Acidic Fibroblast Growth Factor (acidic + fibroblast_growth_factor)

Distribution by Scientific Domains

Kinds of Acidic Fibroblast Growth Factor

  • human acidic fibroblast growth factor


  • Selected Abstracts


    Comparison of acidic fibroblast growth factor on collagen carrier with calcium hydroxide as pulp capping agents in monkeys

    DENTAL TRAUMATOLOGY, Issue 5 2007
    Zhimei Li
    Abstract,,, Acidic fibroblast growth factor (aFGF) has been shown to facilitate wound healing by stimulating fibroblast proliferation and angiogenesis. It has also been reported to possess a powerful anti-apoptotic function This study compared the histological pulp responses to aFGF on collagen carrier and Ca(OH)2 placed on the mechanically exposed dental pulp in monkeys at two observation periods. Thirty-six teeth with pulp exposures were distributed into three groups according to the capping agents used prior to application of the coronal seal: collagen-based matrix carrier (group 1), aFGF on the collagen-based matrix carrier (group 2) and aqueous calcium hydroxide [Ca(OH)2] paste (group 3). Specimens were harvested at 6 and 13 weeks postoperatively and prepared for hematoxylin and eosin, and Gram staining. Histological qualitative evaluation of pulp responses were performed under the light microscope following criteria modified from Cox et al. (17) and Hu et al. (18). Semi-quantitative analysis was also carried out using Kruskal,Wallis and Mann,Whitney U -tests. There was neither negligible inflammatory infiltrates with no bacteria present in the three groups at both timings, nor was there any significant difference in the soft tissue organization among the three groups at or between the 6- and 13-week observation periods. At 6 weeks, the hard tissue barrier produced by Ca(OH)2 group (1.040 ± 0.089) was significantly more superior than aFGF/collagen carrier group (1.930 ± 0.825) (P = 0.030) as well as collagen carrier group (3.142 ± 1.069, P = 0.018). At 13 weeks, both aFGF/collagen carrier group (1.214 ± 0.485) and the collagen carrier group (1.457 ± 0.814) produced significantly better hard tissue barrier (P = 0.040 and P = 0.017, respectively) than earlier timing. However, these two groups did not induce significantly improved hard tissue barrier compared to that produced by aqueous Ca(OH)2 paste which stimulated matrix secretion in a polar tubular dentin-like pattern. [source]


    Hepatic differentiation of human bone marrow-derived UE7T-13 cells: Effects of cytokines and CCN family gene expression

    HEPATOLOGY RESEARCH, Issue 12 2007
    Takashi Shimomura
    Aim:, Bone marrow-derived mesenchymal stem cells (MSC) are expected to be an excellent source of cells for transplantation. We aimed to study the culture conditions and involved genes to differentiate MSC into hepatocytes. Methods:, The culture conditions to induce the efficient differentiation of human bone marrow-derived UE7T-13 cells were examined using cytokines, hormones, 5-azacytidine and type IV collagen. Results:, We found that combination of acidic fibroblast growth factor (aFGF), basic fibroblast growth factor (bFGF) and hepatocyte growth factor (HGF) with type IV collagen coating induced hepatic differentiation of UE7T-13 cells at over 30% frequency, where expression of albumin mRNA was increased over 20-fold. The differentiated cells had functions of albumin production, glycogen synthesis and urea secretion as well as expressing hepatocyte-specific genes. In addition, these cellshave binuclear and cuboidal morphology, which is a characteristic feature of hepatocytes. During hepatic differentiation, UE7T-13 cells showed depressed expression of WISP1 and WISP2 genes, members of the CCN family. Conversely, knockdown of WISP1 or WISP2 gene by siRNA stimulated hepatic differentiation. The effect of aFGF/bFGF/HGF/type IV collagen coating and WISP1-siRNA on hepatic differentiation was additive. Conclusion:, The present study suggests that aFGF/bFGF/HGF/type IV collagen coating is the efficient condition for hepatic differentiation of UE7T-13 cells, and that WISP1 and WISP2 play an important role in hepatic transdifferentiation of these cells. [source]


    Protective effect of non-mitogenic human acidic fibroblast growth factor on hepatocyte injury

    HEPATOLOGY RESEARCH, Issue 10 2007
    Hua Xu
    Aim:, To study whether non-mitogenic human acidic fibroblast growth factor (nm-haFGF) has protective effects on H2O2 -induced hepatocyte injury in vitro and CCl4 -induced hepatocyte injury in vivo. Methods:, (i) HL-7702 hepatocytes were incubated with different concentrations of nm-haFGF for 12 h, and then the activity of lactate dehydrogenase (LDH) in culture medium was detected, and genomic DNA electrophoresis analysis was observed after being exposed to H2O2 (8 mmol/L) for 4 h. Proximately, apoptotic rates and protein expressions of Bcl-2 and Bax of HL-7702 cell were detected after being exposed to H2O2 (0.2 mmol/L) for 20 h. (ii) Being injected intraperitoneally with nm-haFGF, mice were treated with CCl4 intraperitoneally to induce hepatic injury. Twenty-four hours later, serum aspartate aminotransferase (AST) and alanine aminotransferase (ALT) were measured and histopathologic changes were evaluated. Results:, (i) In vitro tests: LDH activities and apoptotic rates decreased, the protein expression of Bcl-2 increased and Baxdecreased in nm-haFGF-treated groups at the concentrations of 100 150 and 200 ng/mL, compared with that in the model control group, which was treated with H2O2 alone. The genomic DNA remained nearly intact at the concentrations of 150 and 200 ng/mL. (ii) In vivo tests: serum ALT and AST in nm-haFGF-treated groups (10 ,g/kg and 20 ,g/kg) were much lower as compared to the model control group, which was treated with CCl4 alone. Histological examination showed that nm-haFGF markedly ameliorated hepatocytes vacuolation, cloudy swelling and inflammatory cells infiltration induced by CCl4. Conclusion:, nm-haFGF had protective effects against H2O2 -induced hepatocyte injury in vitro and CCl4 -induced acute liver injury in vivo. [source]


    Alternative type I and I, turn conformations in the ,8/,9 ,-hairpin of human acidic fibroblast growth factor

    PROTEIN SCIENCE, Issue 3 2002
    Jaewon Kim
    Abstract Human acidic fibroblast growth factor (FGF-1) has a ,-trefoil structure, one of the fundamental protein superfolds. The X-ray crystal structures of wild-type and various mutant forms of FGF-1 have been solved in five different space groups: C2, C2221, P21 (four molecules/asu), P21 (three molecules/asu), and P212121. These structures reveal two characteristically different conformations for the ,8/,9 ,-hairpin comprising residue positions 90,94. This region in the wild-type FGF-1 structure (P21, four molecules/asu), a his-tagged His93,Gly mutant (P21, three molecules/asu) and a his-tagged Asn106,Gly mutant (P212121) adopts a 3:5 ,-hairpin known as a type I (1,4) G1 ,-bulge (containing a type I turn). However, a his-tagged form of wild-type FGF-1 (C2221) and a his-tagged Leu44,Phe mutant (C2) adopt a 3:3 ,-hairpin (containing a type I, turn) for this same region. A feature that distinguishes these two types of ,-hairpin structures is the number and location of side chain positions with eclipsed C, and main-chain carbonyl oxygen groups (, , +60°). The effects of glycine mutations upon stability, at positions within the hairpin, have been used to identify the most likely structure in solution. Type I, turns in the structural data bank are quite rare, and a survey of these turns reveals that a large percentage exhibit crystal contacts within 3.0 Å. This suggests that many of the type I, turns in X-ray structures may be adopted due to crystal packing effects. [source]


    Structure of a highly stable mutant of human fibroblast growth factor 1

    ACTA CRYSTALLOGRAPHICA SECTION D, Issue 1 2009
    Anna Szlachcic
    Fibroblast growth factors (FGFs) are involved in diverse cellular processes such as cell migration, angiogenesis, osteogenesis, wound healing and embryonic and foetal development. Human acidic fibroblast growth factor (FGF-1) is the only member of the FGF family that binds with high affinity to all four FGF receptors and thus is considered to be the human mitogen with the broadest specificity. However, pharmacological applications of FGF-1 are limited owing to its low stability. It has previously been reported that the introduction of single mutations can significantly improve the stability of FGF-1 and its resistance to proteolytic degradation. Here, the structure of the Q40P/S47I/H93G triple mutant of FGF-1, which exhibits much higher stability, a prolonged half-life and enhanced mitogenic activity, is presented. Compared with the wild-type structure, three localized conformational changes in the stable triple mutant were observed, which is in agreement with the perfect energetic additivity of the single mutations described in a previous study. The huge change in FGF-1 stability (the denaturation temperature increased by 21.5,K, equivalent to ,,Gden = 24.3,kJ,mol,1) seems to result from the formation of a short 310 -helix (position 40), an improvement in the propensity of amino acids to form ,-sheets (position 47) and the rearrangement of a local hydrogen-bond network (positions 47 and 93). [source]


    Structure of rat acidic fibroblast growth factor at 1.4,Å resolution

    ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 2 2007
    Elisabeth Bock
    Fibroblast growth factors (FGFs) constitute a family of 22 structurally related heparin-binding polypeptides that are involved in the regulation of cell growth, survival, differentiation and migration. Here, a 1.4,Å resolution X-ray structure of rat FGF1 is presented. Two molecules are present in the asymmetric unit of the crystal and they coordinate a total of five sulfate ions. The structures of human, bovine and newt FGF1 have been published previously. Human and rat FGF1 are found to have very similar structures. [source]