Loading…

Cloning and sequencing of porcine LH-hCG receptor cDNA: variants lacking transmembrane domain

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 a...

Full description

Saved in:
Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1989-08, Vol.245 (4917), p.525-528
Main Authors: Loosfelt, H. (Institut National de la Sante et de la Recherche Medicale Unite, Kremlin Bicetre, France), Misrahi, M, Atger, M, Salesse, R, Vu Hai-Luv Thi, M, Jolivet, A, Guiochon-Mantel, A, Sar, S, Jallal, B, Garnier, J
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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
ISSN:0036-8075
1095-9203
DOI:10.1126/science.2502844