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Ing-ming Chiu - One of the best experts on this subject based on the ideXlab platform.

  • Activation of FGF1B Promoter and FGF1 Are Involved in Cardiogenesis Through the Signaling of PKC, but Not MAPK.
    Stem cells and development, 2015
    Co-Authors: Hung-yu Lin, Don-ching Lee, Horng-dar Wang, Ya-hui Chi, Ing-ming Chiu
    Abstract:

    Heart disease is the leading cause of human death in the 21st century. Heart transplantation is a promising way to treat this. Because donor resources are limited, cell-based therapy has been developed as an alternative. Therefore, genes that trigger cardiogenesis could have potential in the treatment of heart disease. Fibroblast growth factor 1 (FGF1) is reported to stimulate cardiomyocyte proliferation under conditions of myocardial infarction, but little is known about its function during cardiac differentiation. In this study, we established an in vitro cardiogenesis model through a reliable chemical induction protocol to determine whether FGF1 and its gene expression are involved in cardiogenesis. Oxytocin, not only a well-known hormone but also a cardiac differentiation inducer, was used in a mouse embryonic stem cell line, E14Tg2a, to achieve cardiac differentiation. After differentiation, beating cell clusters appeared and the expression of FGF1B mRNA was upregulated in the late differentiation stage (differentiation days 8-14). Interestingly, FGF1B expression patterns during cardiac differentiation were similar to those of a mature cardiomyocyte marker, troponin T2, cardiac. The blockage of FGF1-FGF receptor (FGFR) signaling reduced not only the appearance of beating cluster formation but also the expression levels of cardiomyocyte-associated genes. Moreover, by investigating FGF1 downstream signaling cascades, we observed that the efficiency of beating cluster formation was mainly regulated through the FGF1-FGFR-PKC signaling axis. Taken together, we provide evidence to support that FGF1 could regulate cardiogenesis primarily through the protein kinase C signaling, but not through the mitogen-activated protein kinase signaling, pathway.

  • Human FGF1 promoter is active in ependymal cells and dopaminergic neurons in the brains of F1B-GFP transgenic mice.
    Developmental neurobiology, 2014
    Co-Authors: Mei-shu Chen, Don-ching Lee, Hua-kuo Lin, Hsun Chiu, Yu-fen Chung, Ing-ming Chiu
    Abstract:

    FGF1 is involved in multiple biological functions and exhibits the importance in neuroprotective effects. Our previous studies indicated that, in human brain and retina, the FGF1B promoter controlled the expression of FGF1. However, the exact function and regulation of FGF1 in brain is still unclear. Here, we generated F1B-GFP transgenic mice that expressed the GFP reporter gene under the control of human FGF1B promoter (−540 to +31). Using the fresh brain sections of F1B-GFP transgenic mice, we found that the F1B-GFP cells expressed strong fluorescent signals in the ventricular system throughout the brain. The results of immunohistochemistry further showed that two distinct populations of F1B-GFP+ cells existed in the brains of F1B-GFP transgenic mice. We demonstrated that one population of F1B-GFP+ cells was ependymal cells, which distributed along the entire ventricles, and the second population of F1B-GFP+ cells was neuronal cells that projected their long processes into multiple directions in specific areas of the brain. The double labeling of F1B-GFP+ cells and tyrosine hydroxylase indicated that a subpopulation of F1B-GFP+-neuronal cells was dopaminergic neurons. Importantly, these F1B-GFP+/TH+ cells were distributed in the main dopaminergic neuronal groups including hypothalamus, ventral tegmental area, and raphe nuclei. These results suggested that human FGF1B promoter was active in ependymal cells, neurons, and a portion of dopaminergic neurons. Thus, the F1B-GFP transgenic mice provide an animal model not only for studying FGF1 gene expression in vivo but also for understanding the role of FGF1 contribution in neurodegenerative disorders such as Parkinson's disease and Alzheimer's disease. © 2014 Wiley Periodicals, Inc. Develop Neurobiol 75: 232–248, 2015

  • brain specific 1b promoter of fgf1 gene facilitates the isolation of neural stem progenitor cells with self renewal and multipotent capacities
    Developmental Dynamics, 2009
    Co-Authors: Yi Chao Hsu, Don-ching Lee, Ing-ming Chiu, Su Liang Chen, Weichih Liao, Jia Wei Lin, Wenta Chiu
    Abstract:

    Fibroblast growth factor 1 (FGF1) has been shown to maintain proliferation and self-renewal capacities of neural stem/progenitor cells (NSPCs) in vitro. We have previously identified FGF1B as the major transcript of FGF1 gene expressed exclusively in brain areas that are known to be abundant for NSPCs in vivo. The 540-bp (-540 to +31) sequence upstream of the 1B transcription start site (F1B) is sufficient to drive the expression of a heterologous luciferase reporter in cultured cells. In this study, we report a direct genetic and functional approach to isolate F1B(+) NSPCs using green fluorescent protein (GFP) reporter gene under the control of human F1B promoter. The F1B-GFP reporter could facilitate the isolation of NSPCs with self-renewal and multipotent capacities from human glioblastoma tissues, developing or adult mouse brains by fluorescence-activated cell sorting. Future work elucidating the mechanisms that control FGF1B expression will help to identify new NSPC-related genes.

David G. Fernig - One of the best experts on this subject based on the ideXlab platform.

  • HaloTag is an effective expression and solubilisation fusion partner for a range of fibroblast growth factors
    PeerJ, 2015
    Co-Authors: Yong Li, Sarah E Taylor, Mark C. Wilkinson, David G. Fernig
    Abstract:

    The production of recombinant proteins such as the fibroblast growth factors (FGFs) is the key to establishing their function in cell communication. The production of recombinant FGFs in E. coli is limited, however, due to expression and solubility problems. HaloTag has been used as a fusion protein to introduce a genetically-encoded means for chemical conjugation of probes. We have expressed 11 FGF proteins with an N-terminal HaloTag, followed by a tobacco etch virus (TEV) protease cleavage site to allow release of the FGF protein. These were purified by heparin-affinity chromatography, and in some instances by further ion-exchange chromatography. It was found that HaloTag did not adversely affect the expression of FGF1 and FGF10, both of which expressed well as soluble proteins. The N-terminal HaloTag fusion was found to enhance the expression and yield of FGF2, FGF3 and FGF7. Moreover, whereas FGF6, FGF8, FGF16, FGF17, FGF20 and FGF22 were only expressed as insoluble proteins, their N-terminal HaloTag fusion counterparts (Halo-FGFs) were soluble, and could be successfully purified. However, cleavage of Halo-FGF6, -FGF8 and -FGF22 with TEV resulted in aggregation of the FGF protein. Measurement of phosphorylation of p42/44 mitogen-activated protein kinase and of cell growth demonstrated that the HaloTag fusion proteins were biologically active. Thus, HaloTag provides a means to enhance the expression of soluble recombinant proteins, in addition to providing a chemical genetics route for covalent tagging of proteins.

  • HaloTag is an effective expression and solubilisation fusion partner for a range of fibroblast growth factors
    2014
    Co-Authors: Yong Li, Sarah E Taylor, Mark C. Wilkinson, David G. Fernig
    Abstract:

    The production of recombinant proteins such as the fibroblast growth factors (FGFs) is the key to establishing their function in cell communication. The production of recombinant FGFs in E. coli is limited, however, due to expression and solubility problems. HaloTag has been used as a fusion protein to introduce a genetically-encoded means for chemical conjugation of probes. We have expressed 11 FGF proteins with an N-terminal HaloTag, followed by a tobacco etch virus (TEV) protease cleavage site to allow release of the FGF protein. These were purified by heparin-affinity chromatography, and in some instances by further ion-exchange chromatography. It was found that HaloTag did not adversely affect the expression of FGF1 and FGF10, both of which expressed well as soluble proteins. The N-terminal HaloTag fusion was found to enhance the expression and yield of FGF2, FGF3 and FGF7. Moreover, whereas FGF6, FGF8, FGF16, FGF17, FGF20 and FGF22 were only expressed as insoluble proteins, their N-terminal HaloTag fusion counterparts (Halo-FGFs) were soluble, and could be successfully purified. However, cleavage of Halo-FGF6, -FGF8 and -FGF22 with TEV resulted in aggregation of the FGF protein. Thus, HaloTag provides a means to enhance the expression of soluble recombinant proteins, in addition to providing a chemical genetics route for covalent tagging of proteins.

Masaru Katoh - One of the best experts on this subject based on the ideXlab platform.

  • comparative genomics on fgf16 orthologs
    International Journal of Molecular Medicine, 2005
    Co-Authors: Yuriko Katoh, Masaru Katoh
    Abstract:

    Abstract We have previously reported comparative genomics analyses on FGF3, FGF4, FGF6, FGF7, FGF8, FGF10, FGF11, FGF17, FGF18, FGF19, FGF20, FGF22 and FGF23 genes. Here, we performed comparative genomics analyses on FGF1, FGF2, FGF5, FGF9, FGF12, FGF13, FGF14, FGF16 and FGF21 genes, and further characterized the FGF16 gene. Chimpanzee FGF16, chicken fgf16, and zebrafish fgf16 genes were identified within NW_121938.1, NW_060344.1, and CR855117.3 genome sequences, respectively. Chimpanzee FGF16 (207 aa), chicken fgf16 (207 aa), and zebrafish fgf16 (203 aa) showed 100%, 89.9%, and 79.2% total amino-acid identity with human FGF16. Because FGF16, FGF9, and FGF20 constitute FGF subfamily without N-terminal signal peptide, we next searched for uncharacterized FGF9 or FGF20 orthologs. Zebrafish fgf9 gene was identified within BX927112.11 genome sequence, and chicken fgf20 gene within NW_060349.1 genome sequence. Although N-terminal part was divergent, middle and C-terminal parts were well conserved among vertebrate FGF16, FGF9 and FGF20 orthologs. Phylogenetic analyses revealed that zebrafish fgf9 and fgf20 were more related to each other than to their chicken or mammalian orthologs. TCF/LEF binding site and TATA box were well conserved among the human FGF16, rat Fgf16, and mouse Fgf16 promoters. Because nuclear complex consisting of TCF/LEF (TCF1, TCF3, TCF4 or LEF1), beta-catenin, PYGO (PYGO1 or PYGO2) and Legless (BCL9 or BCL9L) binds to the TCF/LEF-binding site to up-regulate WNT/beta-catenin target genes, FGF16 gene was characterized as the evolutionarily conserved target of the WNT/beta-catenin signaling pathway, just like FGF18 and FGF20 genes. These facts indicate that FGF16, FGF18 and FGF20 are pharmacogenomics targets in the field of oncology and regenerative medicine.

  • Comparative genomics on FGF8, FGF17, and FGF18 orthologs
    International journal of molecular medicine, 2005
    Co-Authors: Masuko Katoh, Masaru Katoh
    Abstract:

    FGF and WNT signaling pathways network together during embryogenesis and carcinogenesis. Among 22 FGF family members within human and rodents genomes, FGF20 orthologs are evolutionarily conserved targets of the WNT/beta-catenin signaling pathway. FGF8, FGF17, and FGF18 constitute one of FGF subfamilies. Here, comparative proteomics and comparative genomics analyses on FGF8, FGF17, and FGF18 orthologs were performed. Rat Fgf8 and FGF17 genes, consisting of five exons, were located within AC096326.7 and AC097410.12 genome sequences, respectively. FGF8, FGF17, and FGF18 orthologs were FGF family members with the N-terminal signal peptide. Human FGF8 isoform F showed 90.6% total-amino-acid identity with rat Fgf8 (268 aa). Human FGF17 showed 98.6% total-amino-acid identity with rat FGF17 (216 aa). Human FGF18 also showed 98.6 total-amino-acid identity with rat Fgf18. FBXW1 (betaTRCP1 or BTRC1)-FGF8-NPM3 locus at human chromosome 10q24.32, FBXW11 (betaTRCP2 or BTRC2)-FGF18-NPM1 locus at human chromosome 5q35.1, and FGF17-NPM2 locus at human chromosome 8p21.3 were paralogous regions within the human genome. FGF8 mRNA was expressed in DMSO-treated embryonic stem (ES) cells. FGF17 mRNA was expressed in ES cells differentiated to an early endodermal phenotype. FGF18 mRNA was expressed in fetal lung, fetal heart, lung carcinoid, colorectal cancer, and ovarian cancer. FGF18 promoter with double TCF/LEF binding sites rather than FGF8 promoter and FGF17 promoter was more conserved between human and rodents. These facts indicate that FGF18 orthologs were evolutionarily conserved targets of the WNT/beta-catenin signaling pathway.

  • Comparative genomics on FGF7, FGF10, FGF22 orthologs, and identification of fgf25.
    International journal of molecular medicine, 2005
    Co-Authors: Yuriko Katoh, Masaru Katoh
    Abstract:

    FGF family members are key molecules for the integrome network in the fields of oncology and regenerative medicine. Based on the comparative genomics on the CCND1-ORAOV1-FGF19-FGF4 locus, we demonstrated that rodent Fgf15 is the ortholog of human FGF19 in 2003. FGF7 (KGF), FGF10, and FGF22 constitute a subfamily among FGF family members. Here, comparative genomics analyses and comparative proteomics analyses on FGF7, FGF10, and FGF22 orthologs were performed. Chicken fgf22, zebrafish fgf22 and fgf25 genes, consisting of three exons, were identified within AC150066.1, BX927243.9 and CR854981.2 genome sequences, respectively. Zebrafish fgf22 (207 aa) showed 46.9%, 48.6% and 53.5% total amino-acid identity with human FGF7, FGF10 and FGF22, respectively. Zebrafish fgf25 (186 aa) showed 39.2%, 52.9% and 45.9% total amino-acid identity with human FGF7, FGF10 and FGF22, respectively. Phylogenetic analyses revealed that zebrafish fgf25 belongs to the FGF10 ortholog group. Zebrafish fgf25 was a novel FGF family member generated by the duplication of fgf10. FGF10-MRPS30-HCN1 locus at human chromosome 5p12 and FGF22-POLRMT-HCN2 locus at 19p13.3 were paralogous regions within the human genome. FGF7 mRNA was expressed in fetal heart, placenta, lung, kidney, and blood vessels. FGF10 mRNA was expressed in fetal lung, placenta, and uterus. FGF22 mRNA was expressed in hippocampus and ovarian fibrotheoma. FGF7 promoter with bHLH biding site and CCAAT box and FGF10 promoter with double bHLH biding sites were conserved well, while FGF22 promoter was significantly divergent. This is the first report on fgf25 gene and also on the comparative integromics analyses of FGF7, FGF10 and FGF22 orthologs.

  • evolutionary conservation of ccnd1 oraov1 fgf19 fgf4 locus from zebrafish to human
    International Journal of Molecular Medicine, 2003
    Co-Authors: Masuko Katoh, Masaru Katoh
    Abstract:

    Abstract The CCND1-ORAOV1-FGF19-FGF4-FGF3-FLJ10261-FADD-PPFIA1-EMS1 locus on human chromosome 11q13 is frequently amplified in esophageal cancer, breast cancer, and bladder tumors. FGF19, FGF4 and FGF3 genes are implicated in embryogenesis and carcinogenesis. We proposed in 2002 the hypothesis that mouse Fgf15 might be the ortholog of human FGF19 based on comparative genomics. Here, we identified zebrafish fgf19 and oraov1 genes by using bioinformatics to demonstrate the hypothesis. Zebrafish fgf19 gene, consisting of three exons, was located around nucleotide position 121802-124963 of zebrafish genome draft sequence AL929586.12 in the reverse orientation. Zebrafish fgf19 (209 aa) was more homologous to chicken fgf19 and human FGF19 than to rodent Fgf15. Zebrafish oraov1 gene, consisting of five exons, was located around nucleotide position 112172-115838 of AL929586.12 in the reverse orientation. Zebrafish oraov1 protein (141 aa) was more homologous to human ORAOV1 than to rodent Oraov1. The CCND1-ORAOV1-FGF19-FGF4 locus was well conserved between human and zebrafish genomes in the order of genes, in the direction of genes, and in the exon-intron structure. Rat Ccnd1-Oraov1-Fgf15-Fgf4 locus was synthenic to mouse Ccnd1-Oraov1 (also known as 2210010N10Rik)-Fgf15-Fgf4 locus. Fgf15, homologous to human FGF19 and zebrafish fgf19, was located on the synthenic locus of human FGF19 and zebrafish fgf19 within rodent genomes. Based on the evolutionary conservation of the CCND1-ORAOV1-FGF19-FGF4 locus from zebrafish to human, it was concluded that Fgf15 gene is the rodent ortholog of human FGF19 gene.

Michael Ittmann - One of the best experts on this subject based on the ideXlab platform.

  • Abstract 1106: Fibroblast growth factor FGF19 signaling promotes prostate cancer progression
    Cancer Research, 2011
    Co-Authors: Shu Feng, Patricia D. Castro, Wendong Yu, Jianghua Wang, Michael Ittmann
    Abstract:

    Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL Aberrant fibroblast growth factor (FGF) signaling can promote tumor development by directly driving cancer cell proliferation and survival, and by supporting tumor angiogenesis. Multiple FGFs have been found upregulated in prostate cancers, including FGF1, FGF2, FGF6, FGF8 and FGF17, all of which can activate FGF receptor 4 (FGFR4). FGFR4 is overexpressed in prostate cancer (PCa) and positively associated with aggressive PCa. FGF19 is a distinct member of FGF family in that it predominantly binds to FGFR4 with high affinity. In this present study we aimed to study the role of FGF19 in human PCa progression, and to determine whether the targeted suppression of FGF19/FGFR4 signaling has potential therapeutic benefits in PCa. Our results demonstrated that FGF19 is upregulated in human PCa compared to normal prostate tissues. FGF19 is expressed in an autocrine manner by all tested PCa cell lines. Exogenous FGF19 stimulates PCa cell proliferation, anchorage-independent growth, adhesion and invasion in vitro. The mRNAs of FGF19 co-receptors αKlotho and sKlotho are expressed in 97.5% and 27.5% of PCa clinical samples, respectively; but αKlotho is expressed in only 57% normal prostate tissues, sKlotho is barely detected in normal prostate tissues. Suppression of FGF19 by short hairpin RNA (shRNA) targeting FGF19 gene inhibits PCa cell proliferation, adhesion and invasiveness in vitro. Immunoprecipitation and western blot assays showed that FGF19 stimulates phosphorylation of FGFR4, FRS2α, Erk1/2 and p-38 MAPK, as well as MEK1/2 in both PC3 and DU145. Our data also revealed that FGF19 induced the serine/threonine protein kinase Akt phosphorylation in PCa cells. Lentiviral shRNA delivery was used for stable FGFR4 gene silencing in PC3 and LNCaP cells. The targeted knockdown of FGFR4 in PC3 and LNCaP cells resulted in significantly inhibited cell proliferation, invasion and remarkably reduced Akt phosphorylation. The upregulated expression of activated Caspase 8 and activated Caspase 3 in FGFR4 knockdown cells indicates that FGFR4 signaling inhibits PCa cell apoptosis. To determine if FGFR4 suppression impacts prostate tumor growth and metastasis in vivo we generated a PCa orthotopic xenograft model in which PC3-sh-FGFR4 or PC3-shV cells are injected directly into the prostates of nude mice in each group. The results revealed that the FGFR4 suppression in PCa cells significantly inhibited tumorigenicity in this model (P=0.01). The primary tumor weight was decreased by 63% in sh-FRGR4 tumors (p

  • FGF17 is an autocrine prostatic epithelial growth factor and is upregulated in benign prostatic hyperplasia.
    The Prostate, 2004
    Co-Authors: Nathaniel Polnaszek, Jianghua Wang, Bernard Kwabi-addo, Michael Ittmann
    Abstract:

    BACKGROUND Fibroblast growth factors (FGFs) are known to play an important role in the growth of prostatic epithelial cells. Benign prostatic hyperplasia (BPH) is characterized by increased epithelial and stromal proliferation within the transition zone of the prostate. FGF2, FGF7, and FGF9 are expressed in BPH tissue but expression of FGF17 has not been previously characterized in human prostate tissue. METHODS Expression of FGF17 in human prostate tissue and primary cultures of prostatic epithelial and stromal cells was determined by reverse-transcriptase polymerase chain reaction (RT-PCR). Growth response to FGF17 was assessed by addition of recombinant FGF17 to immortalized normal and neoplastic epithelial cell lines and primary cultures of prostatic stromal cells in the presence of insulin. Quantitative analysis of expression of FGF17 relative to keratin 18 and/or β-actin in normal and hyperplastic prostate and prostate carcinoma was carried out by real-time quantitative RT-PCR. RESULTS FGF17 is expressed by prostatic epithelial cells and can act as an autocrine growth factor for immortalized and neoplastic prostatic epithelial cells. It can also promote stromal proliferation, although only at higher concentrations. Expression of FGF17 per epithelial cell was increased 2-fold in BPH. CONCLUSIONS FGF17 is expressed by normal, hyperplastic, and neoplastic prostatic epithelial cells and can promote epithelial proliferation in an autocrine manner. FGF17 expression is increased 2-fold in BPH and may contribute to the increased epithelial proliferation seen in this disease. © 2004 Wiley-Liss, Inc.

Nobuyuki Itoh - One of the best experts on this subject based on the ideXlab platform.

  • roles of fgfs as paracrine or endocrine signals in liver development health and disease
    Frontiers in Cell and Developmental Biology, 2016
    Co-Authors: Nobuyuki Itoh, Yoshiaki Nakayama, Morichika Konishi
    Abstract:

    The liver plays important roles in multiple processes including metabolism, the immune system, and detoxification and also has a unique capacity for regeneration. FGFs are growth factors that have diverse functions in development, health, and disease. The FGF family now comprises 22 members. Several FGFs have been shown to play roles as paracrine signals in liver development, health, and disease. FGF8 and FGF10 are involved in embryonic liver development, FGF7 and FGF9 in repair in response to liver injury, and FGF5, FGF8, FGF9, FGF17, and FGF18 in the development and progression of hepatocellular carcinoma. In contrast, FGF15/19 and FGF21 are endocrine signals. FGF15/19, which is produced in the ileum, is a negative regulator of bile acid metabolism and a stimulator of gallbladder filling. FGF15/19 is a postprandial, insulin-independent activator of hepatic protein and glycogen synthesis. It is also required for hepatocellular carcinoma and liver regeneration. FGF21 is a hepatokine produced in the liver. FGF21 regulates glucose and lipid metabolism in white adipose tissue. Serum FGF21 levels are elevated in non-alcoholic fatty liver. FGF21 also protects against non-alcoholic fatty liver. These findings provide new insights into roles of FGFs in the liver and potential therapeutic strategies for hepatic disorders.

  • FGF10 acts as a major ligand for FGF receptor 2 IIIb in mouse multi-organ development.
    Biochemical and biophysical research communications, 2000
    Co-Authors: Hideyo Ohuchi, Hidemitsu Harada, Keisuke Sekine, Shigeaki Kato, Masahiro Yamasaki, Yukiko Hori, Nobuyuki Itoh
    Abstract:

    FGF receptor 2 isoform IIIb (FGFR2b), originally discovered as a receptor for FGF7, is known to be an important receptor in vertebrate morphogenesis, because FGFR2b null mice exhibit agenesis or dysgenesis of various organs, which undergo budding and branching morphogenesis. Since FGF7 null mice do not exhibit marked defects in organogenesis, it has been considered that other FGF(s) than FGF7 might function as a major ligand for FGFR2b during organogenesis. One of the candidate ligands is FGF10, because FGF10 binds to FGFR2b with high affinity and the formation of the limb and lung is arrested in FGF10 null mice as found in FGFR2b-deficient mice. Previous analyses of FGF10 null mice revealed that FGF10 is required for limb and lung development. To elucidate the role of FGF10 in wide-range organogenesis, we further analyzed the phenotypes of the FGF10 knockout mice. We found diverse phenotypes closely related to those for FGFR2b-deficient mice, which includes the absence of thyroid, pituitary, and salivary glands, while minor defects were observed in the formation of teeth, kidneys, hair follicles, and digestive organs. These results suggest that FGF10 acts as a major ligand for FGFR2b in mouse multi-organ development.

  • Comparison of the expression of three highly related genes, Fgf8, FGF17 and Fgf18, in the mouse embryo
    Mechanisms of Development, 1998
    Co-Authors: Yutaka Maruoka, Nobuyuki Itoh, Brigid L M Hogan, Norihiko Ohbayashi, Masamitsu Hoshikawa, Yasuhide Furuta
    Abstract:

    In mammals, 16 members of the Fgf family have so far been described with diverse roles in embryonic cell growth and differentiation. Here, we report the expression from early streak stage to midgestation of two newly-identified murine genes, FGF17 and Fgf18, that are most closely related to Fgf8 (63.7% and 56.8% identical, respectively, at the amino acid level). FGF17 is expressed during gastrulation but at lower levels than Fgf8, while Fgf18 RNA is not expressed until later, in paraxial mesoderm. In the developing tail bud, each Fgf gene shows a different pattern of transcription. Distinct and overlapping expression patterns are also described in the developing brain and limbs.

  • fibroblast growth factor 10 fgf10 and branching morphogenesis in the embryonic mouse lung
    Development, 1997
    Co-Authors: Saverio Bellusci, Nobuyuki Itoh, Justin C Grindley, Hisayo Emoto, Brigid L M Hogan
    Abstract:

    an increase in the rate of endodermal cell proliferation. The activity of FGF1, FGF7 and FGF10 was also tested directly on isolated endoderm in Matrigel culture. Under these conditions, FGF1 elicits immediate endodermal budding, while FGF7 and FGF10 initially induce expansion of the endoderm. However, within 24 hours, samples treated with FGF10 give rise to multiple buds, while FGF7-treated endoderm never progresses to bud formation, at all concentrations of factor tested. Although exogenous FGF1, FGF7 and FGF10 have overlapping activities in vitro, their in vivo expression patterns are quite distinct in relation to early branching events. We conclude that, during early lung development, localized sources of FGF10 in the mesoderm regulate endoderm proliferation and bud outgrowth. SUMMARY

  • Cloning of mouse FGF10 and up-regulation of its gene expression during wound healing.
    Gene, 1997
    Co-Authors: Shuzo Tagashira, Nobuyuki Itoh, Hideyuki Harada, Takashi Katsumata, Masashi Nakatsuka
    Abstract:

    We cloned the mouse homolog of FGF10, which was recently reported as a new member of the FGF family. The predicted molecular mass of this molecule is 23.6 kDa, and both nucleotide and amino acid sequences show high degrees of similarity with those of the rat. Examination of mouse FGF10 mRNA expression in various tissues and developmental stages by Northern hybridization revealed tissue- and developmental stage-specific expression of the gene. Similarly to the rat counterpart, mouse FGF10 mRNA (4.5 kb) was expressed relatively abundantly in embryos and the lung, and at much lower levels in brain and heart. In addition, a shorter transcript (1.3 kb) is expressed only in testis. Considering the high similarity in primary structure between FGF10 and FGF7 (known as keratinocyte growth factor; KGF), we also examined the gene expression of FGF10 during wound healing using a mouse model. FGF10 mRNA was highly induced 1 day after injury and decreased rapidly by 3 days. This suggests that FGF10 is a primary factor in the process of wound healing similarly to other growth factors such as TGF alpha and FGF7.