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Titolo:
QUANTITATIVE EXPORT OF FGF-2 OCCURS THROUGH AN ALTERNATIVE, ENERGY-DEPENDENT, NON-ER GOLGI PATHWAY/
Autore:
FLORKIEWICZ RZ; MAJACK RA; BUECHLER RD; FLORKIEWICZ E;
Indirizzi:
SCRIPPS CLIN & RES INST,DEPT CELL BIOL LA JOLLA CA 92037 WHITTIER INST DIABET & ENDOCRINOL,DEPT MOLEC & CELLULAR GROWTH BIOL LA JOLLA CA 92037 UNIV COLORADO,SCH MED,DEPT PEDIAT DENVER CO 80262 UNIV COLORADO,SCH MED,DEPT CELL & STRUCT BIOL DENVER CO 80262
Titolo Testata:
Journal of cellular physiology
fascicolo: 3, volume: 162, anno: 1995,
pagine: 388 - 399
SICI:
0021-9541(1995)162:3<388:QEOFOT>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
FIBROBLAST GROWTH-FACTOR; SUBENDOTHELIAL EXTRACELLULAR-MATRIX; PLASMINOGEN-ACTIVATOR PRODUCTION; VESICULAR STOMATITIS-VIRUS; SECRETORY SIGNAL SEQUENCE; CELL-GROWTH; ENDOTHELIAL-CELLS; ENDOPLASMIC-RETICULUM; NUCLEOTIDE-SEQUENCE; CHROMAFFIN GRANULES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
88
Recensione:
Indirizzi per estratti:
Citazione:
R.Z. Florkiewicz et al., "QUANTITATIVE EXPORT OF FGF-2 OCCURS THROUGH AN ALTERNATIVE, ENERGY-DEPENDENT, NON-ER GOLGI PATHWAY/", Journal of cellular physiology, 162(3), 1995, pp. 388-399

Abstract

Although basic fibroblast growth factor (bFGF/FGF-2) is found outsidecells, it lacks a conventional signal peptide sequence; the mechanismunderlying its export from cells is therefore unknown. Using a transient COS-l cell expression system, we have identified a novel membrane-associated transport pathway that mediates export of FGF-2. This export pathway is specific for the 18-kD isoform of FGF-2, is resistant to the anti-Golgi effects of Brefeldin A, and is energy-dependent. In FGF-2-transfected COS-1 cells, this ER/Colgi-independent pathway appears to be constitutively active and functions to quantitatively expert metabolically-labeled 18-kD FGF-2. Co-transfection and co-immunoprecipitation experiments, using a vector encoding the cytoplasmic protein neomycin phosphotransferase, further demonstrated the selectivity of this export pathway for FGF-2. When neomycin phosphotransferase was appended to the COOH-terminus of 18-kD FGF-2, the chimera was exported. However, the transmembrane anchor sequence of the integral membrane glycoprotein (G protein) of vesicular stomatitis virus (VSV) blocked export. The chimeric protein localized to the plasma membrane with its FGF-2 domain extracellular and remained cell-associated following alkaline carbonate extraction. Taken together, the data suggest that FGF-2 is ''exported'' from cells via a unique cellular pathway, which is clearly distinct from classical signal peptide-mediated secretion. This model system provides a basis for the development and testing of therapeutic agents which may block FGF-2 export. Such an intervention may be of considerable use for the treatment of angiogenesis-dependent diseases involving FGF-2. (C) 1995 Wiley-Liss, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 23:39:13