Linked Life Data

9849958

Source:http://linkedlifedata.com/resource/pubmed/id/9849958

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1999-2-5
pubmed:databankReference
pubmed:abstractText
The receptors for LH, FSH, and TSH belong to the large G protein-coupled, seven-transmembrane (TM) protein family and are unique in having a large N-terminal extracellular (ecto-) domain containing leucine-rich repeats important for interaction with the glycoprotein ligands. We have identified two new leucine-rich repeat-containing, G protein-coupled receptors and named them as LGR4 and LGR5, respectively. The ectodomains of both receptors contain 17 leucine-rich repeats together with N- and C-terminal flanking cysteine-rich sequences, compared with 9 repeats found in known glycoprotein hormone receptors. The leucine-rich repeats in LGR4 and LGR5 are arrays of 24 amino acids showing similarity to repeats found in the acid labile subunit of the insulin-like growth factor (IGF)/IGF binding protein complexes as well as slit, decorin, and Toll proteins. The TM region and the junction between ectodomain and TM 1 are highly conserved in LGR4, LGR5, and seven other LGRs from sea anemone, fly, nematode, mollusk, and mammal, suggesting their common evolutionary origin. In contrast to the restricted tissue expression of gonadotropin and TSH receptors in gonads and thyroid, respectively, LGR4 is expressed in diverse tissues including ovary, testis, adrenal, placenta, thymus, spinal cord, and thyroid, whereas LGR5 is found in muscle, placenta, spinal cord, and brain. Hybridization analysis of genomic DNA indicated that LGR4 and LGR5 genes are conserved in mammals. Comparison of overall amino acid sequences indicated that LGR4 and LGR5 are closely related to each other but diverge, during evolution, from the homologous receptor found in snail and the mammalian glycoprotein hormone receptors. The identification and characterization of new members of the LGR subfamily of receptor genes not only allow future isolation of their ligands and understanding of their physiological roles but also reveal the evolutionary relationship of G protein-coupled receptors with leucine-rich repeats.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0888-8809
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1830-45
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9849958-Amino Acid Sequence, pubmed-meshheading:9849958-Animals, pubmed-meshheading:9849958-Conserved Sequence, pubmed-meshheading:9849958-DNA, pubmed-meshheading:9849958-Female, pubmed-meshheading:9849958-GTP-Binding Proteins, pubmed-meshheading:9849958-Humans, pubmed-meshheading:9849958-Leucine, pubmed-meshheading:9849958-Male, pubmed-meshheading:9849958-Molecular Sequence Data, pubmed-meshheading:9849958-Organ Specificity, pubmed-meshheading:9849958-Phylogeny, pubmed-meshheading:9849958-Receptors, Cell Surface, pubmed-meshheading:9849958-Receptors, FSH, pubmed-meshheading:9849958-Receptors, G-Protein-Coupled, pubmed-meshheading:9849958-Receptors, LH, pubmed-meshheading:9849958-Receptors, Thyrotropin, pubmed-meshheading:9849958-Repetitive Sequences, Amino Acid, pubmed-meshheading:9849958-Sequence Homology
pubmed:year
1998
pubmed:articleTitle
Characterization of two LGR genes homologous to gonadotropin and thyrotropin receptors with extracellular leucine-rich repeats and a G protein-coupled, seven-transmembrane region.
pubmed:affiliation
Department of Gynecology and Obstetrics, Stanford University Medical School, California 94305-5317, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.