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J Biol Chem, Vol. 273, Issue 41, 26285-26288, October 9, 1998
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From the Steroidogenic acute regulatory protein (StAR)
plays a critical role in steroidogenesis by enhancing the delivery of
substrate cholesterol from the outer mitochondrial membrane to the
cholesterol side chain cleavage enzyme system on the inner membrane. A
recombinant StAR protein lacking the first N-terminal 62 amino acid
residues that includes the mitochondrial targeting sequence was shown
to stimulate the transfer of cholesterol and Center for Research on Reproduction and
Women's Health, the ** Department of Biochemistry and Biophysics, and
the Howard Hughes Medical Institute, University of Pennsylvania
Medical Center, Philadelphia, Pennsylvania 19104 and
¶ Dupont-Merck, Wilmington, Delaware 19880
-sitosterol from
liposomes to heat-treated mitochondria in a dose-, time-, and
temperature-dependent manner. A recombinant mutant StAR
protein that cannot stimulate steroidogenesis by isolated mitochondria
did not promote sterol transfer. Unlike the more promiscuous lipid
transfer protein, sterol carrier protein 2 (SCP2),
StAR did not stimulate phosphatidylcholine transfer in our assay
system. The recombinant StAR protein increased cholesterol transfer to
heat-treated microsomes as well as to heat- and trypsin-treated
mitochondria. These observations demonstrate that StAR has sterol
transfer activity, which may reflect an ability to enhance desorption
of cholesterol from sterol-rich donor membranes. We suggest that the
ability of StAR to promote sterol transfer explains its steroidogenic
activity.
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