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Titolo:
STEROL CARRIER PROTEIN-2 - A ROLE IN STEROID-HORMONE SYNTHESIS
Autore:
PFEIFER SM; FURTH EE; OHBA T; CHANG YJ; RENNERT H; SAKURAGI N; BILLHEIMER JT; STRAUSS JF;
Indirizzi:
UNIV PENN,DEPT OBSTET & GYNECOL PHILADELPHIA PA 19104 UNIV PENN,DEPT OBSTET & GYNECOL PHILADELPHIA PA 19104 UNIV PENN,DEPT PATHOL & LAB MED PHILADELPHIA PA 19104 DUPONT MERCK PHARMACEUT CO,EXPTL STN WILMINGTON DE 19880
Titolo Testata:
Journal of steroid biochemistry and molecular biology
fascicolo: 1-6, volume: 47, anno: 1993,
pagine: 167 - 172
SICI:
0960-0760(1993)47:1-6<167:SCP-AR>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
STEROIDOGENESIS-ACTIVATOR POLYPEPTIDE; LIPID TRANSFER PROTEINS; SIDE-CHAIN CLEAVAGE; RAT ADRENAL-CORTEX; BENZODIAZEPINE RECEPTOR; REGULATED EXPRESSION; CELLS; MITOCHONDRIAL; CDNA; CHOLESTEROL;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
S.M. Pfeifer et al., "STEROL CARRIER PROTEIN-2 - A ROLE IN STEROID-HORMONE SYNTHESIS", Journal of steroid biochemistry and molecular biology, 47(1-6), 1993, pp. 167-172

Abstract

The intracellular movement of cholesterol is an important regulated step in the process of steroidogenesis. However, the molecular mechanisms by which cholesterol is translocated to key organelles, including the mitochondria, remains poorly understood. Lipid transfer proteins may have an important function in this process. One candidate lipid transfer protein is sterol carrier protein 2 (SCP2). This 13.2 kDa proteinenhances the movement of cholesterol between vesicles and isolated mitochondria. It also stimulates mitochondrial pregnenolone synthesis. When introduced into intact cells, anti-SCP2 antibodies reduce steroid secretion. Moreover, expression of SCP2 in COS cells engineered to produce progestins increases steroid formation. SCP2 is abundant in steroidogenic glands and the pattern of SCP2 gene expression is consistent with a role for the protein in hormone synthesis: SCP2 transcripts aremore prominent in the most steroidogenic compartments of the ovary and tropic hormones that stimulate steroidogenesis increase SCP2 gene expression. Other evidence that suggests that SCP2 plays important rolesin cellular function includes a remarkable conservation of primary structure across species. The mechanisms by which SCP2 promotes intracellular sterol movement have not been elucidated. The protein appears tobind sterols and is synthesized with a 20 amino acid N-terminal ''pro-'' sequence that may serve to target SCP2 to mitochondria. In addition, the C-terminus of SCP2 contains a peroxisome-targeting sequence. SCP2 is derived from a large gene that encodes transcripts that are translated into larger proteins of 30 and 58 kDa. The 58 kDa protein, which has some structural homologies with thiolases, seems to be specifically targeted to peroxisomes whereas SCP2 has a broader subcellular distribution. The significance of the peroxisome association of SCP2 and steroidogenesis has not been disclosed. However, diseases of peroxisome function, including adrenoleukodystrophy and Zellweger syndrome, have notable deficits in steroid and bile acid metabolism, thus linking peroxisomes and steroidogenesis. SCP2 is deficient in fibroblasts of patients with these diseases.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/11/20 alle ore 11:24:08