Expression of recombinant tilapia insulin-like growth factor-I and stimulation of juvenile tilapia growth by injection of recombinant IGFs polypeptides

Regulation of endocrine and paracrine sources of Igfs and Gh receptor during compensatory growth in hybrid striped bass (Morone chrysops×Morone saxatilis)

“…While barramundi and salmon Igf1 were more potent in stimulating protein synthesis than Igf2 in rat myoblasts (Degger et al 2001, Wilkinson et al 2004, injection of homologous Igf2 resulted in similar elevations in weight gain in tilapia as injection with Igf1 (Chen et al 2000). Furthermore, Igf2 has recently been shown to have significant mitogenic effects in trout myocytes (Codina et al 2008).…”

“…The potential contribution of locally produced Igf1 to anabolism is further underscored by studies in Gh-transgenic tilapia (Oreochromis niloticus), which showed elevated growth and skeletal igf1 mRNA but reduced plasma Igf1 relative to wild-type controls (Eppler et al 2007). Unlike postnatal mammals, circulating as well as locally produced Igf2 may also have mitogenic effects in adult fishes (Chen et al 2000, Peterson et al 2004, Terova et al 2007). The anabolic effects of both Igf1 and Igf2 are mediated by Igf-binding proteins (Igfbps), four of which have been identified in fishes at the protein level (Igfbp-1, -2, -3, and -5; Shimizu et al 2003.…”

Expression and cellular localization of insulin-like growth factor-II protein and mRNA in Sparus aurata during development

“…Gentil et al (1996) produced recombinant rainbow trout IGF-II for the development of an RIA, in order to measure IGF-II concentrations in fish serum. Subsequently, Chen et al (1997Chen et al ( , 2000 demonstrated that recombinant tilapia IGF-II stimulated DNA synthesis in tilapia ovarian cells in vitro and significantly increased body weight and body length when injected into juvenile tilapia. Recombinant barramundi IGF-II stimulated protein synthesis in L6 rat myoblasts (Degger et al 2001) and recombinant turbot IGF-II inhibited release of growth hormone from turbot pituitary cells in culture (Duval et al 2002).…”

Molecular Cloning, Developmental Expression, and Hormonal Regulation of Zebrafish (Danio rerio) β Crystallin B1, a Member of the Superfamily of β Crystallin Proteins

“…The PCR reaction was carried out in a final volume of 100 L. The reaction consisted of the cDNA library liquids, 10 L of 10ϫ PCR buffer (HT Biotechnology, U.S.A.), 200 M of each dNTP, 1 g of the IGFBP and HDLBP forward and reverse primers, and 2.5 units of Taq DNA polymerase. The reaction and process followed those we published before (12)(13)(14)(15). The PCR product was purified by electroelution and used as a probe for isolating 1 million clones from a zebrafish heart cDNA library and a zebrafish 24-h embryo cDNA library by the plaque hybridization method, as we published previously (12)(13)(14)(15).…”

“…The reaction and process followed those we published before (12)(13)(14)(15). The PCR product was purified by electroelution and used as a probe for isolating 1 million clones from a zebrafish heart cDNA library and a zebrafish 24-h embryo cDNA library by the plaque hybridization method, as we published previously (12)(13)(14)(15). ␤ crystallin B1 cDNA was analyzed with an automated Applied Biosystem 373A Genetic Analysis System.…”