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J Biol Chem, Vol. 273, Issue 11, 6410-6416, March 13, 1998

Transforming Growth Factor ₁ Decreases Cholesterol Supply to Mitochondria via Repression of Steroidogenic Acute Regulatory Protein Expression

From the Commissariat à l'Energie Atomique, Département de Biologie Moléculaire et Structurale, Biochìmìe des Régulations Cellulaires Endocrines, INSERM Unité 244, 17 rue des Martyrs, F-38054 Grenoble, France and the ^§ Division of Endocrinology and Diabetology, Department of Internal Medicine, Faculty of Medicine, University Hospital, CH-1211 Geneva 14, Switzerland

Transforming growth factor-s (TGF-s) constitute a family of dimeric proteins that affect growth and differentiation of many cell types. TGF-₁ has also been proposed to be an autocrine regulator of adrenocortical steroidogenesis, acting mainly by decreasing the expression of cytochrome P450c17. Here, we demonstrate that TGF-₁ has a second target in bovine adrenocortical cells, namely the steroidogenic acute regulatory protein (StAR). Indeed, supplying cells with steroid precursors revealed that TGF-₁ inhibited two steps in the steroid synthesis pathway, one prior to pregnenolone production and another corresponding to P450c17. More specifically, TGF-₁ inhibited pregnenolone production but neither the conversion of 25-hydroxycholesterol to pregnenolone nor P450scc activity. Thus, TGF-₁ must decrease the cholesterol supply to P450scc. We therefore examined the effect of TGF-₁ on the expression of StAR, a mitochondrial protein implicated in intramitochondrial cholesterol transport. TGF-₁ decreased the steady state level of StAR mRNA in a time- and concentration-dependent manner. This inhibition occurs at the level of StAR transcription and depends on RNA and protein synthesis. It is likely that the TGF-₁-induced decrease of StAR expression that we report here may be expanded to other steroidogenic cells in which a decrease of cholesterol accessibility to P450scc by TGF-₁ has been hypothesized.

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