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Ca2+-activated ATPase and ATP-dependent calmodulin-stimulated Ca2+ transport in islet cell plasma membrane

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Abstract

Calcium is known to play an essential part in the regulation of insulin secretion in the pancreatic β cell1,2. Calcium influx/efflux studies indicate that glucose promotes an accumulation of calcium by the β cell2. However, interpretation of such data is particularly difficult due to the complex compartmentalization of calcium within the cell. Although indirect evidence using chlorotetracycline suggests that control of calcium homeostasis at the plasma membrane may be central to insulin secretion3, the mechanism by which secretagogues influence the handling of calcium remains unknown. Despite its continuous diffusive entry, intracellular calcium is maintained in the submicromolar range4,5 by energy-dependent mechanisms5–9. One such process which has been well characterized in erythrocytes is a plasma membrane calcium extrusion pump whose enzymatic basis is a high affinity (Ca2+ + Mg2+) ATPase9. A similar mechanism10,11 regulated by insulin12,13 has recently been identified in adipocyte plasma membranes. We report here the presence of a high affinity (Ca2+ + Mg2+) ATPase and ATP-dependent calmodulin-stimulated calcium transport system in rat pancreatic islet cell plasma membranes14.

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Author notes

  1. Harrihar A. Pershadsingh

    Present address: University of Missouri-Columbia, School of Medicine, Columbia, Missouri, 65212

Authors and Affiliations

  1. Division of Laboratory Medicine, Departments of Pathology and Medicine, Washington University School of Medicine, St Louis, Missouri, 63110

    Harrihar A. Pershadsingh, Michael L. McDaniel, Michael Landt, Cheryl G. Bry, Paul E. Lacy & Jay M. McDonald

Authors
  1. Harrihar A. Pershadsingh
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  2. Michael L. McDaniel
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  3. Michael Landt
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  4. Cheryl G. Bry
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  5. Paul E. Lacy
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  6. Jay M. McDonald
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Pershadsingh, H., McDaniel, M., Landt, M. et al. Ca2+-activated ATPase and ATP-dependent calmodulin-stimulated Ca2+ transport in islet cell plasma membrane. Nature 288, 492–495 (1980). https://doi.org/10.1038/288492a0

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