Characterization of hepatic growth hormone binding sites in two fish species, Gillichthys mirabilis (Teleostei) and Acipenser transmontanus (Chondrostei).
To obtain information on the presence of growth hormone (GH) receptors in liver of nonmammalian vertebrates the specific binding of 125I-bovine growth hormone (bGH) to liver membranes of seven species representing the major groups was studied by radioreceptor assay. A substantial degree of specific binding was detected with sturgeon (Acipenser transmontanus) liver membranes and a much lower amount was detected on hepatic membranes of Gillichthys mirabilis. No significant specific binding was detected on liver membranes of pigeon, turtle, bullfrog, tilapia, or leopard shark. Gillichthys and sturgeon liver membranes were further characterized and compared with hepatic membranes from male rabbits. The sturgeon and Gillichthys membranes showed binding that was dependent upon time, temperature, pH, and membrane concentration. Scatchard analysis of the binding of 125I-bGH to sturgeon and rabbit membranes revealed both high and low affinity binding sites. The high affinity sites had KA values of 3.1 X 10(11) and 1.0 X 10(11) M-1, and capacities of 12 and 50 fmol/mg protein, respectively. Membranes from Gillichthys liver contained only a single class of binding sites with a KA of 6.7 X 10(9) M-1 and a binding capacity of 49 fmol/mg. Hormonal specificity of the sturgeon and Gillichthys hepatic binding sites was studied using methionyl-human GH (met-hGH), ovine prolactin (oPRL), and a crude preparation of sturgeon (st)GH. The met-hGH and stGH inhibited the binding of 125I-bGH to sturgeon liver membranes while only met-hGH displaced labeled bGH from Gillichthys liver membranes. One microgram of oPRL did not significantly inhibit 125I-bGH binding in either membrane assay. Based on these studies, sturgeon hepatic GH receptors seem to be more like those of nonprimate mammals than those of teleosts. Our results, in conjunction with the data of J. N. Fryer (Gen. Comp. Endocrinol. 39, 123-130 (1979)), indicate that considerable evolutionary divergence has occurred among teleost hepatic GH receptors. Thus, vertebrate GH receptors seem to have undergone at least as much evolution as has the hormone itself.
D000818:Animals; D001667:Binding, Competitive; D002462:Cell Membrane / Q000378:metabolism; D010856:Columbidae; D005399:Fishes / Q000378:metabolism*; D013006:Growth Hormone / Q000031:analogs & derivatives / Q000378:metabolism; D019382:Human Growth Hormone; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000378:metabolism*; D008297:Male; D008970:Molecular Weight; D011388:Prolactin / Q000378:metabolism; D011817:Rabbits; D011892:Rana catesbeiana; D011956:Receptors, Cell Surface / Q000378:metabolism*; D011986:Receptors, Somatotropin; D012474:Salmon; D012754:Sharks; D013045:Species Specificity; D013696:Temperature; D014426:Turtles
D011956:Receptors, Cell Surface; D011986:Receptors, Somatotropin; D019382:Human Growth Hormone; D011388:Prolactin; D013006:Growth Hormone