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| Reference : Characterization of a single prolactin (PRL) receptor in tilapia (Oreochromis niloticus)... |
| Scientific journals : Article | |||
| Life sciences : Biochemistry, biophysics & molecular biology | |||
| http://hdl.handle.net/2268/19846 | |||
| Characterization of a single prolactin (PRL) receptor in tilapia (Oreochromis niloticus) which binds both PRLI and PRLII | |
| English | |
| Auperin, B. [> > > >] | |
Rentier-Delrue, Françoise  [Université de Liège - ULg > Département des sciences de la vie > Biologie et génétique moléculaire - GIGA-R : Coordination scientifique >] | |
| Martial, Joseph [Université de Liège - ULg > Département des sciences de la vie > GIGA-R : Biologie et génétique moléculaire >] | |
| Prunet, P. [> > > >] | |
| 1994 | |
| Journal of Molecular Endocrinology | |
| Society for Endocrinology | |
| 13 | |
| 3 | |
| 241-51 | |
| Yes (verified by ORBi) | |
| 0952-5041 | |
| 1479-6813 | |
| Bristol | |
| United Kingdom | |
| [en] Animals ; Binding, Competitive ; Cell Membrane/metabolism ; Gills/*metabolism ; Kidney/*metabolism ; Kinetics ; Liver/metabolism ; Prolactin/*metabolism ; Protein Binding ; Receptors, Prolactin/*metabolism ; Recombinant Proteins/metabolism ; Skin/metabolism ; Temperature ; Tilapia/*metabolism ; Water-Electrolyte Balance/physiology | |
| [en] In tilapia, there are two forms of prolactin (PRL) whose effects on sodium and chloride movements differ and depend on the living environment of the fish. To see whether different receptors or the same receptor mediates these different effects, we have characterized the specific binding of both forms of tilapia (ti)PRL in two osmoregulatory organs, the gill and kidney. Two recombinant tiPRLs were used for this analysis. The recombinant hormones had the same properties as the native hormones in a tilapia gill radioreceptor assay. Specific binding to gill and kidney membranes was increased by optimizing the quality of the tissue preparations (physiological state of fish, membrane preparation) and the incubation conditions (pH, salt concentrations, temperature, time). Under these optimized conditions, we detected only one class of high affinity PRL receptor in gill and kidney. Its binding affinity was higher for tiPRLI than for tiPRLII in both gill and kidney (for tiPRLI the respective affinity values were 2.9 and 2.3 x 10(10) per M, for tiPRLII they were 1.9 and 0.5 x 10(10) per M). In competition studies, tiPRLI was more potent, followed by tiPRLII and ovine (o)PRL. tiGH and oGH did not significantly displace either tiPRL. The receptor we have characterized thus recognizes quite specifically both tiPRLs. | |
| http://hdl.handle.net/2268/19846 | |
| http://jme.endocrinology-journals.org/cgi/reprint/13/3/241 | |
| 1994/12/01 |
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