Insulin-like growth factor-I increases bone sialoprotein (BSP) expression through fibroblast growth factor-2 response element and homeodomain protein-binding site in the proximal promoter of the BSP gene

2006 ◽  
Vol 208 (2) ◽  
pp. 326-335 ◽  
Author(s):  
Youhei Nakayama ◽  
Yu Nakajima ◽  
Naoko Kato ◽  
Hideki Takai ◽  
Dong-Soon Kim ◽  
...  
Keyword(s):  
Growth Factor ◽  
Protein Binding ◽  
Binding Site ◽  
Fibroblast Growth Factor ◽  
Bone Sialoprotein ◽  
Proximal Promoter ◽  
Fibroblast Growth Factor 2 ◽  
Homeodomain Protein ◽  
Fibroblast Growth ◽  
Factor I

Fibroblast growth factor 2 and cyclic AMP synergistically regulate bone sialoprotein gene expression

Bone ◽  
2006 ◽  
Vol 39 (1) ◽  
pp. 42-52 ◽  
Author(s):  
Emi Shimizu ◽  
Youhei Nakayama ◽  
Yu Nakajima ◽  
Naoko Kato ◽  
Hideki Takai ◽  
...  
Keyword(s):  
Gene Expression ◽  
Growth Factor ◽  
Cyclic Amp ◽  
Fibroblast Growth Factor ◽  
Bone Sialoprotein ◽  
Fibroblast Growth Factor 2 ◽  
Fibroblast Growth

scholarly journals Transcriptional Regulation of Fibroblast Growth Factor-2 Expression in Human Astrocytes: Implications for Cell Plasticity

1998 ◽  
Vol 9 (8) ◽  
pp. 2269-2285 ◽  
Author(s):  
John Moffett ◽  
Erica Kratz ◽  
Jason Myers ◽  
Ewa K. Stachowiak ◽  
Robert Z. Florkiewicz ◽  
...  
Keyword(s):  
Growth Factors ◽  
Growth Factor ◽  
Protein Binding ◽  
Fibroblast Growth Factor ◽  
Fibroblast Growth Factor 2 ◽  
Cell Contact ◽  
Fibroblast Growth ◽  
Two Stage ◽  
Human Astrocytes ◽  
Camp Stimulation

Induction of the fibroblast growth factor-2 (FGF-2) gene and the consequent accumulation of FGF-2 in the nucleus are operative events in mitotic activation and hypertrophy of human astrocytes. In the brain, these events are associated with cellular degeneration and may reflect release of the FGF-2 gene from cell contact inhibition. We used cultures of human astrocytes to examine whether expression of FGF-2 is also controlled by soluble growth factors. Treatment of subconfluent astrocytes with interleukin-1β, epidermal or platelet-derived growth factors, 18-kDa FGF-2, or serum or direct stimulation of protein kinase C (PKC) with phorbol 12-myristate 13-acetate or adenylate cyclase with forskolin increased the levels of 18-, 22-, and 24-kDa FGF-2 isoforms and FGF-2 mRNA. Transfection of FGF-2 promoter–luciferase constructs identified a unique −555/−513 bp growth factor-responsive element (GFRE) that confers high basal promoter activity and activation by growth factors to a downstream promoter region. It also identified a separate region (−624/−556 bp) essential for PKC and cAMP stimulation. DNA–protein binding assays indicated that novel cis-acting elements and trans-acting factors mediate activation of the FGF-2 gene. Southwestern analysis identified 40-, 50-, 60-, and 100-kDa GFRE-binding proteins and 165-, 112-, and 90-kDa proteins that interacted with the PKC/cAMP-responsive region. The GFRE and the element essential for PKC and cAMP stimulation overlap with the region that mediates cell contact inhibition of the FGF-2 promoter. The results show a two-stage regulation of the FGF-2 gene: 1) an initial induction by reduced cell contact, and 2) further activation by growth factors or the PKC-signaling pathway. The hierarchic regulation of the FGF-2 gene promoter by cell density and growth factors or PKC reflects a two-stage activation of protein binding to the GFRE and to the PKC/cAMP-responsive region, respectively.

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