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Related Experiment Videos

Chicken gizzard: relation between calcium-activated phosphorylation and contraction.

P E Hoar, W G Kerrick, P S Cassidy

    Science (New York, N.Y.)
    |May 4, 1979
    PubMed
    Summary

    Chicken gizzard myosin light chains showed Ca2+ and Sr2+ dependent phosphorylation linked to muscle tension. ATP analogs induced irreversible tension and blocked phosphorylation, revealing key regulatory mechanisms.

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    Area of Science:

    • Muscle physiology
    • Biochemistry

    Background:

    • Mechanically disrupted chicken gizzard fibers lack a functional sarcolemma.
    • Protein phosphorylation plays a crucial role in regulating muscle contraction.

    Purpose of the Study:

    • To investigate the role of protein phosphorylation in chicken gizzard muscle tension.
    • To identify specific proteins involved in Ca2+- and Sr2+-dependent phosphorylation and tension.

    Main Methods:

    • Analysis of protein phosphorylation in mechanically disrupted chicken gizzard fibers.
    • Measurement of Ca2+- and Sr2+-activated tensions.
    • Use of adenosine 5'-O-(3'-thiotriphosphate) and [gamma-32P]adenosine triphosphate to study phosphorylation dynamics.

    Main Results:

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  • Only the 20,000-dalton light chains of myosin exhibited significant Ca2+- and Sr2+-dependent phosphorylation.
  • Phosphorylation levels closely correlated with activated muscle tensions.
  • Adenosine 5'-O-(3'-thiotriphosphate) induced irreversible, Ca2+-insensitive tension and thiophosphorylation of myosin light chains, while blocking further 32P incorporation.

    • Conclusions:

    • The 20,000-dalton myosin light chains are key regulators of Ca2+- and Sr2+-dependent tension in chicken gizzard fibers.
    • Myosin light chain phosphorylation is directly linked to muscle force generation.
    • ATP analogs can irreversibly activate tension and alter phosphorylation, highlighting regulatory pathways.