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Fish Growth Hormone Receptor: Molecular Characterization of Two Membrane-Anchored Forms

Institudo de Acuicultura de Torre de la Sal (J.C., J.P.), CSIC, 12595 Ribera de Cabanes, Castellón, Spain; Interactions Cellulaires et Moléculaires (H.D., F.C., D.B.), UMR CNRS/Université de Rennes 1, Campus de Beaulieu, 35042 Rennes, and Observatoire Banyuls (G.B.) CNRS/Université Paris 6, France

Abstract

A RT-PCR approach was used to clone and sequence the full-length growth hormone receptor (GHR) of a teleost fish, the turbot (Scophthalmus maximus). Total liver RNA was amplified by RT-PCR with degenerate primers designed in extracellular and cytoplasmic regions, and a single DNA fragment of 1100 bp was obtained. The entire coding region was obtained by 5’ and 3’ RACE assays, and comprises an open-reading frame of 633 amino acids. This sequence shows the characteristic motifs of the class I cytokine receptor superfamily, and its amino acid identity with mammalian, avian, reptilian and amphibian GHRs is 32–36%. The 3’ RACE also revealed the occurrence of an alternate messenger encoding a membrane-anchored truncated receptor, which could facilitate the production of GH-binding protein in fish species. This report represents the first data on fish GHR sequence, and it provides evidence for the conservation of this receptor throughout vertebrate evolution.

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