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January 1, 1984Cell Motility

Ca2+‐dependent contraction of human lung fibroblasts treated with triton X‐100: A role of Ca2+‐calmodulin‐dependent phosphorylation of myosin 20,000‐dalton light chain

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Population

Human lung fibroblast MRC-5 cells treated with Triton X-100 (MRC-5 cell models)

Design

Preclinical

Authors

HMHirohisa MasudaNational Institutes of HealthKOKatsushi OwaribeNagoya UniversityHHHiroshi HayashiTokyo Metropolitan Institute of Public Health

Discussion

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Implication

Does not support clinical translation; leaves open whether myosin light chain phosphorylation is a druggable target in human fibrosis.

Structured PICO

P
Population
Human lung fibroblast MRC-5 cells treated with Triton X-100 (MRC-5 cell models)
I
Intervention
MgATP and Ca2+ (>1 microM), calmodulin antagonists, exogenous calmodulin, or ATP analogue (adenosine 5'-0-(3-thiotriphosphate))
O
Outcome
Contraction of stress fibers and phosphorylation of myosin 20,000-dalton (20 Kd) light chainsurrogate

This basic science study demonstrates that Ca2+-calmodulin-dependent phosphorylation of the myosin 20 Kd light chain is essential for the contraction of human lung fibroblasts.

Cite This Study

Masuda et al. (1984) studied this question.

synapsesocial.com/papers/6a703a2b5d37378ac1dd5007https://doi.org/10.1002/cm.970040503
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Also Consider

Synapse has enriched one closely related paper. Consider it for comparative context:

  1. 1Mechanism of retraction of the trailing edge during fibroblast movement.1981 · 287 citations