Reference : Identification and modulation of a growth hormone-binding protein in rainbow trout (Onco...
Scientific journals : Article
Life sciences : Anatomy (cytology, histology, embryology...) & physiology
http://hdl.handle.net/2268/24959
Identification and modulation of a growth hormone-binding protein in rainbow trout (Oncorhynchus mykiss) plasma during seawater adaptation.
English
Sohm, F. [> > > >]
Manfroid, Isabelle mailto [Université de Liège - ULg > > GIGA-Research >]
Pezet, A. [> > > >]
Rentier-Delrue, Françoise mailto [Université de Liège - ULg > Département des sciences de la vie > Biologie et génétique moléculaire - GIGA-R : Coordination scientifique >]
Rand-Weaver, M. [> > > >]
Kelly, P. A. [> > > >]
Boeuf, G. [> > > >]
Postel-Vinay, M. C. [> > > >]
de Luze, A. [> > > >]
Edery, M. [> > > >]
1998
General and Comparative Endocrinology
Elsevier
111
2
216-24
Yes (verified by ORBi)
International
0016-6480
1095-6840
New York
NY
[en] Adaptation, Physiological ; Animals ; Binding, Competitive ; Carrier Proteins/metabolism ; Chromatography, High Pressure Liquid ; Fish Proteins ; Glycoproteins/metabolism ; Growth Hormone/metabolism ; Iodine Radioisotopes ; Oncorhynchus mykiss/blood ; Pituitary Hormones/metabolism ; Precipitin Tests ; Receptors, Somatotropin/metabolism ; Recombinant Proteins ; Seawater
[en] A soluble protein that specifically bound 125I-human growth hormone (hGH) was identified in rainbow trout plasma, using HPLC-gel filtration. The binding affinity of the protein for hGH was 1.2 x 10(9)M-1. 125I-rainbow trout GH (tGH) was also able to bind to the protein albeit with a lower affinity (6.6 x 10(7)M-1) than hGH. Crosslinking experiments using 125I-hGH revealed two specific bands of 150 and 130 kDa. The complex 125I-hGH-BP could be precipitated by a monoclonal anti-GH receptor antibody, suggesting a close relationship between the plasma GH-BP and the GH receptor. A fourfold increase in the hGH binding to the GH-BP was shown 48 h after transfer of the fishes from freshwater to seawater. The increase in binding was related to a high binding capacity without significant changes in binding affinity. These results suggest a potential role of this related GH-BP as an index of GH effects during seawater adaptation in salmonids.
http://hdl.handle.net/2268/24959
10.1006/gcen.1998.7106
Copyright 1998 Academic Press.

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