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Titolo:
GOLGI RETARDATION IN MADIN-DARBY CANINE KIDNEY AND CHINESE-HAMSTER OVARY CELLS OF A TRANSMEMBRANE CHIMERA OF 2 SURFACE-PROTEINS
Autore:
LOW SH; TANG BL; WONG SH; HONG WJ;
Indirizzi:
NATL UNIV SINGAPORE,INST MOLEC & CELL BIOL,MEMBRANE BIOL LAB,10 KENT RIDGE CRESCENT SINGAPORE 0511 SINGAPORE NATL UNIV SINGAPORE,INST MOLEC & CELL BIOL,MEMBRANE BIOL LAB,10 KENT RIDGE CRESCENT SINGAPORE 0511 SINGAPORE
Titolo Testata:
The Journal of biological chemistry
fascicolo: 3, volume: 269, anno: 1994,
pagine: 1985 - 1994
SICI:
0021-9258(1994)269:3<1985:GRIMCK>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
DIPEPTIDYL PEPTIDASE-IV; ASPARAGINE-LINKED OLIGOSACCHARIDES; BETA-GALACTOSIDE ALPHA-2,6-SIALYLTRANSFERASE; ROUGH ENDOPLASMIC-RETICULUM; MEMBRANE-PROTEIN; AMINOPEPTIDASE-N; RETENTION; TRANSPORT; APPARATUS; DOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
53
Recensione:
Indirizzi per estratti:
Citazione:
S.H. Low et al., "GOLGI RETARDATION IN MADIN-DARBY CANINE KIDNEY AND CHINESE-HAMSTER OVARY CELLS OF A TRANSMEMBRANE CHIMERA OF 2 SURFACE-PROTEINS", The Journal of biological chemistry, 269(3), 1994, pp. 1985-1994

Abstract

Dipeptidyl peptidase IV (DDD) is a type II plasma membrane protein. Replacement of its transmembrane domain with that of another surface protein, aminopeptidase N, resulted in accumulation in the Golgi apparatus of Madin-Darby canine kidney cells and a delayed Golgi to surface transport in Chinese hamster ovary (CHO) cells. The compartment of retardation was identified as post medial-Golgi, most likely to be the trans-Golgi/trans Golgi network (TGN). Compared to native DDD, the rate of endoplasmic reticulum to Golgi transport for the chimera was largelyunchanged in both cell types. On the other hand, Golgi to surface transport was delayed by more than 2 h in CHO cells and essentially undetectable up to 22 h of chase in Madin-Darby canine kidney cells. The decrease in the rate of Golgi to surface transport in CHO cells resultedin a significant accumulation of the fusion protein in the trans-Golgi/TGN. This phenomena is very unlikely to be due to any drastic conformational changes, as neither the enzyme activity nor the dimerization of the constructed molecule was affected. The findings of this study indicate that the transmembrane domain, in the context of its flanking sequences, is important for efficient Golgi to cell surface transport.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 22:10:27