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Titolo:
HISTIDINE-RICH GLYCOPROTEIN AND PLATELET FACTOR-4 MASK HEPARAN-SULFATE PROTEOGLYCANS RECOGNIZED BY ACIDIC AND BASIC FIBROBLAST GROWTH-FACTOR
Autore:
BROWN KJ; PARISH CR;
Indirizzi:
AUSTRALIAN NATL UNIV,JOHN CURTIN SCH MED RES,DIV CELL BIOL CANBERRA ACT 2601 AUSTRALIA
Titolo Testata:
Biochemistry
fascicolo: 46, volume: 33, anno: 1994,
pagine: 13918 - 13927
SICI:
0006-2960(1994)33:46<13918:HGAPFM>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLASMINOGEN-ACTIVATOR PRODUCTION; ANTITHROMBIN-BINDING SEQUENCE; AUTOROSETTE INHIBITION-FACTOR; ALPHA-GRANULE RELEASE; HUMAN SERUM-PROTEINS; EXTRACELLULAR-MATRIX; 3-DIMENSIONAL STRUCTURE; ENDOTHELIAL-CELLS; HIGH-AFFINITY; FACTOR-IV;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
56
Recensione:
Indirizzi per estratti:
Citazione:
K.J. Brown e C.R. Parish, "HISTIDINE-RICH GLYCOPROTEIN AND PLATELET FACTOR-4 MASK HEPARAN-SULFATE PROTEOGLYCANS RECOGNIZED BY ACIDIC AND BASIC FIBROBLAST GROWTH-FACTOR", Biochemistry, 33(46), 1994, pp. 13918-13927

Abstract

Recent studies have shown that fibroblast growth factors (FGFs) need to interact with cell-surface heparan sulfate proteoglycans (HSPGs) inorder to bind to and activate FGF receptors. In this paper, three major heparin-binding proteins, histidine-rich glycoprotein (HRG) and antithrombin III (ATIII), which are constitutively present at high concentrations in plasma, and platelet factor 4 (PF4), which is released locally at high concentrations by degranulating platelets, were tested for their ability to act as modulators of FGF activity by competing withthe FGFs for cell-surface HSPGs. HRGs from both chicken and human, and human PF4, were demonstrated to compete with each other and with acidic FGF (aFGF) and basic FGF (bFGF) for binding to BALB/c 3T3 cell-surface HSPGs,whereas ATIII did not compete. Thus, HRG, PF4, aFGF, and bFGF all interact with the same HS chains on the 3T3 cell surface, either binding to the same or binding to adjacent saccharide sequences on the chains. In terms of their relative binding affinity for cell-surface HSPGs, the hierachy was shown to be PF4 greater than or equal to bFGF > aFGF = cHRG > hRG. HRG was also shown to significantly inhibit both FGF-stimulated and endogenous 3T3 cell DNA synthesis. HRG also bindsto extracellular matrices (ECM), originating from bovine corneal endothelial cells, in a heparin-inhibitable manner. Indeed, both HRG and PF4, at physiological concentrations, were shown to effectively inhibitthe binding of I-125-aFGF and I-125-bFGF to ECM. In addition, HRG wasable to displace biologically active bFGF from the ECM. On the basis of these findings, it is proposed that HRG and PF4 may act as positiveregulators of FGF activity by displacing FGF from the ECM or basementmembrane and making FGF available to responsive cells. Alternatively,they could act as negative regulators by masking HSPGs on responsive cells and preventing FGF receptor activation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 18:10:55