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The Role of Protein Phosphorylation in the Response of Dihydropyridine-Sensitive Calcium Channels to Membrane Depolarization in Mammalian Pituitary Tumor Cells

  • Chapter
Calcium and Ion Channel Modulation

Abstract

The phosphorylation and dephosphorylation of serine and threonine alters the activity of a wide variety of proteins that contribute to the characteristic structure and function of cells in the brain (Nestler & Greengard, 1986). In fact, since electric fields act only on charged molecules, it may seem obvious in retrospect that adding or removing a densely charged phosphate group should alter the response of ion channels to changes in the voltage across the membrane. In that regard it is interesting to note that, despite the striking structural homology in the putative membrane spanning portions of voltage-activated sodium and calcium channel proteins (Tanabe et al., 1987), only sodium channels continue to respond to depolarization when the cell’s cytoplasm is replaced with artificial saline solutions lacking the ingredients to support protein phosphorylation (Baker et al., 1962; Hagiwara & Nakajima, 1966). The recent advances in electrophysiological techniques which allow one to observe the current passing through individual ion channels in cell-free patches of native membrane (Hamill et al., 1981) have made it possible to investigate such differences directly by studying the phosphorylation-dependent alterations in ion channel activity produced by purified kinases and phosphatases and inhibitors of their native counterparts. We have used this approach to study the role of protein phosphorylation in the regulation of a prominent class of voltageactivated calcium channels in cells derived from a rat pituitary tumor (GH3; Tashjian, 1979).

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Author information

Authors and Affiliations

  1. Department of Biology, UCLA, Los Angeles, California, USA

    David Armstrong & Daniel Kalman

  2. Laboratory of Cellular and Molecular Pharmacology, National Institute of Environmental Health Sciences Research, Triangle Park, North Carolina, USA

    David Armstrong

Authors
  1. David Armstrong
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  2. Daniel Kalman
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Editor information

Editors and Affiliations

  1. UCLA School of Medicine, Los Angeles, California, USA

    Alan D. Grinnell

  2. National Institute of Environmental Health Sciences, Research Triangle, North Carolina, USA

    David Armstrong

  3. University of California, Los Angeles, Los Angeles, California, USA

    Meyer B. Jackson

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© 1988 Plenum Press, New York

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Armstrong, D., Kalman, D. (1988). The Role of Protein Phosphorylation in the Response of Dihydropyridine-Sensitive Calcium Channels to Membrane Depolarization in Mammalian Pituitary Tumor Cells. In: Grinnell, A.D., Armstrong, D., Jackson, M.B. (eds) Calcium and Ion Channel Modulation. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0975-8_17

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  • DOI: https://doi.org/10.1007/978-1-4613-0975-8_17

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4612-8273-0

  • Online ISBN: 978-1-4613-0975-8

  • eBook Packages: Springer Book Archive

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