin light chains was extracted from bovine aortic smooth muscle. This enzyme, when added to aortic native actomyosin (a) significantly suppressed phosphorylation of the light chains of the native hexameric smooth muscle myosin, (b) accelerated the rate and increased the magnitude of myosin light chain dephosphorylation in actomyosin that had been prephosphorylated, and (c) markedly attenuated the rate of actin-myosin interaction. These results support the hypothesis that myosin phosphorylation and subsequent actin-myosin interactions (contractility) in vascular smooth muscle may be modulated by spontaneously active aortic phosphatase.

authors

Di Salvo J,Gifford D,Bialojan C,Rüegg JC

doi

10.1016/0006-291x(83)91385-2

subject

Has Abstract

pub_date

1983-03-29 00:00:00

pages

906-11

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(83)91385-2

journal_volume

111

pub_type

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