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Titolo:
RETARDATION OF A SURFACE PROTEIN CHIMERA AT THE CIS GOLGI
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
Titolo Testata:
Biochemistry
fascicolo: 16, volume: 34, anno: 1995,
pagine: 5618 - 5626
SICI:
0006-2960(1995)34:16<5618:ROASPC>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
DIPEPTIDYL PEPTIDASE-IV; APICAL CELL-SURFACE; BETA-GALACTOSIDE ALPHA-2,6-SIALYLTRANSFERASE; POLARIZED EPITHELIAL-CELLS; MEMBRANE-SPANNING DOMAIN; CANINE KIDNEY-CELLS; ENDOPLASMIC-RETICULUM; BREFELDIN-A; TRANSMEMBRANE DOMAIN; MDCK CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
56
Recensione:
Indirizzi per estratti:
Citazione:
S.H. Low et al., "RETARDATION OF A SURFACE PROTEIN CHIMERA AT THE CIS GOLGI", Biochemistry, 34(16), 1995, pp. 5618-5626

Abstract

Dipeptidyl peptidase IV (D4) and the alpha subunit of human chorionicgonadotrophin (alpha hcg) are plasma membrane and secretory proteins,respectively. In the course of studies to understand mechanisms involved in transport along the exocytotic pathway, the ectoplasmic domain of D4 was replaced by the mature polypeptide of alpha hcg, resulting in the membrane anchored chimera, D4 alpha hcg. Surprisingly, when transfected into Chinese hamster ovary (CHO) and Madin-Darby canine kidney(MDCK) cells, strong perinuclear Golgi staining was predominant, in addition to the expected surface staining. By following the biogenesis and transport of the molecule, it was established that newly synthesized D4 alpha hdg is eventually transported to the cell surface but onlyafter a significant retardation in the Golgi apparatus. The compartment of retardation was identified as the early or cis Golgi, before themedial Golgi, where resistance to endoglycosidase (endo) H is conferred. As a result of the transport retardation of the chimera, we were able to document the appearance of an endo D sensitive intermediate, which is usually too transient to be apparent in normal cells. The retardation of this chimera in the cis Golgi complements our previous report in which the D4 molecule with its transmembrane domain replaced by that of aminopeptidase N resulted in retardation in the trans Golgi/trans Golgi network in MDCK and CHO cells [Low, S. H., Tang, B. L., Wong,S. H., and Hong, W. (1994) J. Biol. Chem. 269, 1985-1994). Together, these reports indicate that transport along the exocytic pathway may not be simply by default but requires some sort of signal, the disruption of which results in inefficient intra-Golgi and/or Golgi to surfacetransport.

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Documento generato il 20/09/20 alle ore 00:39:53