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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Di Salvo J,Gifford D,Bialojan C,Rüegg JCdoi
10.1016/0006-291x(83)91385-2subject
Has Abstractpub_date
1983-03-29 00:00:00pages
906-11issue
3eissn
0006-291Xissn
1090-2104pii
0006-291X(83)91385-2journal_volume
111pub_type
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journal_title:Biochemical and biophysical research communications
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