Fibroblast growth factor-2

Okada-Ban, M; Thiery, Jean Paul; Jouanneau, Jacqueline

doi:10.1016/s1357-2725(99)00133-8

Cited by 188 publications

(150 citation statements)

References 17 publications

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“…Consequently, mutation of the two proximal ATGs encoding Met 715 and Met 719 abolished the expression of SPRACT. Initiation at internal ATGs within an open reading frame has been observed previously (65)(66)(67)(68)in several cellular mRNAs and, more commonly, in viral RNAs. The expression of SPRACT in untransfected human cell lines as well as in transfected cells suggests that SPRACT is a physiological endogenous protein.…”

Section: Fig 6 Tryptic Peptide Analysis Of Tace Phosphorylationmentioning

confidence: 62%

Characterization of Growth Factor-induced Serine Phosphorylation of Tumor Necrosis Factor-α Converting Enzyme and of an Alternatively Translated Polypeptide

Fan

Turck

Derynck

2003

Journal of Biological Chemistry

107

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Tumor necrosis factor-␣ converting enzyme (TACE) is a prototype member of the adamalysin family of transmembrane metalloproteases that effects ectodomain cleavage and release of many transmembrane proteins, including transforming growth factor-␣. Growth factors that act through tyrosine kinase receptors, as well as other stimuli, induce shedding through activation of the Erk mitogen-activated protein (MAP) kinase pathway without the need of new protein synthesis. How MAP kinase regulates shedding by TACE is not known. We now report that the cytoplasmic domain of TACE is phosphorylated in response to growth factor stimulation. We also identified a naturally expressed smaller polypeptide corresponding to most of the cytoplasmic domain of TACE. This protein, which we named SPRACT, is derived through alternative translation of the TACE-coding sequence and is, similarly to TACE, phosphorylated in response to growth factor and phorbol 12-myristate 13-acetate stimulation. Phosphoamino acid analysis revealed that growth factor-induced phosphorylation of TACE occurs only on serine and not on threonine or tyrosine. Tryptic mapping experiments coupled with site-directed mutagenesis identified Ser 819 as the major target of growth factor-induced phosphorylation, whereas Ser 791 undergoes dephosphorylation in response to growth factor stimulation. The phosphorylation of Ser 819 , but not the dephosphorylation of Ser 791 , depends on activation of the Erk MAP kinase pathway. Increased SPRACT expression or mutation of the TACE cytoplasmic domain to inactivate growth factor-induced phosphorylation did not detectably affect growth factor-induced shedding of transmembrane transforming growth factor-␣ by TACE. The roles of SPRACT and the cytoplasmic phosphorylation of TACE remain to be defined.

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Section: Fig 6 Tryptic Peptide Analysis Of Tace Phosphorylationmentioning

confidence: 62%

Characterization of Growth Factor-induced Serine Phosphorylation of Tumor Necrosis Factor-α Converting Enzyme and of an Alternatively Translated Polypeptide

Fan

Turck

Derynck

2003

Journal of Biological Chemistry

107

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“…Basic fibroblast growth factor (bFGF), also known as FGF-2, is a soluble heparin-binding polypeptide with pleiotropic effects when applied to diverse tissues, including mitogenesis, cell migration, cell differentiation and a variety of developmental processes [18]. The 18-kD human bFGF sequence shares 97% and 99% amino acid identity with mouse/rat and bovine/ovine bFGF, respectively [1,16].…”

Section: Introductionmentioning

confidence: 99%

Correlation between plasma and synovial fluid basic fibroblast growth factor with radiographic severity in primary knee osteoarthritis

Honsawek

Yuktanandana

Tanavalee

et al. 2011

International Orthopaedics (SICOT)

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Purpose The aim of this study was to investigate plasma and synovial fluid basic fibroblast growth factor (bFGF) levels in patients with primary knee osteoarthritis (OA) and to evaluate the correlation between bFGF levels and disease severity. Methods Thirty-five patients with knee OA and 15 healthy individuals were recruited into this study. Knee OA grading was performed according to the Kellgren-Lawrence classification. bFGF concentrations in both plasma and synovial fluid were determined using enzyme-linked immunosorbent assay. Results Plasma and synovial fluid bFGF levels in knee OA patients were significantly higher than in controls (P<0.001). Moreover, plasma and synovial fluid bFGF concentrations were positively correlated with radiographic severity (r0 0.535, P<0.001 and r00.570, P<0.001, respectively). Further analysis revealed that there was a positive correlation between plasma and synovial fluid bFGF levels (r00.674, P<0.001). Conclusions Plasma and synovial fluid bFGF levels were significantly increased in OA patients, and these elevated levels were positively correlated with radiographic severity.These findings indicate that bFGF levels may be a monitor of disease severity and could play an essential part in the pathophysiology of degenerative process in OA.

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“…In humans, there are several FGF2 protein isoforms as follows: high molecular weight (HMW) 3 isoforms (22, 22.5, and 24 kDa) and a low molecular weight (LMW/18 kDa) isoform (2). The LMW isoform is initiated from a traditional AUG start codon, whereas the HMW isoforms are translated from individual nonconventional CUG codons upstream of the LMW start site (3). In rodents, there are three isoforms as follows: two HMW isoforms (20.5 and 21 kDa) as well as a LMW isoform (17.5 kDa) (4).…”

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confidence: 99%

Knockout of Nuclear High Molecular Weight FGF2 Isoforms in Mice Modulates Bone and Phosphate Homeostasis

Homer-Bouthiette

Doetschman

Xiao

et al. 2014

Journal of Biological Chemistry

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Background: FGF2 isoforms have differential effects on bone and phosphate homeostasis. Results: Knock-out of HMWFGF2 increased bone density and reduced bone Fgf23, Sost mRNA, and serum sclerostin. Conclusion: HMWKO mice display increased bone mineralization and normal serum phosphate due to modulation of bonerelated genes. Significance: Modulation of HMWFGF2 could possibly be utilized in development of therapeutic targets to treat osteomalacia and phosphate disorders.

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Fibroblast growth factor-2

Cited by 188 publications

References 17 publications

Characterization of Growth Factor-induced Serine Phosphorylation of Tumor Necrosis Factor-α Converting Enzyme and of an Alternatively Translated Polypeptide

Characterization of Growth Factor-induced Serine Phosphorylation of Tumor Necrosis Factor-α Converting Enzyme and of an Alternatively Translated Polypeptide

Correlation between plasma and synovial fluid basic fibroblast growth factor with radiographic severity in primary knee osteoarthritis

Knockout of Nuclear High Molecular Weight FGF2 Isoforms in Mice Modulates Bone and Phosphate Homeostasis

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