Molecular signaling in pathogenesis of craniosynostosis: the role of fibroblast growth factor and transforming growth factor–β

2011 ◽  
Vol 31 (2) ◽  
pp. E7 ◽  
Author(s):  
Harvey Chim ◽  
Sunil Manjila ◽  
Alan R. Cohen ◽  
Arun K. Gosain
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Cranial Sutures ◽  
Fibroblast Growth ◽  
Molecular Signaling ◽  
Ongoing Research ◽  
Suture Fusion

The interplay of signals between dura mater, suture mesenchyme, and brain is essential in determining the fate of cranial sutures and the pathogenesis of premature suture fusion leading to craniosynostosis. At the forefront of research into suture fusion is the role of fibroblast growth factor and transforming growth factor–β, which have been found to be critical in the cell-signaling cascade involved in aberrant suture fusion. In this review, the authors discuss recent and ongoing research into the role of fibroblast growth factor and transforming growth factor–β in the etiopathogenesis of craniosynostosis.

Expression of transforming growth factor β and fibroblast growth factor 2 in the lens epithelium of Morioka cataract mice

2014 ◽  
Vol 54 (2) ◽  
pp. 104-109 ◽  
Author(s):  
Tomohiro Kondo ◽  
Naoko Ishiga-Hashimoto ◽  
Hiroaki Nagai ◽  
Ai Takeshita ◽  
Masaki Mino ◽  
...  
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Lens Epithelium ◽  
Fibroblast Growth Factor 2 ◽  
Fibroblast Growth

scholarly journals Latent transforming growth factor-β complex in Chinese hamster ovary cells contains the multifunctional cysteine-rich fibroblast growth factor receptor, also termed E-selectin-ligand or MG-160

1997 ◽  
Vol 324 (2) ◽  
pp. 427-434 ◽  
Author(s):  
Anders OLOFSSON ◽  
Ulf HELLMAN ◽  
Peter TEN DIJKE ◽  
Susanne GRIMSBY ◽  
Hidenori ICHIJO ◽  
...  
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Major Part ◽  
Transforming Growth Factor ◽  
Chinese Hamster ◽  
Transforming Growth Factor Β ◽  
Cell Types ◽  
Fibroblast Growth ◽  
Selectin Ligand ◽  
Tgf Β1

Transforming growth factor-β (TGF-β) is secreted as latent high molecular mass complexes from producer cells. The N-terminal precursor remnant, also called latency-associated peptide (LAP), forms a non-covalently linked complex with TGF-β and confers the latency to TGF-β. In human platelets and certain other cell types, latent TGF-β binding protein-1 (LTBP-1) is disulphide-linked to LAP, and forms complexes of more than 230 kDa. In addition, LTBP-2 and -3, which are structurally similar to LTBP-1, can be part of latent TGF-β complexes. In Chinese hamster ovary (CHO) cells transfected with the TGF-β1 cDNA, a major part of the latent TGF-β secreted into the medium is a 100-kDa small latent complex containing TGF-β and LAP. In addition, we found two other forms of latent TGF-β complexes, i.e. a 220-kDa complex containing LTBP-1, and a 220-kDa complex containing a 140-kDa protein. Purification of the 140-kDa component, termed latent TGF-β complexed protein-1 (LTCP-1), followed by amino acid sequencing and cDNA cloning from a CHO cell cDNA library, revealed that it is a hamster counterpart of a previously identified, multifunctional protein known as chicken cysteine-rich fibroblast growth factor (FGF) receptor, mouse E-selectin-ligand and rat MG-160 (a 160-kDa membrane sialoglycoprotein of the Golgi apparatus). Immunoprecipitation of LTCP-1 and TGF-β1 from CHO cells stably transfected with TGF-β1 precursor cDNA revealed that the expressed protein forms a complex with LAP, and that a major part of the complex is secreted. Northern blot analysis showed that mRNA for LTCP-1 was expressed in large amounts in testis, ovary and placenta, but less abundantly in other tissues. These results suggest that TGF-β, produced in certain cell types, may form a complex with LTCP-1, which may have different properties compared with other latent TGF-β complexes. It remains to be investigated whether the complex formation between LTCP-1 and TGF-β1 also occurs in other cells, whether the association between them occurs in the Golgi complex, and whether it affects the interaction of LTCP-1 with FGF or E-selectin.

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