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The Testicular Receptor for Follicle Stimulating Hormone: Structure and Functional Expression of Cloned cDNA
- Source :
- Molecular Endocrinology
- Publication Year :
- 1990
- Publisher :
- The Endocrine Society, 1990.
-
Abstract
- Cloned cDNA encoding the rat Sertoli cell receptor for FSH was isolated from a cognate library and functionally expressed in cultured mammalian cells. The FSH receptor (FSH-R), as predicted from the cDNA, is a single 75K polypeptide with a 348 residue extracellular domain which contains three N-linked glycosylation sites. This domain is connected to a structure containing seven putative transmembrane segments which displays sequence similarity to G protein-coupled receptors. Thus, the FSH-R is identical in its structural design to the LH/CG receptor (LH/CG-R). Furthermore, both receptors display 50% sequence similarity in their large extracellular domains and 80% identity across the seven transmembrane segments. Expression of the cloned cDNA in mammalian cells conferred FSH-dependent cAMP accumulation. The selectivity for FSH is attested by the fact that the related human glycoprotein hormones human CG and human TSH do not stimulate adenylyl cyclase in FSH-R expressing cells even when these hormones are present at high concentrations.
- Subjects :
- Male
endocrine system
Protein Conformation
Recombinant Fusion Proteins
Molecular Sequence Data
Biology
Adenylyl cyclase
chemistry.chemical_compound
Endocrinology
Sequence Homology, Nucleic Acid
Complementary DNA
Animals
Amino Acid Sequence
Receptor
Molecular Biology
G protein-coupled receptor
chemistry.chemical_classification
Sertoli Cells
Base Sequence
DNA
General Medicine
Testicular receptor
Receptors, LH
Molecular biology
Rats
Enzyme Activation
chemistry
Receptors, FSH
Gonadotropin receptor
Follicle Stimulating Hormone
Glycoprotein
Follicle-stimulating hormone receptor
Sequence Alignment
hormones, hormone substitutes, and hormone antagonists
Adenylyl Cyclases
Subjects
Details
- ISSN :
- 19449917 and 08888809
- Volume :
- 4
- Database :
- OpenAIRE
- Journal :
- Molecular Endocrinology
- Accession number :
- edsair.doi.dedup.....8faf5383bf49121bb4c34ffaf985259a
- Full Text :
- https://doi.org/10.1210/mend-4-4-525