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.
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© 1989 Plenum Press, New York
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Steinschneider, A., McLean, M.P., Billheimer, J.T., Palfrey, H.C., Gibori, G. (1989). Phosphorylation of Sterol Carrier Protein 2 by Protein Kinase C. In: Hirshfield, A.N. (eds) Growth Factors and the Ovary. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5688-2_55
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DOI: https://doi.org/10.1007/978-1-4684-5688-2_55
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