Human Opiorphin, a Natural Antinociceptive Modulator of Opioid-Dependent Pathways
Mammalian zinc ectopeptidases play important roles in turning off neural and hormonal peptide signals at the cell surface, notably those processing sensory information. We report here the discovery of a previously uncharacterized physiological inhibitor of enkephalin inactivating zinc ectopeptidases...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2006-11, Vol.103 (47), p.17979-17984 |
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| creator | Wisner, Anne Dufour, Evelyne Messaoudi, Michaël Nejdi, Amine Marcel, Audrey Ungeheuer, Marie-Noelle Rougeot, Catherine |
| description | Mammalian zinc ectopeptidases play important roles in turning off neural and hormonal peptide signals at the cell surface, notably those processing sensory information. We report here the discovery of a previously uncharacterized physiological inhibitor of enkephalin inactivating zinc ectopeptidases in humans, which we have named Opiorphin. It is a QRFSR peptide that inhibits two enkephalin-catabolizing ectoenzymes, human neutral ecto-endopeptidase, hNEP (EC 3.4.24.11), and human ecto-aminopeptidase, hAP-N (EC 3.4.11.2). Opiorphin displays potent analgesic activity in chemical and mechanical pain models by activating endogenous opioid-dependent transmission. Its function is closely related to the rat sialorphin peptide, which is an inhibitor of pain perception and acts by potentiating endogenous μ- and δ-opioid receptor-dependent enkephalinergic pathways. Here we demonstrate the functional specificity in vivo of human Opiorphin. The pain-suppressive potency of Opiorphin is as effective as morphine in the behavioral rat model of acute mechanical pain, the pin-pain test. Thus, our discovery of Opiorphin is extremely exciting from a physiological point of view in the context of endogenous opioidergic pathways, notably in modulating mood-related states and pain sensation. Furthermore, because of its in vivo properties, Opiorphin may have therapeutic implications. |
| doi_str_mv | 10.1073/pnas.0605865103 |
| format | Article |
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We report here the discovery of a previously uncharacterized physiological inhibitor of enkephalin inactivating zinc ectopeptidases in humans, which we have named Opiorphin. It is a QRFSR peptide that inhibits two enkephalin-catabolizing ectoenzymes, human neutral ecto-endopeptidase, hNEP (EC 3.4.24.11), and human ecto-aminopeptidase, hAP-N (EC 3.4.11.2). Opiorphin displays potent analgesic activity in chemical and mechanical pain models by activating endogenous opioid-dependent transmission. Its function is closely related to the rat sialorphin peptide, which is an inhibitor of pain perception and acts by potentiating endogenous μ- and δ-opioid receptor-dependent enkephalinergic pathways. Here we demonstrate the functional specificity in vivo of human Opiorphin. The pain-suppressive potency of Opiorphin is as effective as morphine in the behavioral rat model of acute mechanical pain, the pin-pain test. Thus, our discovery of Opiorphin is extremely exciting from a physiological point of view in the context of endogenous opioidergic pathways, notably in modulating mood-related states and pain sensation. Furthermore, because of its in vivo properties, Opiorphin may have therapeutic implications.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0605865103</identifier><identifier>PMID: 17101991</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Adenosine Deaminase - genetics ; Adenosine Deaminase - metabolism ; Amino Acid Sequence ; Analgesics ; Analgesics - metabolism ; Animals ; Behavior, Animal - physiology ; Biological Sciences ; CD13 Antigens - antagonists & inhibitors ; CD13 Antigens - genetics ; CD13 Antigens - metabolism ; Cell Line ; Cell membranes ; Dipeptidyl Peptidase 4 - genetics ; Dipeptidyl Peptidase 4 - metabolism ; Enkephalins - metabolism ; Enzymes ; Epithelial cells ; Glycoproteins - genetics ; Glycoproteins - metabolism ; HEK293 cells ; Humans ; Male ; Mammals ; Morphine ; Narcotics ; Neprilysin - antagonists & inhibitors ; Neprilysin - genetics ; Neprilysin - metabolism ; Neurons ; Oligopeptides - genetics ; Oligopeptides - metabolism ; Opioid Peptides - genetics ; Opioid Peptides - metabolism ; Pain ; Pain Measurement ; Peptides ; Rats ; Rats, Wistar ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Saliva ; Saliva - chemistry ; Salivary Proteins and Peptides - genetics ; Salivary Proteins and Peptides - metabolism ; Vehicles</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2006-11, Vol.103 (47), p.17979-17984</ispartof><rights>Copyright 2006 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Nov 21, 2006</rights><rights>2006 by The National Academy of Sciences of the USA 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c621t-8b0ef2e676a41ac8c74e79f0fd932d4bb2d04971e7ac0144cee53492763c3eac3</citedby><cites>FETCH-LOGICAL-c621t-8b0ef2e676a41ac8c74e79f0fd932d4bb2d04971e7ac0144cee53492763c3eac3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/103/47.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/30052574$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/30052574$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17101991$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wisner, Anne</creatorcontrib><creatorcontrib>Dufour, Evelyne</creatorcontrib><creatorcontrib>Messaoudi, Michaël</creatorcontrib><creatorcontrib>Nejdi, Amine</creatorcontrib><creatorcontrib>Marcel, Audrey</creatorcontrib><creatorcontrib>Ungeheuer, Marie-Noelle</creatorcontrib><creatorcontrib>Rougeot, Catherine</creatorcontrib><title>Human Opiorphin, a Natural Antinociceptive Modulator of Opioid-Dependent Pathways</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Mammalian zinc ectopeptidases play important roles in turning off neural and hormonal peptide signals at the cell surface, notably those processing sensory information. We report here the discovery of a previously uncharacterized physiological inhibitor of enkephalin inactivating zinc ectopeptidases in humans, which we have named Opiorphin. It is a QRFSR peptide that inhibits two enkephalin-catabolizing ectoenzymes, human neutral ecto-endopeptidase, hNEP (EC 3.4.24.11), and human ecto-aminopeptidase, hAP-N (EC 3.4.11.2). Opiorphin displays potent analgesic activity in chemical and mechanical pain models by activating endogenous opioid-dependent transmission. Its function is closely related to the rat sialorphin peptide, which is an inhibitor of pain perception and acts by potentiating endogenous μ- and δ-opioid receptor-dependent enkephalinergic pathways. Here we demonstrate the functional specificity in vivo of human Opiorphin. The pain-suppressive potency of Opiorphin is as effective as morphine in the behavioral rat model of acute mechanical pain, the pin-pain test. Thus, our discovery of Opiorphin is extremely exciting from a physiological point of view in the context of endogenous opioidergic pathways, notably in modulating mood-related states and pain sensation. Furthermore, because of its in vivo properties, Opiorphin may have therapeutic implications.</description><subject>Adenosine Deaminase - genetics</subject><subject>Adenosine Deaminase - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Analgesics</subject><subject>Analgesics - metabolism</subject><subject>Animals</subject><subject>Behavior, Animal - physiology</subject><subject>Biological Sciences</subject><subject>CD13 Antigens - antagonists & inhibitors</subject><subject>CD13 Antigens - genetics</subject><subject>CD13 Antigens - metabolism</subject><subject>Cell Line</subject><subject>Cell membranes</subject><subject>Dipeptidyl Peptidase 4 - genetics</subject><subject>Dipeptidyl Peptidase 4 - metabolism</subject><subject>Enkephalins - metabolism</subject><subject>Enzymes</subject><subject>Epithelial cells</subject><subject>Glycoproteins - genetics</subject><subject>Glycoproteins - metabolism</subject><subject>HEK293 cells</subject><subject>Humans</subject><subject>Male</subject><subject>Mammals</subject><subject>Morphine</subject><subject>Narcotics</subject><subject>Neprilysin - antagonists & inhibitors</subject><subject>Neprilysin - genetics</subject><subject>Neprilysin - metabolism</subject><subject>Neurons</subject><subject>Oligopeptides - genetics</subject><subject>Oligopeptides - metabolism</subject><subject>Opioid Peptides - genetics</subject><subject>Opioid Peptides - metabolism</subject><subject>Pain</subject><subject>Pain Measurement</subject><subject>Peptides</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Saliva</subject><subject>Saliva - chemistry</subject><subject>Salivary Proteins and Peptides - genetics</subject><subject>Salivary Proteins and Peptides - metabolism</subject><subject>Vehicles</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0c9vFCEUB3BiNHatnj1pJh5MTJz2PWAGuJg09UdNqtVEz4RlGJdmFqYDU-1_L-tuuuqlJw583jcPvoQ8RThCEOx4DCYdQQuNbBsEdo8sEBTWLVdwnywAqKglp_yAPErpEgBUI-EhOUCBgErhgnw9m9cmVBejj9O48uF1ZarPJs-TGaqTkH2I1ls3Zn_tqk-xmweT41TF_s-E7-q3bnShcyFXX0xe_TQ36TF50JshuSe785B8f__u2-lZfX7x4ePpyXltW4q5lktwPXWtaA1HY6UV3AnVQ98pRju-XNIOuBLohLGAnFvnGsYVFS2zzBnLDsmbbe44L9eus2WHsrQeJ782042Oxut_b4Jf6R_xWmOrmGxkCXi5C5ji1exS1mufrBsGE1yck24lCiUV3glRNUCBNwW--A9exnkK5Rc0BWRKlryCjrfITjGlyfW3KyPoTal6U6rel1omnv_90r3ftVhAtQObyX0c01wUpYQq5NUdRPfzMGT3Kxf7bGsvUyn7FjOAhjaCs9-LFcCY</recordid><startdate>20061121</startdate><enddate>20061121</enddate><creator>Wisner, Anne</creator><creator>Dufour, Evelyne</creator><creator>Messaoudi, Michaël</creator><creator>Nejdi, Amine</creator><creator>Marcel, Audrey</creator><creator>Ungeheuer, Marie-Noelle</creator><creator>Rougeot, Catherine</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20061121</creationdate><title>Human Opiorphin, a Natural Antinociceptive Modulator of Opioid-Dependent Pathways</title><author>Wisner, Anne ; 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We report here the discovery of a previously uncharacterized physiological inhibitor of enkephalin inactivating zinc ectopeptidases in humans, which we have named Opiorphin. It is a QRFSR peptide that inhibits two enkephalin-catabolizing ectoenzymes, human neutral ecto-endopeptidase, hNEP (EC 3.4.24.11), and human ecto-aminopeptidase, hAP-N (EC 3.4.11.2). Opiorphin displays potent analgesic activity in chemical and mechanical pain models by activating endogenous opioid-dependent transmission. Its function is closely related to the rat sialorphin peptide, which is an inhibitor of pain perception and acts by potentiating endogenous μ- and δ-opioid receptor-dependent enkephalinergic pathways. Here we demonstrate the functional specificity in vivo of human Opiorphin. The pain-suppressive potency of Opiorphin is as effective as morphine in the behavioral rat model of acute mechanical pain, the pin-pain test. 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| subjects | Adenosine Deaminase - genetics Adenosine Deaminase - metabolism Amino Acid Sequence Analgesics Analgesics - metabolism Animals Behavior, Animal - physiology Biological Sciences CD13 Antigens - antagonists & inhibitors CD13 Antigens - genetics CD13 Antigens - metabolism Cell Line Cell membranes Dipeptidyl Peptidase 4 - genetics Dipeptidyl Peptidase 4 - metabolism Enkephalins - metabolism Enzymes Epithelial cells Glycoproteins - genetics Glycoproteins - metabolism HEK293 cells Humans Male Mammals Morphine Narcotics Neprilysin - antagonists & inhibitors Neprilysin - genetics Neprilysin - metabolism Neurons Oligopeptides - genetics Oligopeptides - metabolism Opioid Peptides - genetics Opioid Peptides - metabolism Pain Pain Measurement Peptides Rats Rats, Wistar Recombinant Proteins - genetics Recombinant Proteins - metabolism Saliva Saliva - chemistry Salivary Proteins and Peptides - genetics Salivary Proteins and Peptides - metabolism Vehicles |
| title | Human Opiorphin, a Natural Antinociceptive Modulator of Opioid-Dependent Pathways |
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