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Titolo:
A common binding site on the microsomal triglyceride transfer protein for apolipoprotein B and protein disulfide isomerase
Autore:
Bradbury, P; Mann, CJ; Kochl, S; Anderson, TA; Chester, SA; Hancock, JM; Ritchie, PJ; Amey, J; Harrison, GB; Levitt, DG; Banaszak, LJ; Scott, J; Shoulders, CC;
Indirizzi:
Univ,London Imperial Coll Sci Technol & Med, Hammersmith Hosp, Ctr Clin Sci Univ London Imperial Coll Sci Technol & Med London England W12 0NN n Sci Univ,London Imperial Coll Sci Technol & Med, Hammersmith Hosp, Ctr Clin Sci Univ London Imperial Coll Sci Technol & Med London England W12 0NN n Sci Univ London Imperial Coll Sci Technol & Med, Hammersmith Hosp, Natl Heart & Univ London Imperial Coll Sci Technol & Med London England W12 0NN art & Inst Gerichtliche Med, A-6020 Innsbruck, Austria Inst Gerichtliche Med Innsbruck Austria A-6020 A-6020 Innsbruck, Austria Univ Minnesota, Sch Med, Dept Biochem, Minneapolis, MN 55455 USA Univ Minnesota Minneapolis MN USA 55455 iochem, Minneapolis, MN 55455 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 5, volume: 274, anno: 1999,
pagine: 3159 - 3164
SICI:
0021-9258(19990129)274:5<3159:ACBSOT>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
UBIQUITIN-PROTEASOME PATHWAY; CONTAINING LIPOPROTEINS; ABETALIPOPROTEINEMIA GENE; HEPG2 CELLS; VITELLOGENIN; DEGRADATION; EXPRESSION; SECRETION; SEQUENCE; PRODUCT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
26
Recensione:
Indirizzi per estratti:
Indirizzo: Shoulders, CC Univ,London Imperial Coll Sci Technol & Med, Hammersmith Hosp, Ctr Clin Sci Univ London Imperial Coll Sci Technol & Med Du Cane Rd London England W12 0NN
Citazione:
P. Bradbury et al., "A common binding site on the microsomal triglyceride transfer protein for apolipoprotein B and protein disulfide isomerase", J BIOL CHEM, 274(5), 1999, pp. 3159-3164

Abstract

The assembly of triglyceride-rich lipoproteins requires the formation in the endoplasmic reticulum of a complex between apolipoprotein B (apoB), a microsomal triglyceride transfer protein (MTP), and protein disulfide isomerase (PDI). In the MTP complex, the aminoterminal region of MTP (residues 22-303) interacts with the amino-terminal region of apoB (residues 1-264). Here, we report the identification and characterization of a site on apoB between residues 512 and 721, which interacts with residues 517-603 of MTP. PDIbinds in close proximity to this apoB binding site on MTP. The proximity of these binding sites on MTP for PDI and amino acids 512-721 of apoB was evident from studies carried out in a yeast two-hybrid system and by coimmunoprecipitation. The expression of PDI with MTP and apoB16 (residues 1-721) in the baculovirus expression system reduced the amount of MTP co-immunoprecipitated with apoB by 73%. The interaction of residues 512-721 of apoB withMTP facilitates lipoprotein production. Mutations of apoB that markedly reduced this interaction also reduced the level of apoB-containing lipoprotein secretion.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/09/20 alle ore 00:46:09