Structure and function of the heparin-binding (fibroblast) growth factor family

Introduction: HNSCC is a type of cancer in the oral and pharynx region. Several mutations/variations are observed in these cancer phenotypes. Fibroblast growth factor belongs to the family of heparin binding growth factors. FGFs are multifunctional proteins with a wide variety of effects; they are most commonly mitogens. Their expression pattern correlates with invasion of HNSCC. Aim: To assess the genetic alterations in genes of the fibroblast growth factor family and their association with HNSCC. Materials and Methods: The demographic data and samples of 528 HNSCC patients was collected from the cBioportal database. Oncoprint analysis was done to assess the amplification and genetic alterations of the members of the FGF gene family. String analysis was performed to evaluate the protein-protein interaction. The information about previous reported mutation and correlation with novel and reported mutation was obtained using GnomAD analysis. Results and Discussion: FGF3,4 and 19 genes showed maximum variation (25%). FGF4 and FGF19 genes showed maximum amplification in addition to deletion mutation. Excitingly FGF3, FGF4 and FGF19 genes showed similar amplification patterns in most of the HNSCC patients. Statistical significant difference in the gene expression of FGF3 9.578 x 10-3 observed between normal and primary tumour. S. Findings showed many novel mutations and also 4 reported mutations ie:FGF1, FGF12, FGF20, FGF21 Conclusion: Our present study concludes that more evidence is required to confirm their association with HNSCC.

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Abstract P015: Fibroblast Growth Factor 23 and Echocardiographic Measures of Cardiac Structure and Function among African Americans: The Atherosclerosis Risk in Communities (ARIC) Study

Circulation ◽

10.1161/circ.129.suppl_1.p015 ◽

2014 ◽

Vol 129 (suppl_1) ◽

Author(s):

Jeffrey R Misialek ◽

Alvaro Alonso ◽

Erin D Michos ◽

Scott D Solomon ◽

Amil M Shah ◽

...

Keyword(s):

Growth Factor ◽

Fibroblast Growth Factor ◽

Fibroblast Growth Factor 23 ◽

Structure And Function ◽

Cardiac Structure ◽

Fibroblast Growth ◽

Lv Mass ◽

Cardiac Structure And Function ◽

And Function ◽

Aric Study

Introduction: Fibroblast growth factor 23 (FGF23), an endocrine hormone, induced left ventricular (LV) hypertrophy through direct action in experimental animal models. The association of FGF23 with echocardiographic measures in humans is relatively uncharacterized. Hypothesis: Higher levels of FGF23 will be cross-sectionally associated with more adverse echocardiographic measures of LV structure and function. Methods: We conducted a cross-sectional analysis of 2086 African-American adults (66% female, median age 55) from a subset of the ARIC Study, a community-based cohort in the United States. Intact active FGF23 was assessed in blood samples collected at ARIC visit two (1990-1992). Echocardiography was performed at visit three (1993-1995) in participants recruited at the Jackson field center only. We used multivariable linear regression to evaluate the associations of FGF23 (per 15 pg/mL change) with echocardiographic measures after adjustment for traditional cardiovascular risk factors assessed at visit two. We also examined differences in observed associations by age and sex using interaction terms. Results: FGF23 was significantly associated with greater left atrial diameter and LV mass index (Table). A significant sex interaction was identified for LV diameter (p-interaction = 0.005). No association was observed in men while a positive association was observed among women. An adverse, decreasing trend in percent fractional shortening of the LV diameter at higher levels of FGF was stronger in individuals aged >55 (p-interaction = 0.03). No linear association was found between FGF23 and E/A ratio. Conclusion: FGF23 was associated with higher LV mass, larger LV size, and lower LV systolic function. These findings are consistent with results from experimental animal studies and provide evidence suggesting that cardiac structure and function may be influenced by FGF23 in humans. Prospective studies are needed to evaluate whether FGF23 is associated with change in markers of cardiac structure and function.

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Fibroblast growth factor homologous factors: Evolution, structure, and function

Cytokine & Growth Factor Reviews ◽

10.1016/j.cytogfr.2005.02.002 ◽

2005 ◽

Vol 16 (2) ◽

pp. 215-220 ◽

Cited By ~ 126

Author(s):

Mitchell Goldfarb

Keyword(s):

Growth Factor ◽

Fibroblast Growth Factor ◽

Structure And Function ◽

Fibroblast Growth ◽

And Function

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Thrombospondin 1 as a scavenger for matrix-associated fibroblast growth factor 2

Blood ◽

10.1182/blood-2003-03-0893 ◽

2003 ◽

Vol 102 (13) ◽

pp. 4399-4406 ◽

Cited By ~ 57

Author(s):

Barbara Margosio ◽

Daniela Marchetti ◽

Veronica Vergani ◽

Raffaella Giavazzi ◽

Marco Rusnati ◽

...

Keyword(s):

Endothelial Cells ◽

Growth Factor ◽

Fibroblast Growth Factor ◽

Angiogenic Factors ◽

Fibroblast Growth Factor 2 ◽

Fibroblast Growth ◽

Heparin Binding ◽

Factors Affecting ◽

Thrombospondin 1 ◽

And Function

AbstractThe antiangiogenic factor thrombospondin 1 (TSP-1) binds with high affinity to several heparin-binding angiogenic factors, including fibroblast growth factor 2 (FGF-2), vascular endothelial growth factor (VEGF), and hepatocyte growth factor/scatter factor (HGF/SF). The aim of this study was to investigate whether TSP-1 affects FGF-2 association with the extracellular matrix (ECM) and its bioavailability. TSP-1 prevented the binding of free FGF-2 to endothelial cell ECM. It also promoted the mobilization of matrix-bound FGF-2, generating a TSP-1/FGF-2 complex. The region of TSP-1 responsible for these activities was located within the 140-kDa antiangiogenic and FGF-2 binding fragment, whereas the 25-kDa heparin-binding fragment was inactive. Matrix-released FGF-2/TSP-1 complex had a reduced ability to bind to and induce proliferation of endothelial cells. TSP-1 depleted the ECM laid by FGF-2-overproducing tumor cells of its FGF-2-dependent mitogenic activity for endothelial cells. Besides FGF-2, TSP-1 also inhibited VEGF and HGF/SF binding to the ECM and mobilized them from the ECM. Our study shows that TSP-1 acts as a scavenger for matrix-associated angiogenic factors, affecting their location, bioavailability, and function. (Blood. 2003; 102:4399-4406)

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