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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

  • David Armstrong
  • Daniel Kalman

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).

Keywords

Calcium Channel Calcium Current Large Conductance Channel Barium Current Sensitive Calcium Channel 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • David Armstrong
    • 1
    • 2
  • Daniel Kalman
    • 1
  1. 1.Department of BiologyUCLALos AngelesUSA
  2. 2.Laboratory of Cellular and Molecular PharmacologyNational Institute of Environmental Health Sciences ResearchTriangle ParkUSA

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