Linked Life Data

11856342

Source:http://linkedlifedata.com/resource/pubmed/id/11856342

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2002-3-7
pubmed:abstractText
Orexin A and B (also known as hypocretins), two recently discovered neuropeptides, play an important role in food intake, sleep/wake cycle and neuroendocrine functions. Orexins are endogenous ligands of two G-protein-coupled receptors, termed OX1 and OX2. This work presents the first short orexin A and B analogues, orexin A 23-33 and orexin B 18-28, with high affinity (119 +/- 49 and 49 +/- 23 nm) for OX1 receptors expressed on SK-N-MC cells and indicates the importance of the C-terminal part of the orexin peptides for this ligand-receptor interaction. However, these C-terminal fragments of orexin did not displace the 125I-labelled orexin B from the recombinant orexin 1 receptor stably expressed in Chinese hamster ovary cells. To examine the role of the shortened orexin A 23-33 in feeding, its effects in mimicking or antagonizing the effects of orexin A were studied in rats after administration via the lateral hypothalamus. In contrast with orexin A, which potently induced feeding up to 4 h after administration, orexin A 23-33 neither induced feeding nor inhibited orexin A-induced feeding. Modafinil (Vigil), which was shown earlier to activate orexin neurons, displayed binding neither to the orexin receptor expressed on SK-N-MC cells nor to the recombinant orexin 1 receptor, which indicates that modafinil displays its antinarcoleptic action via another yet unknown mechanism. PCR and subsequent sequencing revealed expression of the full-length orexin 1 receptor mRNA in SK-N-MC and NT-2 cells. Interestingly, sequencing of several cDNA clones derived from RNA of both SK-N-MC and NT-2 cells differed from the published nucleotide sequence at position 1375. Amino acid prediction of this A -->G change results in an isoleucine --> valine substitution at the protein level, which may provide evidence for an editing process.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1128-35
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed-meshheading:11856342-Amino Acid Sequence, pubmed-meshheading:11856342-Animals, pubmed-meshheading:11856342-Appetite Regulation, pubmed-meshheading:11856342-Binding Sites, pubmed-meshheading:11856342-CHO Cells, pubmed-meshheading:11856342-Carrier Proteins, pubmed-meshheading:11856342-Cell Line, pubmed-meshheading:11856342-Cricetinae, pubmed-meshheading:11856342-Humans, pubmed-meshheading:11856342-Infant, Newborn, pubmed-meshheading:11856342-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:11856342-Male, pubmed-meshheading:11856342-Molecular Sequence Data, pubmed-meshheading:11856342-Neuropeptides, pubmed-meshheading:11856342-Peptide Fragments, pubmed-meshheading:11856342-Protein Binding, pubmed-meshheading:11856342-Rats, pubmed-meshheading:11856342-Receptors, G-Protein-Coupled, pubmed-meshheading:11856342-Receptors, Neuropeptide, pubmed-meshheading:11856342-Recombinant Proteins, pubmed-meshheading:11856342-Sequence Homology, Amino Acid, pubmed-meshheading:11856342-Tumor Cells, Cultured
pubmed:year
2002
pubmed:articleTitle
The SK-N-MC cell line expresses an orexin binding site different from recombinant orexin 1-type receptor.
pubmed:affiliation
Division of Preclinical Research, Boehringer Ingelheim Pharma KG, Biberach, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't