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Titolo:
SECRETION FROM CELL-CULTURE OF HDL AND VLDL BEARING APO-B-33 WITH A LARGE INTERNAL DELETION
Autore:
WU MJ; CHENLIU LW; XIAO QN; PHILLIPS ML; ELOVSON J; LINTON MF; YOUNG SG; SCHUMAKER VN;
Indirizzi:
UNIV CALIF LOS ANGELES,DEPT CHEM & BIOCHEM LOS ANGELES CA 90095 UNIV CALIF LOS ANGELES,DEPT CHEM & BIOCHEM LOS ANGELES CA 90095 UNIV CALIF LOS ANGELES,INST MOL BIOL LOS ANGELES CA 90095 W LOS ANGELES VET AFFAIRS MED CTR LOS ANGELES CA 90073 UNIV CALIF SAN FRANCISCO,DEPT MED,INST CARDIOVASC RES,GLADSTONE FDN LABS CARDIOVASC DIS SAN FRANCISCO CA 94141
Titolo Testata:
Journal of lipid research
fascicolo: 12, volume: 38, anno: 1997,
pagine: 2473 - 2482
SICI:
0022-2275(1997)38:12<2473:SFCOHA>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
LOW-DENSITY LIPOPROTEINS; APOLIPOPROTEIN-B-GENE; TRIGLYCERIDE-RICH LIPOPROTEINS; RAT-LIVER; FAMILIAL HYPOBETALIPOPROTEINEMIA; PLASMA-LIPOPROTEINS; 2-STEP MODEL; EXPRESSION; MUTATION; CONFORMATION;
Keywords:
VERY LOW DENSITY LIPOPROTEINS; LOW DENSITY LIPOPROTEINS; LIPOPROTEIN BIOSYNTHESIS; APOLIPOPROTEIN B; MICROSOMAL TRIGLYCERIDE TRANSFER PROTEINS;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
M.J. Wu et al., "SECRETION FROM CELL-CULTURE OF HDL AND VLDL BEARING APO-B-33 WITH A LARGE INTERNAL DELETION", Journal of lipid research, 38(12), 1997, pp. 2473-2482

Abstract

Rat hepatoma McA-RH7777 cells synthesize and secrete two populations of apoB-containing lipoproteins: a larger, VLDL-sized population floating in the S-f 40-150 range and a smaller, LDL and HDL-sized population. Three permanently transfected cell lines of McA-RH7777 cells secreted (in addition to the endogenous lipoproteins) lipoproteins containing 1) a carboxyl-terminally truncated human apoB-53 (2377 amino acids in length); 2) a carboxyl-terminally truncated human apoB-31 (1420 amino acids in length); or 3) an internally deleted human apoB protein, apoB-18/95, containing a total of 1490 amino acid residues, equivalent in length to an apoB-33. The apoB-18/95 protein contained amino acid residues 1-782 joined to 708 residues near the C-terminus of apoB (residues 3636-4343). All three of the apoB peptides, apoB-53, apoB-31, and apoB-18/95, were present on smaller LDL-HCL-class lipoproteins, with buoyant densities in the HDL density range. The sizes of the HDL class lipoproteins agreed with prior observations that lipoprotein core circumference is directly proportional to apoB size. As HDL containing apoB-18/95 conformed to this rule, contiguous apoB amino acid sequence isnot required for the rule to be obeyed. In addition, apoB-18/95, but not apoB-31, was also present on the VLDL-sized lipoproteins even in the absence of serum or oleate supplementation. As the latter two constructs encode equally sized apoB peptides, their particular amino acid sequences rather than just overall length must determine whether they can assemble into a VLDL particle.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 16:07:09