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June 1, 1982Journal of Biological ChemistryOpen Access

Phosphorylation-dependent activated tension in skinned gizzard muscle fibers in the absence of Ca2+.

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Population

Skinned gizzard muscle fibers

Comparison

Ca2+-insensitive myosin light chain kinase in… vs Ca2+-activated tension

Design

Preclinical

Authors

MWMichael P. WalshRBRobert BridenbaughDHDavid J. Hartshorne

Discussion

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Overview

Supports myosin phosphorylation dominance in animal smooth muscle; leaves open translation to human vascular tone regulation.

Structured PICO

P
Population
Skinned gizzard muscle fibers
I
Intervention
Ca2+-insensitive myosin light chain kinase in the absence of Ca2+
C
Comparator
Ca2+-activated tension
O
Outcome
Isometric force development (tension)surrogate

This study demonstrates that phosphorylation of myosin light chains is the primary driver of tension development in smooth muscle, even in the absence of calcium.

Cite This Study

Walsh et al. (1982) studied this question.

synapsesocial.com/papers/6a7270543ce530166bc352cahttps://doi.org/10.1016/s0021-9258(20)65090-6
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Calcium regulation of porcine aortic myosin.1981 · 46 citations
  2. 2Force measurements in skinned muscle fibres1969 · 326 citations
  3. 3Does Phosphoryiation of Myosin Light Chain Have Direct Relation to Regulation in Smooth Muscle?11977 · 56 citations
  4. 4Myosin Phosphorylation and the Cross-Bridge Cycle in Arterial Smooth Muscle1981 · 708 citations
  5. 5Ca2+ Regulation in Vascular Smooth Muscle11977 · 81 citations