July 1, 1993Proceedings of the National Academy of SciencesOpen Access

Caldesmon and a 20-kDa actin-binding fragment of caldesmon inhibit tension development in skinned gizzard muscle fiber bundles.

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Population

Chemically skinned gizzard muscle fiber bundles

Design

Preclinical

Authors

GPGabriele PfitzerGeneral Cardiology CZC. ZeugnerEast Carolina University MTMonika TroschkaHeidelberg University

Discussion

Member takes

Implication

Hypothesis-generating for caldesmon modulation of smooth muscle contraction; leaves open relevance to human vascular disease.

Structured PICO

Population

Chemically skinned gizzard muscle fiber bundles

Intervention

Caldesmon and its 20-kDa actin-binding fragment

Outcome

Force/tension developmentsurrogate

Caldesmon inhibits force production in smooth muscle fibers, suggesting it modulates contraction by increasing the myosin phosphorylation requirement rather than cross-linking myosin with actin.

Cite This Study

Pfitzer et al. (1993) studied this question.

synapsesocial.com/papers/69d92059ccb0bba5a5684397 https://doi.org/10.1073/pnas.90.13.5904

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