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Titolo:
Heparan sulfate proteoglycan modulates keratinocyte growth factor signaling through interaction with both ligand and receptor
Autore:
LaRochelle, WJ; Sakaguchi, K; Atabey, N; Cheon, HG; Takagi, Y; Kinaia, T; Day, RM; Miki, T; Burgess, WH; Bottaro, DP;
Indirizzi:
NCI, Cellular & Mol Biol Lab, Div Basic Sci, NIH, Bethesda, MD 20892 USA NCI Bethesda MD USA 20892 Lab, Div Basic Sci, NIH, Bethesda, MD 20892 USA NIDR, Glycobiol Program, NIH, Bethesda, MD 20892 USA NIDR Bethesda MD USA20892 Glycobiol Program, NIH, Bethesda, MD 20892 USA NIDDKD, Metab Dis Branch, NIH, Bethesda, MD 20892 USA NIDDKD Bethesda MD USA 20892 etab Dis Branch, NIH, Bethesda, MD 20892 USA Amer Red Cross, Holland Lab, Dept Mol Biol, Rockville, MD 20895 USA Amer Red Cross Rockville MD USA 20895 t Mol Biol, Rockville, MD 20895 USA
Titolo Testata:
BIOCHEMISTRY
fascicolo: 6, volume: 38, anno: 1999,
pagine: 1765 - 1771
SICI:
0006-2960(19990209)38:6<1765:HSPMKG>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLASMINOGEN-ACTIVATOR PRODUCTION; INFLAMMATORY BOWEL-DISEASE; AFFINITY BINDING-SITES; FIBROBLAST GROWTH; CELL-GROWTH; EXPRESSION; IDENTIFICATION; STIMULATION; MITOGENESIS; ATTACHMENT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Bottaro, DP NCI,entllular & Mol Biol Lab, Div Basic Sci, NIH, Bldg 37,Room1E24,37 Conv NCI Bldg 37,Room 1E24,37 Convent Dr,MSC 4255 Bethesda MD USA 20892
Citazione:
W.J. LaRochelle et al., "Heparan sulfate proteoglycan modulates keratinocyte growth factor signaling through interaction with both ligand and receptor", BIOCHEM, 38(6), 1999, pp. 1765-1771

Abstract

Keratinocyte growth factor (KGF) is an unusual fibroblast growth factor (FGF) family member in that its activity is largely restricted to epithelial cells, and added heparin/heparan sulfate inhibits its activity in most celltypes. The effects of heparan sulfate proteoglycan (HSPG) on binding and signaling by acidic FGF (aFGF) and KGF via the KGFR were studied using surface-bound and soluble receptor isoforms expressed in wild type and mutant Chinese hamster ovary (CHO) cells lacking HSPG. Low concentrations of added heparin (1 mu g/mL) enhanced the affinity of ligand binding to surface-boundKGFR in CHO mutants, as well as ligand-stimulated MAP kinase activation and c-fos induction, but had little effect on binding or signaling in wild type CHO cells. Higher heparin concentrations inhibited KGF, but not aFGF, binding and signaling. In addition to the known interaction between HSPG and KGF, we found that the KGFR also bound heparin. The biphasic effect of heparin on KGF, but not aFGF, binding and signaling suggests that occupancy of the HSPG binding site on the KGFR may specifically inhibit KGF signaling. In contrast to events on the cell surface, added heparin was not required for high-affinity soluble KGF-KGFR interaction. These results suggest that high-affinity ligand binding is an intrinsic property of the receptor, and that the difference between the HSPG-dependent ligand binding to receptor on cell surfaces and the HSPG-independent binding to soluble receptor may be due to other molecule(s) present on cell surfaces.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 09:57:24