Regulatory mechanism by the phosphorylation of 20-kDa light chain of porcine aorta smooth muscle myosin.

Regulatory mechanism by the phosphorylation of 20-kDa light chain of porcine aorta smooth muscle myosin. Research Abstract Details 

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Regulatory mechanism by the phosphorylation of 20-kDa light chain of porcine aorta smooth muscle myosin. Abstract Text:

Y Hasegawa,K Tanahashi,F Morita,

Porcine aorta smooth muscle myosin was subjected to limited proteolysis by Staphylococcus aureus protease (V8-protease) at 30 mM KCl, under which condition the myosin is in the filamentous form. The heavy chain of the myosin molecule was mainly digested at the 68-160 kDa junction, which corresponds to the 50-20-kDa junction in the heavy chain of skeletal muscle myosin subfragment-1 (S-1). When the filamentous myosin formed a rigor complex in the presence of F-actin, this site was blocked, and the junction between S-1 and subfragment-2 (S-2) was in turn digested specifically. Both phosphorylated and unphosphorylated 20-kDa light chain (LC20) in the aorta myosin remained intact under these conditions. The actin-activated ATPase activity of phosphorylated myosin was not influenced by the cleavage of the S-1-S-2 junction. With unphosphorylated myosin, however, the actin-activated ATPase activity increased with the cleavage of the S-1-S-2 junction and reached the level of ATPase activity of phosphorylated myosin at the stage of complete cleavage. The increase of ATPase activity was found to be proportional to the loss of double-headed myosin. The overall data indicate that LC20 works to suppress the actin-activated ATPase activity, and the suppression is released by the phosphorylation of LC20. The presence of two heads in myosin is required to reveal such regulation by LC20.

Regulatory mechanism by the phosphorylation of 20-kDa light chain of porcine aorta smooth muscle myosin. Publishing Authors By Initials

Y Hasegawa,K Tanahashi,F Morita,

For similar animals: chordata: vertebrates: mammals: artiodactyla: swine research abstracts see: animals: chordata: vertebrates: mammals: artiodactyla: swine research

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Regulatory mechanism by the phosphorylation of 20-kDa light chain of porcine aorta smooth muscle myosin. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 108

Page Numbers: 909-13

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Dec

YEAR: 1990

Regulatory mechanism by the phosphorylation of 20-kDa light chain of porcine aorta smooth muscle myosin. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Regulatory mechanism by the phosphorylation of 20-kDa light chain of porcine aorta smooth muscle myosin. Keywords Mesh Terms:

KEYWORDS: Swine

MESH TERMS: pharmacology

Chemical & Substance for Abstract: Regulatory mechanism by the phosphorylation of 20-kDa light chain of porcine aorta smooth muscle myosin. Information

Substance Name: Myosins

Registry Number: EC 3.6.1.4

Grant and Affiliation Information for Regulatory mechanism by the phosphorylation of 20-kDa light chain of porcine aorta smooth muscle myosin.

AFFILIATION: Department of Chemistry, Faculty of Science, Hokkaido University.

Country: JAPAN

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MEDLINETA: J Biochem

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