Identification of Binding Domains for Basic Fibroblast Growth Factor in Proteoglycan Macrophage Colony-Stimulating Factor

1997 ◽  
Vol 230 (2) ◽  
pp. 392-397 ◽  
Author(s):  
Shinya Suzu ◽  
Fumihiko Kimura ◽  
Hiroshi Matsumoto ◽  
Muneo Yamada ◽  
Koichi Hashimoto ◽  
...  
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Basic Fibroblast Growth Factor ◽  
Fibroblast Growth ◽  
Colony Stimulating Factor ◽  
Binding Domains ◽  
Macrophage Colony Stimulating Factor ◽  
Macrophage Colony ◽  
Stimulating Factor

scholarly journals Direct interaction of proteoglycan macrophage colony-stimulating factor and basic fibroblast growth factor

Blood ◽  
1994 ◽  
Vol 83 (11) ◽  
pp. 3113-3119 ◽  
Author(s):  
S Suzu ◽  
F Kimura ◽  
M Yamada ◽  
N Yanai ◽  
T Kawashima ◽  
...  
Keyword(s):  
Growth Factor ◽  
Heparan Sulfate ◽  
Chondroitin Sulfate ◽  
Fibroblast Growth Factor ◽  
Carboxyl Terminus ◽  
Fibroblast Growth ◽  
Colony Stimulating Factor ◽  
Macrophage Colony Stimulating Factor ◽  
Macrophage Colony ◽  
Stimulating Factor

Abstract The proteoglycan form of macrophage colony-stimulating factor (PG-M- CSF), but not M-CSF with a molecular weight of 85 kD (85-kD M-CSF), bound to immobilized basic fibroblast growth factor (bFGF), and, conversely, bFGF bound to immobilized PG-M-CSF, but not to the 85-kD M- CSF. PG-M-CSF has an additional amino acid sequence at its carboxyl terminus (part of a precursor sequence that is removed in 85-kD M-CSF by proteolytic processing) and it has one or two chondroitin sulfate glycosaminoglycan chains at the carboxyl terminus. Enzymatic removal of the chondroitin sulfate chain from PG-M-CSF had no effect on the binding between PG-M-CSF and bFGF. Ligand blotting analysis with radioiodinated bFGF showed that bFGF specifically bound to the polypeptide that corresponded to the carboxyl terminus of PG-M-CSF and was produced in Escherichia coli transfected with its gene. The exogeneous addition of heparan sulfate, which has strong affinity for bFGF, efficiently inhibited the binding between PG-M-CSF and bFGF. These results show that PG-M-CSF binds bFGF through its carboxyl terminal peptide and that the binding sites for PG-M-CSF and heparan sulfate on bFGF are located close together. PG-M-CSF also significantly reduced the mitogenic action of bFGF on Balb/c 3T3 mouse fibroblastic cells. Therefore, we conclude that PG-M-CSF not only binds bFGF, but also neutralizes the activity of the growth factor.

scholarly journals Direct interaction of proteoglycan macrophage colony-stimulating factor and basic fibroblast growth factor

Blood ◽  
1994 ◽  
Vol 83 (11) ◽  
pp. 3113-3119
Author(s):  
S Suzu ◽  
F Kimura ◽  
M Yamada ◽  
N Yanai ◽  
T Kawashima ◽  
...  
Keyword(s):  
Growth Factor ◽  
Heparan Sulfate ◽  
Chondroitin Sulfate ◽  
Fibroblast Growth Factor ◽  
Carboxyl Terminus ◽  
Fibroblast Growth ◽  
Colony Stimulating Factor ◽  
Macrophage Colony Stimulating Factor ◽  
Macrophage Colony ◽  
Stimulating Factor

The proteoglycan form of macrophage colony-stimulating factor (PG-M- CSF), but not M-CSF with a molecular weight of 85 kD (85-kD M-CSF), bound to immobilized basic fibroblast growth factor (bFGF), and, conversely, bFGF bound to immobilized PG-M-CSF, but not to the 85-kD M- CSF. PG-M-CSF has an additional amino acid sequence at its carboxyl terminus (part of a precursor sequence that is removed in 85-kD M-CSF by proteolytic processing) and it has one or two chondroitin sulfate glycosaminoglycan chains at the carboxyl terminus. Enzymatic removal of the chondroitin sulfate chain from PG-M-CSF had no effect on the binding between PG-M-CSF and bFGF. Ligand blotting analysis with radioiodinated bFGF showed that bFGF specifically bound to the polypeptide that corresponded to the carboxyl terminus of PG-M-CSF and was produced in Escherichia coli transfected with its gene. The exogeneous addition of heparan sulfate, which has strong affinity for bFGF, efficiently inhibited the binding between PG-M-CSF and bFGF. These results show that PG-M-CSF binds bFGF through its carboxyl terminal peptide and that the binding sites for PG-M-CSF and heparan sulfate on bFGF are located close together. PG-M-CSF also significantly reduced the mitogenic action of bFGF on Balb/c 3T3 mouse fibroblastic cells. Therefore, we conclude that PG-M-CSF not only binds bFGF, but also neutralizes the activity of the growth factor.

scholarly journals Basic fibroblast growth factor stimulates myelopoiesis in long-term human bone marrow cultures

Blood ◽  
1991 ◽  
Vol 77 (5) ◽  
pp. 954-960 ◽  
Author(s):  
EL Wilson ◽  
DB Rifkin ◽  
F Kelly ◽  
MJ Hannocks ◽  
JL Gabrilove
Keyword(s):  
Bone Marrow ◽  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Progenitor Cells ◽  
Basic Fibroblast Growth Factor ◽  
Fibroblast Growth ◽  
Colony Stimulating Factor ◽  
Low Concentrations ◽  
Stimulating Factor

Abstract We previously showed that basic fibroblast growth factor (bFGF) is a potent mitogen for human bone marrow (BM) stromal cells and significantly delays their senescence. In the present study, we demonstrated that low concentrations of bFGF (0.2 to 2 ng/mL) enhance myelopoiesis in long-term human BM culture. Addition of bFGF to long- term BM cultures resulted in an increase in (a) the number of nonadherent cells (sixfold), particularly those of the neutrophil granulocyte series; (b) the number of nonadherent granulocyte colony- stimulating factor (G-CSF)- and granulocyte-macrophage colony- stimulating factor (GM-CSF)-responsive progenitor cells; (c) the number of adherent foci of hematopoietic cells (10-fold); and (d) the number of progenitor cells in the adherent stromal cell layer. These effects were not noted with higher concentrations of bFGF (20 ng/mL). Thus, low concentrations of bFGF effectively augment myelopoiesis in human long- term BM cultures, and bFGF may therefore be a regulator of the hematopoietic system in vitro and in vivo.

scholarly journals Basic fibroblast growth factor stimulates myelopoiesis in long-term human bone marrow cultures

Blood ◽  
1991 ◽  
Vol 77 (5) ◽  
pp. 954-960 ◽  
Author(s):  
EL Wilson ◽  
DB Rifkin ◽  
F Kelly ◽  
MJ Hannocks ◽  
JL Gabrilove
Keyword(s):  
Bone Marrow ◽  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Progenitor Cells ◽  
Basic Fibroblast Growth Factor ◽  
Fibroblast Growth ◽  
Colony Stimulating Factor ◽  
Low Concentrations ◽  
Stimulating Factor

We previously showed that basic fibroblast growth factor (bFGF) is a potent mitogen for human bone marrow (BM) stromal cells and significantly delays their senescence. In the present study, we demonstrated that low concentrations of bFGF (0.2 to 2 ng/mL) enhance myelopoiesis in long-term human BM culture. Addition of bFGF to long- term BM cultures resulted in an increase in (a) the number of nonadherent cells (sixfold), particularly those of the neutrophil granulocyte series; (b) the number of nonadherent granulocyte colony- stimulating factor (G-CSF)- and granulocyte-macrophage colony- stimulating factor (GM-CSF)-responsive progenitor cells; (c) the number of adherent foci of hematopoietic cells (10-fold); and (d) the number of progenitor cells in the adherent stromal cell layer. These effects were not noted with higher concentrations of bFGF (20 ng/mL). Thus, low concentrations of bFGF effectively augment myelopoiesis in human long- term BM cultures, and bFGF may therefore be a regulator of the hematopoietic system in vitro and in vivo.

Regulation of macrophage colony-stimulating factor in liver fat-storing cells by peptide growth factors

1992 ◽  
Vol 262 (4) ◽  
pp. C876-C881 ◽  
Author(s):  
M. Pinzani ◽  
H. E. Abboud ◽  
L. Gesualdo ◽  
S. L. Abboud
Keyword(s):  
Growth Factor ◽  
Constitutive Expression ◽  
Liver Fat ◽  
Northern Analysis ◽  
Mrna Levels ◽  
Colony Stimulating Factor ◽  
Term Survival ◽  
Macrophage Colony Stimulating Factor ◽  
Macrophage Colony ◽  
Stimulating Factor

Macrophage colony-stimulating factor (M-CSF) selectively promotes mononuclear phagocyte survival, proliferation, and differentiation. The production of this factor within the liver may be necessary to support the relatively long-term survival of circulating monocytes as they migrate into tissues and differentiate into macrophages. We studied the constitutive expression and the effects of platelet-derived growth factor (PDGF), basic fibroblast growth factor (bFGF), and epidermal growth factor (EGF) on M-CSF mRNA levels and secretion of M-CSF in murine liver fat-storing cells (FSC), vascular pericytes likely involved in the development of liver fibrosis. By Northern analysis, using a murine M-CSF cDNA, FSC constitutively express two major transcripts of 4.4 and 2.2 kb, similar to those detected in mouse L cells, used as a control. Exposure to 10 ng/ml PDGF or bFGF increased M-CSF mRNA levels. Peak effects were observed at 3 and 6 h for PDGF and bFGF, respectively, returning to baseline levels by 12 h. Under basal conditions, detectable amounts of M-CSF, measured by radioimmunoassay, were found in cell supernatants conditioned for 8 and 24 h. PDGF and bFGF markedly stimulated the release of M-CSF as early as 8 h, an effect persisting for at least 24 h. These findings suggest that liver FSC release M-CSF upon stimulation by PDGF and bFGF and may contribute to the activation of resident or infiltrating cells in inflammatory liver diseases.

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