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Ca-ATPases in pancreatic islets.

K Capito, B Formby, C J Hedeskov

    Hormone and Metabolic Research. Supplement Series
    |January 1, 1980
    PubMed
    Summary
    This summary is machine-generated.

    This study investigated calcium-dependent ATPase (Ca-ATPase) in mouse pancreatic islets, revealing high- and low-affinity forms. Inhibitors like cyclic AMP and caffeine affected Ca-ATPase, impacting calcium transport and insulin release regulation.

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    Area of Science:

    • Biochemistry
    • Cell Biology
    • Endocrinology

    Background:

    • Calcium-dependent ATPase (Ca-ATPase) plays a crucial role in cellular calcium homeostasis.
    • Understanding Ca-ATPase activity in pancreatic islets is vital for elucidating insulin secretion mechanisms.

    Purpose of the Study:

    • To characterize Mg-independent Ca-ATPase activity in various mouse islet subfractions.
    • To investigate the effects of different modulators on Ca-ATPase and calcium uptake in secretory granules.

    Main Methods:

    • Measurement of Mg-independent Ca-ATPase activity in secretory granules, mitochondria, and microsomes.
    • Assessment of 45Ca uptake in isolated secretory granules from ob/ob mouse islets.
    • Evaluation of inhibitor effects on Ca-ATPase and calcium transport.

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    Main Results:

    • Two forms of Ca-ATPase (high- and low-affinity) were identified in islet subfractions.
    • Cyclic AMP, caffeine, and Na+ inhibited high-affinity Ca-ATPase.
    • Alloxan stimulated microsomal Ca-ATPase, while NADH inhibited secretory granule Ca-ATPase.
    • pCMBS and chlorpromazine abolished 45Ca uptake in secretory granules.

    Conclusions:

    • Ca-ATPase is present in multiple forms within mouse pancreatic islets, with distinct regulatory properties.
    • Specific inhibitors significantly impact Ca-ATPase activity and calcium transport, suggesting a role in insulin release regulation.