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Science 4 August 1989: Vol. 245. no. 4917, pp. 525 - 528 DOI: 10.1126/science.2502844
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Articles
Science, Vol 245, Issue 4917, 525-528
Copyright © 1989 by American Association for the Advancement of Science
Cloning and sequencing of porcine LH-hCG receptor cDNA: variants lacking transmembrane domain
H Loosfelt,
M Misrahi,
M Atger,
R Salesse,
MT Vu Hai-Luu Thi,
A Jolivet,
A Guiochon-Mantel,
S Sar,
B Jallal,
J Garnier,
and
al. et
Institut National de la Sante et de la Recherche Medicale Unite 135, Hopital de Bicetre, France.
Complementary DNA clones, encoding the LH-hCG (luteinizing hormone-human choriogonadotropic hormone) receptor were isolated by screening a lambda gt11 library with monoclonal antibodies. The primary structure of the protein was deduced from the DNA sequence analysis; the protein contains 696 amino acids with a putative signal peptide of 27 amino acids. Hydropathy analysis suggests the existence of seven transmembrane domains that show homology with the corresponding regions of other G protein-coupled receptors. Three other types of clones corresponding to shorter proteins were observed, in which the putative transmembrane domain was absent. These probably arose through alternative splicing. RNA blot analysis showed similar patterns in testis and ovary with a major RNA of 4700 nucleotides and several minor species. The messenger RNA was expressed in COS-7 cells, yielding a protein that bound hCG with the same affinity as the testicular receptor.
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