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Phosphorylation of Sterol Carrier Protein 2 by Protein Kinase C

  • A. Steinschneider
  • M. P. McLean
  • J. T. Billheimer
  • H. C. Palfrey
  • G. Gibori

Abstract

Ca++ has been implicated in the regulation of the steroidogenic response to tropic hormones (1–3), including the transport of cholesterol to the mitochondrial site of side-chain cleavage, a step thatmay also involve sterol carrier protein 2 (SCP2) (4). SCP2 is a cholesterol carrier that facilitates the intracellular transfer of cholesterol to cytochrome P450scc, the rate-limiting enzyme in the steroidogenic process, located in the inner mitochondrial membrane. Thus, changes in the content and/or activity of SCP2 may be expected to play a key role in cholesterol transport and, therefore, in steroidogenesis (5). SCP2 is present in nonsteroidogenic and steroidogenic tissues, including the ovary (6,7). Ovarian SCP2 closely resembles hepatic SCP2 in its amino acid composition (7) and, presumably, in its overall structure.

Keywords

Granulosa Cell Myosin Light Chain Myosin Light Chain Kinase Luteal Cell Sterol Carrier 
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 1989

Authors and Affiliations

  • A. Steinschneider
    • 1
  • M. P. McLean
    • 1
  • J. T. Billheimer
    • 2
  • H. C. Palfrey
    • 3
  • G. Gibori
    • 1
  1. 1.Department of Physiology and Biophysics, College of MedicineUniversity of IllinoisChicagoUSA
  2. 2.DuPont Experimental StationWilmingtonUSA
  3. 3.University of ChicagoChicagoUSA

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