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    Biochem Biophys Res Commun. 1998 Feb 4;243(1):148-52.

    Structure and expression of a novel member, FGF-16, on the fibroblast growth factor family.

    Miyake A, Konishi M, Martin FH, Hernday NA, Ozaki K, Yamamoto S, Mikami T, Arakawa T, Itoh N.

    Department of Genetic Biochemistry, Kyoto University Graduate School of Pharmaceutical Sciences, Japan.

    We have isolated cDNA encoding a novel member (207 amino acids) of the FGF family from the rat heart by homology-based polymerase chain reaction. As this protein is the 16th documented member of the FGF family, we tentatively term it FGF-16. Among FGF family members, FGF-16 is most similar (73% amino acid identity) to FGF-9. We have also determined the structure of human FGF-16 with high amino acid sequence identity (98.6%) to rat FGF-16. Although the predicted FGF-16 amino acid sequence lacks a typical signal sequence, recombinant rat FGF-16 was efficiently secreted by Sf9 insect cells infected with recombinant baculovirus containing the cDNA. FGF-16 mRNA was predominantly expressed in the rat heart among the adult major tissues examined. The expression profile of FGF-16 mRNA was quite different from those of other members of the FGF family. In rat embryos, FGF-16 mRNA was predominantly expressed in the brown adipose tissue. However, the expression decreased greatly after birth. These results indicate that FGF-16 in embryos might play a role in development of the brown adipose tissue.

    PMID: 9473496 [PubMed - indexed for MEDLINE]

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