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Titolo:
IDENTIFICATION OF A FORM OF ACYL-COA-CHOLESTEROL ACYLTRANSFERASE SPECIFIC TO LIVER AND INTESTINE IN NONHUMAN-PRIMATES
Autore:
ANDERSON RA; JOYCE C; DAVIS M; REAGAN JW; CLARK M; SHELNESS GS; RUDEL LL;
Indirizzi:
WAKE FOREST UNIV,SCH MED,DEPT COMPARAT MED WINSTON SALEM NC 27157 WAKE FOREST UNIV,SCH MED,DEPT COMPARAT MED WINSTON SALEM NC 27157 WAKE FOREST UNIV,SCH MED,DEPT BIOCHEM,ARTERIOSCLEROSIS RES PROGRAM WINSTON SALEM NC 27157 WAKE FOREST UNIV,SCH MED,DEPT INTERNAL MED WINSTON SALEM NC 27157 WAKE FOREST UNIV,SCH MED,DEPT PATHOL WINSTON SALEM NC 27157
Titolo Testata:
The Journal of biological chemistry
fascicolo: 41, volume: 273, anno: 1998,
pagine: 26747 - 26754
SICI:
0021-9258(1998)273:41<26747:IOAFOA>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
AFRICAN-GREEN MONKEYS; CORONARY-ARTERY ATHEROSCLEROSIS; APO-B SECRETION; COENZYME-A; MOLECULAR-CLONING; DIETARY-CHOLESTEROL; ACYLCOENZYME-A; ACAT; EXPRESSION; PROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
R.A. Anderson et al., "IDENTIFICATION OF A FORM OF ACYL-COA-CHOLESTEROL ACYLTRANSFERASE SPECIFIC TO LIVER AND INTESTINE IN NONHUMAN-PRIMATES", The Journal of biological chemistry, 273(41), 1998, pp. 26747-26754

Abstract

The present study demonstrates that two different forms of the intracellular cholesterol esterification enzyme acyl-CoA:cholesterol acyltransferase (ACAT) are present in the nonhuman primate hepatocyte; one issimilar to that originally cloned from human genomic DNA, here termedACAT1, while a second gene product, termed ACAT2, is reported here. The primate ACAT2 gene product was cloned from an African green monkey liver cDNA library. Sequence analysis of an isolated, full-length clone of ACAT2 cDNA identified an open reading frame encoding a 526-amino acid protein with essentially no sequence similarity to the ACAT1 cDNAover the N-terminal 101 amino acids but with 57% identity predicted over the remaining 425 amino acids. Transfection of the cloned ACAT2 cDNA into two different mammalian cell types resulted in the production of abundant ACAT activity which was sensitive to ACAT inhibitors. Northern blot analysis showed that the ACAT2 mRNA was expressed primarily in liver and intestine in monkeys. In contrast, ACAT1 mRNA was expressed in almost all tissues examined. Topologic predictions from the amino acid sequence of ACAT2 indicates that it has seven trans-membrane domains in a configuration that places the putative active site of the enzyme in the lumen of the endoplasmic reticulum. This orientation of ACAT2 in the endoplasmic reticulum membrane, in addition to its expression only in liver and intestine, suggests that this enzyme may have asa primary function, the secretion of cholesteryl esters into apoB-containing lipoproteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/06/20 alle ore 09:24:53