Robert P, Amsellem S, Christophe S, Benifla J L, Bellet D, Koman A, Bidart J M
Laboratoire d'Immunologie CNRS URA 1484, Faculté des Sciences, Pharmaceutiques et Biologiques, Paris, France.
Biochem Biophys Res Commun. 1994 May 30;201(1):201-7. doi: 10.1006/bbrc.1994.1689.
To investigate the possibility that specific structural determinants within the equine follitropin receptor (eFSHR) are critical to the enhanced specificity of this receptor compared to other FSHRs, we used the RACE-PCR technique to clone the eFSHR from equine testis. Sequence analysis revealed that the eFSHR is highly homologous to other mammal FSHRs, but it presents 10 unique amino acid residue replacements in the extracellular domain. Furthermore, a potential N-glycosylation site was detected at a position not encountered in other receptors. Northern blot analysis identified three transcripts of 4.2 kb, 2.3 kb and 1.0 kb in horse testis.