Linked Life Data

10490881

Source:http://linkedlifedata.com/resource/pubmed/id/10490881

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-10-12
pubmed:abstractText
Endomorphin-1 and endomorphin-2 are tetrapeptides of the brain whose binding profiles and analgesic activities indicate that they are endogenous ligands at micro opioid receptors. To analyze the classes of G transducer proteins activated by these opioids in the production of supraspinal antinociception, the expression of alpha subunits of the G(i) protein class, G(i1), G(i2), G(i3), G(o1), G(o2), and G(z), and those of the G(q) protein family, G(q) and G(11), was reduced by administration of antisense oligodeoxynucleotides (ODNs) complementary to sequences in their respective mRNAs. The ODN treatments promoted differences in the analgesic effects displayed by morphine, [D-Ala(2),N-MePhe(4), Gly-ol(5)]enkephalin (DAMGO), and the novel opioids endomorphin-1 and endomorphin-2. The impairment of G(i1)alpha and G(i3)alpha function led to a weaker analgesic response to the endomorphins and to the alpha(2)-adrenoceptor agonist clonidine, whereas the effects of morphine and DAMGO were not affected. An antisense probe targeting G(i2)alpha blocked the antinociceptive effects of endomorphin-2, morphine, DAMGO, and clonidine but was without effect on the activity of endomorphin-1. Mice receiving the ODN to G(z)alpha subunits showed impaired response to all agonists. The knockdown of either G(o1)alpha, G(o2)alpha, G(q)alpha, or G(11)alpha had little or no influence on the antinociception induced by any of the opioids in the study. Thus, agonists exhibit differences in activating the variety of GTP-binding proteins regulated by mu opioid receptors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Analgesics, http://linkedlifedata.com/resource/pubmed/chemical/Analgesics, Opioid, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Protein alpha Subunit..., http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Protein alpha..., http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Gnai2 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides, http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Opioid, mu, http://linkedlifedata.com/resource/pubmed/chemical/endomorphin 1, http://linkedlifedata.com/resource/pubmed/chemical/endomorphin 2
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-3565
pubmed:author
pubmed:issnType
Print
pubmed:volume
291
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Endomorphin-1 and endomorphin-2 show differences in their activation of mu opioid receptor-regulated G proteins in supraspinal antinociception in mice.
pubmed:affiliation
Neurofarmacología, Instituto de Neurobiología Santiago Ramón y Cajal, Consejo Superior de Investigaciones Científicas, Madrid, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't