Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-8-17
pubmed:abstractText
Interleukin (IL)-2 is not only an immunoregulatory factor, but also an analgesic molecule. There are distinct domains of immune and analgesic functions in the IL-2 molecule. The analgesic domain is located around the 45th Tyr residue of human IL-2 in tertiary structure. Antiopioid (beta-endorphin, Leu-enkephalin, Met-enkephalin and dynorphin A1-13) sera partially neutralized the analgesic activity of IL-2. Monoclonal antibody against the IL-2 receptor alpha subunit (Tac) could not block the analgesic activity of IL-2. There existed cross-reactivity between IL-2 and antiopioid sera by indirect ELISA. These studies show strong structural and biological similarities between IL-2 and opioid peptides. The tertiary structure around the 45th residue of IL-2 composes the analgesic domain that is similar to that of endogenous opioids. These results are consistent with the hypothesis that multiple domains of cytokines serve as the structural bases for the immunoregulatory and neuroregulatory effects of cytokines.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Analgesics, http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal, http://linkedlifedata.com/resource/pubmed/chemical/Dynorphins, http://linkedlifedata.com/resource/pubmed/chemical/Enkephalin, Leucine, http://linkedlifedata.com/resource/pubmed/chemical/Enkephalin, Methionine, http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2, http://linkedlifedata.com/resource/pubmed/chemical/Opioid Peptides, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Opioid, http://linkedlifedata.com/resource/pubmed/chemical/beta-Endorphin, http://linkedlifedata.com/resource/pubmed/chemical/dynorphin (1-13)
pubmed:status
MEDLINE
pubmed:issn
1021-7401
pubmed:author
pubmed:copyrightInfo
Copyright 2000 S. Karger AG, Basel
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
20-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10859484-Analgesics, pubmed-meshheading:10859484-Animals, pubmed-meshheading:10859484-Antibodies, pubmed-meshheading:10859484-Antibodies, Monoclonal, pubmed-meshheading:10859484-Brain Chemistry, pubmed-meshheading:10859484-Cross Reactions, pubmed-meshheading:10859484-Dynorphins, pubmed-meshheading:10859484-Enkephalin, Leucine, pubmed-meshheading:10859484-Enkephalin, Methionine, pubmed-meshheading:10859484-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:10859484-Humans, pubmed-meshheading:10859484-Interleukin-2, pubmed-meshheading:10859484-Male, pubmed-meshheading:10859484-Mutagenesis, Site-Directed, pubmed-meshheading:10859484-Neuroimmunomodulation, pubmed-meshheading:10859484-Nociceptors, pubmed-meshheading:10859484-Opioid Peptides, pubmed-meshheading:10859484-Pain Threshold, pubmed-meshheading:10859484-Peptide Fragments, pubmed-meshheading:10859484-Protein Structure, Tertiary, pubmed-meshheading:10859484-Rats, pubmed-meshheading:10859484-Rats, Sprague-Dawley, pubmed-meshheading:10859484-Receptors, Opioid, pubmed-meshheading:10859484-Structure-Activity Relationship, pubmed-meshheading:10859484-beta-Endorphin
pubmed:year
2000
pubmed:articleTitle
Interleukin-2: structural and biological relatedness to opioid peptides.
pubmed:affiliation
Department of Neurobiology, Second Military Medical University, Shanghai, People's Republic of China. jiangclk@online.sh.cn
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't