July 1, 1992AJP Cell Physiology

Cooperative activation of myosin by light chain phosphorylation in permeabilized smooth muscle

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Population

Permeabilized rabbit portal vein smooth muscle

Comparison

Myosin light chain thiophosphorylation vs Resting muscle (unphosphorylated)

Design

Preclinical

Authors

TVTapan B. VyasJefferson College SMSusan U. MooersThomas Jefferson University SNS. NarayanThomas Jefferson University

Discussion

Member takes

Implication

Small thiophosphorylation maximally activates animal smooth muscle myosin; hypothesis-generating for human vascular regulation.

Structured PICO

Population

Permeabilized rabbit portal vein smooth muscle

Intervention

Myosin light chain thiophosphorylation (varying degrees)

Comparator

Resting muscle (unphosphorylated)

Outcome

Rate of exchange of bound nucleoside diphosphate (ADP exchange) and ATPase activitysurrogate

A small degree of myosin light chain thiophosphorylation cooperatively activates the maximum number of myosin molecules in smooth muscle, with higher phosphorylation levels increasing the myosin cycle speed.

Cite This Study

Vyas et al. (1992) studied this question.

synapsesocial.com/papers/6a843f50de69cb059c72f9c3 https://doi.org/10.1152/ajpcell.1992.263.1.c210

View Full Paper

Ask AI

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Cooperative activation of myosin by light chain phosphorylation in permeabilized smooth muscle

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Cooperative activation of myosin by light chain phosphorylation in permeabilized smooth muscle

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider