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Titolo:
HEPARIN INCREASES THE AFFINITY OF BASIC FIBROBLAST GROWTH-FACTOR FOR ITS RECEPTOR BUT IS NOT REQUIRED FOR BINDING
Autore:
ROGHANI M; MANSUKHANI A; DELLERA P; BELLOSTA P; BASILICO C; RIFKIN DB; MOSCATELLI D;
Indirizzi:
NYU MED CTR,DEPT CELL BIOL,550 1ST AVE NEW YORK NY 10016 NYU MED CTR,DEPT CELL BIOL NEW YORK NY 10016 NYU MED CTR,DEPT MICROBIOL NEW YORK NY 10016 NYU MED CTR,KAPLAN COMPREHENS CANC CTR NEW YORK NY 10016 RAYMOND & BEVERLY SACKLER LABS NEW YORK NY 10016
Titolo Testata:
The Journal of biological chemistry
fascicolo: 6, volume: 269, anno: 1994,
pagine: 3976 - 3984
SICI:
0021-9258(1994)269:6<3976:HITAOB>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLASMINOGEN-ACTIVATOR PRODUCTION; CAPILLARY ENDOTHELIAL-CELLS; FACTOR FGF RECEPTOR; SULFATE PROTEOGLYCAN; EXTRACELLULAR-MATRIX; PROTEOLYTIC DEGRADATION; 3-DIMENSIONAL STRUCTURE; PHOSPHOLIPASE-C; ACIDIC FGF; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
61
Recensione:
Indirizzi per estratti:
Citazione:
M. Roghani et al., "HEPARIN INCREASES THE AFFINITY OF BASIC FIBROBLAST GROWTH-FACTOR FOR ITS RECEPTOR BUT IS NOT REQUIRED FOR BINDING", The Journal of biological chemistry, 269(6), 1994, pp. 3976-3984

Abstract

The role of heparin or heparan sulfates in the interaction of basic fibroblast growth factor (bFGF) with its high affinity receptor were investigated using purified extracellular ligand-binding region of FGF receptor-1 (FGFR-1) and intact receptors expressed in a myeloid cell line (32D) that does not express detectable levels of heparan sulfate proteoglycans or in Chinese hamster ovary (CHO) cell mutants defective in heparan sulfate synthesis. The purified extracellular domain of FGFR-1 formed complexes with I-125-bFGF both in the presence or absence ofheparin. Intact FGFR-1 expressed in 32D cells also bound the same amount of I-125-bFGF in the presence or absence of heparin when saturating concentrations of bFGF were used. Varying the concentration of I-125-bFGF showed that heparin increased the amount of I-125-bFGF bound at low bFGF concentrations and increased the affinity of bFGF for its receptor by about 3-fold. To eliminate the possibility of alteration of bFGF properties through the chemical modification reactions, bFGF was labeled biosynthetically. The binding of biosynthetically labeled bFGF to FGFR-1 also did not require heparin. When FGFR-1 or FGFR-2 were expressed in mutant CHO cells deficient in heparan sulfate synthesis, thecells also bound I-125-bFGF in the absence of heparin, and the addition of heparin increased the affinity of bFGF for its receptors 2-3-fold. Thus, heparin or heparan sulfate is not required for the binding ofbFGF to its receptors but increases the binding affinity to a moderate degree. Finally, the requirement for heparin in signal transduction through the receptor was investigated. Expression of c-fos mRNA was induced by bFGF in 32D cells expressing FGFR-1 to the same extent in thepresence or absence of heparin.

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Documento generato il 29/11/20 alle ore 00:32:01