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Título

Identification of two isoforms of the Kisspeptin-1 receptor (kiss1r) generated by alternative splicing in a modern teleost, the Senegalese sole (Solea senegalensis)

AutorMechaly, Alejandro S. ; Viñas, Jordi ; Piferrer, Francesc
Palabras claveAlternative splicing
Brain
Fish model
gpr54
Kiss1r
Kisspeptin
Kisspeptin receptor
Kisspeptin-1 receptor
Neuroendocrinology
Puberty
Senegalese sole
Solea senegalensis
Teleost
Fecha de publicación1-ene-2009
EditorSociety for the Study of Reproduction
HighWire Press
CitaciónBiology of Reproduction 80(1): 60-69 (2009)
ResumenThe KISSPEPTIN-1 receptor (KISS1R) and its ligands (KISSPEPTINS) are implicated in the regulation of the onset of puberty. We report the coding region and genomic structure of the kiss1r gene of a modern teleost, the Senegalese sole (Ss). Ss kiss1r cDNA contained an opening frame of 1137 bp, which results in a predicted 378 amino acid protein. Searching genomic databases allowed the identification of kiss1r orthologues in six new species belonging to three vertebrate groups and established the evolutionary relationships of all KISS1R sequences available to date. Analysis of Ss kiss1r revealed for the first time in any vertebrate KISS1R gene the presence of features that are characteristic of a mechanism of alternative splicing. This was confirmed by the identification of two transcripts, Ss kiss1r_v1 and Ss kiss1r_v2. The latter, arising from intron III retention, contained a 27 codons insert in transmembrane region 4 with two stop codons, suggesting it may lead to a truncated protein. The mRNA of the two variants was differently expressed in several tissues. In the brain, levels of the Ss kiss1r_v1 were higher than those of Ss kiss1r_v2. In the gonads, the opposite was observed. Both isoforms exhibited changes depending on sex and maturity stage. The presence of two variants may help to explain some discrepancies observed in past studies regarding KISS1R expression during puberty. Thus, the existence of alternative splicing for the KISS1R gene may contribute to our understanding of the many physiological functions suspected to be mediated by KISSPEPTIN-KISS1R signaling.
Descripción10 pages.-- PMID: 18815354 [PubMed].-- Available online Sep 24, 2008.
Versión del editorhttp://dx.doi.org/10.1095/biolreprod.108.072173
URIhttp://hdl.handle.net/10261/9399
DOI10.1095/biolreprod.108.072173
ISSN0006-3363 (Print)
1529-7268 (Online)
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