Source:http://linkedlifedata.com/resource/pubmed/id/10764554
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
2000-5-11
|
pubmed:abstractText |
Gonadotropin-releasing hormone receptors (GnRH-Rs) expressed in the pituitary of eutherian species of mammal are unique in lacking the cytoplasmic C-terminal tail characteristic of GnRH-Rs of nonmammalian vertebrates and other G protein-coupled receptors. To further investigate evolutionary relationships among vertebrate GnRH-Rs, a full-coding region cDNA of the pituitary GnRH-R was cloned from a metatherian marsupial mammal, the Australian brushtail possum (Trichosurus vulpecula). We have determined the pharmacological characteristics and internalization kinetics of this GnRH-R from an early evolved, metatherian species of mammal and compared it with the corresponding receptors in eutherian species of mammal and nonmammalian vertebrates. The predicted GnRH-R protein from the possum pituitary has high homology with the other mammalian GnRH-Rs (80% identity) and, in common with other mammals, lacks an intracellular C-terminal tail. The ligand selectivity of the possum GnRH-R transfected into COS-1 cells, assessed using inositol phosphate assays and radioreceptor binding assays, was similar to that of the other mammalian GnRH-Rs, and distinct from those of the nonmammalian GnRH-Rs. The pharmacological characteristics of the possum GnRH-R were similar to those of other mammalian GnRH-Rs, for a selection of agonists (including naturally occurring GnRH ligands and superagonists) and antagonists. Receptor-mediated internalization of GnRH agonist by the possum GnRH-R was slightly more rapid than that of the human GnRH-R, while the internalization kinetics of the chicken GnRH-R, in which a cytoplasmic C-terminal tail is present, was considerably more rapid. In terms of the evolution of the GnRH-R in vertebrates, the possum (a metatherian mammal) GnRH-R has a striking resemblance, in both structure and pharmacological characteristics, to GnRH-Rs in eutherian mammals, which are quite distinct from the nonmammalian vertebrate GnRH-Rs, and are unique among G protein-coupled receptors in lacking an intracellular C-terminal tail. The distinct structure of the pituitary GnRH-R in mammalian vertebrates is likely to have important functional consequences in the reproductive physiology of mammals.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0016-6480
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
117
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
439-48
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:10764554-Amino Acid Sequence,
pubmed-meshheading:10764554-Animals,
pubmed-meshheading:10764554-COS Cells,
pubmed-meshheading:10764554-Cloning, Molecular,
pubmed-meshheading:10764554-Gene Expression,
pubmed-meshheading:10764554-Gonadotropin-Releasing Hormone,
pubmed-meshheading:10764554-Humans,
pubmed-meshheading:10764554-Inositol Phosphates,
pubmed-meshheading:10764554-Kinetics,
pubmed-meshheading:10764554-Mice,
pubmed-meshheading:10764554-Molecular Sequence Data,
pubmed-meshheading:10764554-Opossums,
pubmed-meshheading:10764554-Pituitary Gland,
pubmed-meshheading:10764554-Receptors, LHRH,
pubmed-meshheading:10764554-Sequence Alignment,
pubmed-meshheading:10764554-Sequence Homology, Amino Acid,
pubmed-meshheading:10764554-Transfection
|
pubmed:year |
2000
|
pubmed:articleTitle |
Cloning and expression, pharmacological characterization, and internalization kinetics of the pituitary GnRH receptor in a metatherian species of mammal.
|
pubmed:affiliation |
Department of Chemical Pathology, University of Cape Town Medical School and Groote Schuur Hospital, South Africa. JAKING@chempath.uct.ac.za
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|