May 1, 1987AJP Cell Physiology

Effects of Ca2+, Mg2+, and myosin phosphorylation on skinned smooth muscle fibers

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Population

Skinned chicken gizzard fibers

Comparison

Various Ca2+ concentrations, two concentrations… vs Different concentrations of Ca2+ and Mg2+ within…

Design

Preclinical

Authors

RBRobert BarsottiPhiladelphia College of Osteopathic Medicine MIMitsuo IkebeGeneral Cardiology DHDavid J. HartshorneRutgers, The State University of New Jersey

Discussion

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Implication

Caution against clinical translation; leaves open how Mg2+-Ca2+ myosin interactions affect human cardiac contractility.

Structured PICO

Population

Skinned chicken gizzard fibers

Intervention

Various Ca2+ concentrations, two concentrations of free Mg2+ (0.7 and 2.2 mM), and incubation with Ca2+-independent kinase (approximately 3 microM)

Comparator

Different concentrations of Ca2+ and Mg2+ within the experimental setup

Outcome

Isometric tension, unloaded shortening velocity (Vus), and myosin light chain phosphorylationsurrogate

The study suggests that Ca2+ binding to the Ca2+-Mg2+ sites of myosin increases unloaded shortening velocity at Ca2+ concentrations higher than those necessary to saturate calmodulin.

Cite This Study

Barsotti et al. (1987) studied this question.

synapsesocial.com/papers/6a7f31abfc226ad0a00dfbd3 https://doi.org/10.1152/ajpcell.1987.252.5.c543

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Effects of Ca2+, Mg2+, and myosin phosphorylation on skinned smooth muscle fibers

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Effects of Ca2+, Mg2+, and myosin phosphorylation on skinned smooth muscle fibers

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider