The comparison of Ca2+/CaM-independent and Ca2+/CaM-dependent phosphorylation of myosin light chains by MLCK.

The comparison of Ca2+/CaM-independent and Ca2+/CaM-dependent phosphorylation of myosin light chains by MLCK. Research Abstract Details 

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The comparison of Ca2+/CaM-independent and Ca2+/CaM-dependent phosphorylation of myosin light chains by MLCK. Abstract Text:

Z Tang,H Chen,J Yang,S Dai,Y Lin,

The main regulatory mechanism of smooth muscle contraction involves Ca2+/calmodulin (CaM)-dependent phosphorylation of myosin (CDPM), by myosin light chain kinase (MLCK). It is also known that the increase in intracellular Ca2+ and phosphorylation of myosin occurs within a short time under physiological conditions, but the muscle tension may persist for a longer period of time. However, the mechanism of this phenomenon is still not clear. We hypothesize that MLCK also phosphorylates myosin in a Ca2+/CaM-independent manner (CIPM). The difference between CIPM and CDPM are as follows. Firstly, the extent of CIPM by MLCK was temperature-independent, whereas CDPM by MLCK was apparently decreasing with increasing temperature. Secondly, in contrast to the decreased extent of CDPM, the prolongation of incubation time did not decrease the extent of CIPM. Thirdly, a high concentration of K+ influences CIPM less than CDPM. Furthermore, the MLCK inhibitor ML-9 significantly inhibited CDPM by MLCK but not CIPM by MLCK. Lastly, arachidonic acid selectively increased CIPM by MLCK but not CDPM by MLCK. Finally, the activity of Mg2+-ATPase of myosin followed the sequence as this: CDPM>CIPM>unphosphorylated myosin. Our results revealed some primary features of CIPM by MLCK.

The comparison of Ca2+/CaM-independent and Ca2+/CaM-dependent phosphorylation of myosin light chains by MLCK. Publishing Authors By Initials

Z Tang,H Chen,J Yang,S Dai,Y Lin,

For similar natural sciences: time: time factors research abstracts see: natural sciences: time: time factors research

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The comparison of Ca2+/CaM-independent and Ca2+/CaM-dependent phosphorylation of myosin light chains by MLCK. Journal Published:

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

Journal: Physiological research / Academia Scientiarum Bohe

VOLUME: 54

Page Numbers: 671-8

Journal Abbreviation: Physiol Res

ISSN: 0862-8408

DAY: 2

MONTH: 04

YEAR: 2005

The comparison of Ca2+/CaM-independent and Ca2+/CaM-dependent phosphorylation of myosin light chains by MLCK. Information

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LANGUAGE: eng

NlmUniqueID: 9112413

The comparison of Ca2+/CaM-independent and Ca2+/CaM-dependent phosphorylation of myosin light chains by MLCK. Keywords Mesh Terms:

KEYWORDS: Time Factors

MESH TERMS: metabolism

Chemical & Substance for Abstract: The comparison of Ca2+/CaM-independent and Ca2+/CaM-dependent phosphorylation of myosin light chains by MLCK. Information

Substance Name: Myosins

Registry Number: EC 3.6.1.4

Grant and Affiliation Information for The comparison of Ca2+/CaM-independent and Ca2+/CaM-dependent phosphorylation of myosin light chains by MLCK.

AFFILIATION: Department of Pharmacology, Dalian Medical University, 465# Zhongshan Road, Dalian, P.R.China, 116027.

Country: Czech Republic

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MEDLINETA: Physiol Res

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