Mitochondrial biosynthesis of cholesterol in leydig cells from rat testis

The subcellular location of some enzymes responsible for cholesterol biosynthesis was studied in metrizamide-purified rat Leydig cells.The highest activity of 3-hydroxy-3-methyl glutaryl coenzyme A reductase (HMG-CoA reductase), a key regulatory enzyme in the cholesterol pathway, was associated with...

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Autor principal: Pignataro, O.P
Otros Autores: Radicella, J.P, Calvo, J.C, Charreau, E.H
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 1983
Acceso en línea:Registro en Scopus
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Registro en la Biblioteca Digital
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024 7 |2 cas  |a hydroxymethylglutaryl coenzyme A reductase, 37250-24-1; Acetates; Acetyl Coenzyme A, 72-89-9; Cholesterol, 57-88-5; Hydroxymethylglutaryl CoA Reductases, EC 1.1.1.- 
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100 1 |a Pignataro, O.P. 
245 1 0 |a Mitochondrial biosynthesis of cholesterol in leydig cells from rat testis 
260 |c 1983 
270 1 0 |m Pignataro, O.P. 
506 |2 openaire  |e Política editorial 
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504 |a Moyle, Jungas, Greep, Metabolism of free and esterified cholesterol by Leydig-cell tumour mitochondria. (1973) Biochem J, 134, pp. 415-424 
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504 |a Payne, Downing, Wong, (1980) Endocrinology, 106, pp. 1424-1429 
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504 |a van der Vusse, Kalkman, van der Molen, 3β-Hydroxysteroid dehydrogenase in rat testis tissue inter- and subcellular localization and inhibition by cyanoketone and nagarse (1974) Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 348, pp. 404-414 
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520 3 |a The subcellular location of some enzymes responsible for cholesterol biosynthesis was studied in metrizamide-purified rat Leydig cells.The highest activity of 3-hydroxy-3-methyl glutaryl coenzyme A reductase (HMG-CoA reductase), a key regulatory enzyme in the cholesterol pathway, was associated with highly enriched mitochondrial fractions with recovery of 62% of the total activity and was located on the inner membrane. A significant part of the activity (35%) was also present in the cytoplasm. The activity of this enzyme in the other subcellular fractions was negligible. The HMG-CoA synthase activity was also found almost entirely in the mitochondria (90%). Otherwise no detectable activity of HMG-CoA lyase was present in the subcellular fractions studied. Furthermore, cholesterol may be synthesized from acetyl-CoA inside the mitochondrion, since a significant incorporation (90%) of [14C]acetyl-CoA into digitonin-precipitable sterols was observed in this organelle and only 10% in the cytoplasmic fraction. The evidence strongly suggests that much of the cholesterol biosynthesis that takes place in Leydig cells is carried out within the mitochondria. © 1983.  |l eng 
593 |a Instituto de Biologia y Medicina Experimental and Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Obligado 2490, 1428 Buenos AiresArgentina 
690 1 0 |a CHOLESTEROL BIOSYNTHESIS 
690 1 0 |a HMG-COA REDUCTASE 
690 1 0 |a LEYDIG CELL 
690 1 0 |a HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE 
690 1 0 |a RADIOISOTOPE 
690 1 0 |a ACETYL COENZYME A C 14 
690 1 0 |a ANIMAL EXPERIMENT 
690 1 0 |a BIOLOGICAL MODEL 
690 1 0 |a CHOLESTEROL SYNTHESIS 
690 1 0 |a ENDOCRINE SYSTEM 
690 1 0 |a LEYDIG CELL 
690 1 0 |a MALE GENITAL SYSTEM 
690 1 0 |a MITOCHONDRION 
690 1 0 |a NONHUMAN 
690 1 0 |a RAT 
690 1 0 |a ACETATES 
690 1 0 |a ACETYL COENZYME A 
690 1 0 |a ANIMAL 
690 1 0 |a CELL COMPARTMENTATION 
690 1 0 |a CHOLESTEROL 
690 1 0 |a HYDROXYMETHYLGLUTARYL COA REDUCTASES 
690 1 0 |a LEYDIG CELLS 
690 1 0 |a MALE 
690 1 0 |a MITOCHONDRIA 
690 1 0 |a RATS 
690 1 0 |a SUPPORT, NON-U.S. GOV'T 
700 1 |a Radicella, J.P. 
700 1 |a Calvo, J.C. 
700 1 |a Charreau, E.H. 
773 0 |d 1983  |g v. 33  |h pp. 53-67  |k n. 1  |x 03037207  |w (AR-BaUEN)CENRE-6138  |t Mol. Cell. Endocrinol. 
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