The independent effects of size and fatness, 1 year prior to maturity, on male sexual development of chinook salmon (Oncorhynchus tshawytscha) were tested. Beginning in March 1995, ration size and dietary lipid were independently manipulated to produce four groups of spring chinook salmon differing in size and fatness. Size, growth rate, adiposity, liver triacylglycerol and glycogen contents, and plasma insulin and insulin-like growth factor I (IGF-I) levels were monitored to follow the metabolic states of fish in the different treatment groups and to observe whether plasma levels of these growth mediators predict sexual development. Differences in size and fatness were well established by the first autumn (September 1995), 1 year prior to sexual maturity, and common ration size groups were pooled for further rearing. Subsequently in winter-spring (February-March), 6 months prior to sexual maturity, there were no within-tank differences in size or fatness. Nevertheless, the effects of size and fatness, from 1 year earlier, on incidence of sexual maturity were significant. Overall, size appeared to have the primary effect, but for smaller fish, an effect of fat content was indicated. Plasma insulin levels, and in limited cases, IGF-I levels, were correlated with growth rate and size, but were not accurate indicators of sexual development.
Protein and cDNA sequence analysis have revealed that the insulin-like growth factor (IGF-I) has been highly conserved among several mammalian species. Using the combined techniques of polymerase chain reaction and molecular cloning, we have now obtained the cDNA sequence encoding preproIGF-I from a teleost species, Oncorhynchus kisutch (coho salmon). The 2020 nucleotide (nt) cloned cDNA sequence contains a 528 nt open reading frame encoding 176 amino acids in preproIGF-I and 175 nt and 1317 nt of flanking 5'- and 3'-untranslated regions, respectively. The deduced amino acid sequence of salmon IGF-I is highly conserved relative to its mammalian homologues and there are only 14 amino acid differences out of 70 between salmon and human IGF-I. Interestingly, the C-terminal E domain of salmon proIGF-I, which is presumed to be proteolytically cleaved during biosynthesis, also shows striking amino acid sequence homology with its mammalian counterpart, except for an internal 27 residue segment that is unique to salmon proIGF-I. Northern analysis revealed that salmon preproIGF-I mRNA consists predominantly of a single 3900 nt sized band although minor bands were also observed after prolonged autoradiographic exposure. The RNA analysis also revealed that the level of preproIGF-I mRNA is increased 6-fold in liver RNA isolated from salmon injected with bovine GH, as compared to untreated controls. These results demonstrate that the primary structure and regulated expression of IGF-I by GH have been conserved in teleosts.
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