Orphanin FQ/nociceptin and naloxone benzoylhydrazone activate distinct receptors in BE(2)-C human neuroblastoma cells
κ 3 opioid receptors have a unique binding and analgesic profile, as originally defined by naloxone benzoylhydrazone (NalBzoH). Although antisense studies demonstrated the close relationship between κ 3 opioid and Orphan opioid receptor-like receptor (ORL1) and implied they were generated from the s...
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| Veröffentlicht in: | Neuroscience letters 2001-02, Vol.299 (3), p.173-176 |
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| creator | Mathis, John P Mandyam, Chitra D Altememi, Ghazi F Pasternak, Gavril W Standifer, Kelly M |
| description | κ
3 opioid receptors have a unique binding and analgesic profile, as originally defined by naloxone benzoylhydrazone (NalBzoH). Although antisense studies demonstrated the close relationship between
κ
3 opioid and Orphan opioid receptor-like receptor (ORL1) and implied they were generated from the same gene, these studies also revealed differences in the sensitivity profiles of NalBzoH and orphanin FQ/nociceptin (OFQ/N), indicating that they were not identical. To help define the relationship between
κ
3 and ORL1 receptors, we utilized BE(2)-C human neuroblastoma cells that natively express functional ORL1 and
κ
3 opioid receptors.
125I-[Tyr
14]OFQ/N binds to a single population of receptors in BE(2)-C cells. Competition binding and adenylyl cyclase studies clearly illustrated marked selectivity differences between the ORL1 and the
κ
3 sites. Furthermore, antisense DNA targeting ORL1 blocked the inhibition of cAMP by OFQ/N, but not by NalBzoH. Thus, the receptor mechanisms mediating the activity of OFQ/N and NalBzoH in BE(2)-C cells are distinct. |
| doi_str_mv | 10.1016/S0304-3940(01)01524-5 |
| format | Article |
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3 opioid receptors have a unique binding and analgesic profile, as originally defined by naloxone benzoylhydrazone (NalBzoH). Although antisense studies demonstrated the close relationship between
κ
3 opioid and Orphan opioid receptor-like receptor (ORL1) and implied they were generated from the same gene, these studies also revealed differences in the sensitivity profiles of NalBzoH and orphanin FQ/nociceptin (OFQ/N), indicating that they were not identical. To help define the relationship between
κ
3 and ORL1 receptors, we utilized BE(2)-C human neuroblastoma cells that natively express functional ORL1 and
κ
3 opioid receptors.
125I-[Tyr
14]OFQ/N binds to a single population of receptors in BE(2)-C cells. Competition binding and adenylyl cyclase studies clearly illustrated marked selectivity differences between the ORL1 and the
κ
3 sites. Furthermore, antisense DNA targeting ORL1 blocked the inhibition of cAMP by OFQ/N, but not by NalBzoH. Thus, the receptor mechanisms mediating the activity of OFQ/N and NalBzoH in BE(2)-C cells are distinct.</description><identifier>ISSN: 0304-3940</identifier><identifier>EISSN: 1872-7972</identifier><identifier>DOI: 10.1016/S0304-3940(01)01524-5</identifier><identifier>PMID: 11165763</identifier><identifier>CODEN: NELED5</identifier><language>eng</language><publisher>Shannon: Elsevier Ireland Ltd</publisher><subject>Antisense Elements (Genetics) - pharmacology ; Binding Sites - drug effects ; Binding Sites - physiology ; Binding, Competitive - drug effects ; Binding, Competitive - physiology ; Biological and medical sciences ; cAMP ; Cell Membrane - drug effects ; Cell Membrane - metabolism ; Cyclic AMP - metabolism ; Homologous desensitization ; Humans ; Kappa 3 opioid receptor ; Medical sciences ; Naloxone - analogs & derivatives ; Naloxone - pharmacology ; Neuroblastoma ; Neuropharmacology ; Neurotransmitters. Neurotransmission. Receptors ; Nociceptin ; Nociceptin Receptor ; Opioid Peptides - metabolism ; Opioid Peptides - pharmacology ; Orphan opioid receptor-like receptor ; Peptidergic system (neuropeptide, opioid peptide, opiates...). Adenosinergic and purinergic systems ; Pharmacology. Drug treatments ; Radioligand Assay ; Receptors, Opioid - chemistry ; Receptors, Opioid - drug effects ; Receptors, Opioid - metabolism ; Receptors, Opioid, kappa - chemistry ; Receptors, Opioid, kappa - drug effects ; Receptors, Opioid, kappa - metabolism ; Subcellular Fractions - drug effects ; Subcellular Fractions - metabolism ; Tumor Cells, Cultured - drug effects ; Tumor Cells, Cultured - metabolism</subject><ispartof>Neuroscience letters, 2001-02, Vol.299 (3), p.173-176</ispartof><rights>2001 Elsevier Science Ireland Ltd</rights><rights>2001 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c420t-12859fe2af2999c5a1369f16ce88edfad065a1de1c2c5d26d144dc0fd3754403</citedby><cites>FETCH-LOGICAL-c420t-12859fe2af2999c5a1369f16ce88edfad065a1de1c2c5d26d144dc0fd3754403</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0304-3940(01)01524-5$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=879484$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11165763$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mathis, John P</creatorcontrib><creatorcontrib>Mandyam, Chitra D</creatorcontrib><creatorcontrib>Altememi, Ghazi F</creatorcontrib><creatorcontrib>Pasternak, Gavril W</creatorcontrib><creatorcontrib>Standifer, Kelly M</creatorcontrib><title>Orphanin FQ/nociceptin and naloxone benzoylhydrazone activate distinct receptors in BE(2)-C human neuroblastoma cells</title><title>Neuroscience letters</title><addtitle>Neurosci Lett</addtitle><description>κ
3 opioid receptors have a unique binding and analgesic profile, as originally defined by naloxone benzoylhydrazone (NalBzoH). Although antisense studies demonstrated the close relationship between
κ
3 opioid and Orphan opioid receptor-like receptor (ORL1) and implied they were generated from the same gene, these studies also revealed differences in the sensitivity profiles of NalBzoH and orphanin FQ/nociceptin (OFQ/N), indicating that they were not identical. To help define the relationship between
κ
3 and ORL1 receptors, we utilized BE(2)-C human neuroblastoma cells that natively express functional ORL1 and
κ
3 opioid receptors.
125I-[Tyr
14]OFQ/N binds to a single population of receptors in BE(2)-C cells. Competition binding and adenylyl cyclase studies clearly illustrated marked selectivity differences between the ORL1 and the
κ
3 sites. Furthermore, antisense DNA targeting ORL1 blocked the inhibition of cAMP by OFQ/N, but not by NalBzoH. Thus, the receptor mechanisms mediating the activity of OFQ/N and NalBzoH in BE(2)-C cells are distinct.</description><subject>Antisense Elements (Genetics) - pharmacology</subject><subject>Binding Sites - drug effects</subject><subject>Binding Sites - physiology</subject><subject>Binding, Competitive - drug effects</subject><subject>Binding, Competitive - physiology</subject><subject>Biological and medical sciences</subject><subject>cAMP</subject><subject>Cell Membrane - drug effects</subject><subject>Cell Membrane - metabolism</subject><subject>Cyclic AMP - metabolism</subject><subject>Homologous desensitization</subject><subject>Humans</subject><subject>Kappa 3 opioid receptor</subject><subject>Medical sciences</subject><subject>Naloxone - analogs & derivatives</subject><subject>Naloxone - pharmacology</subject><subject>Neuroblastoma</subject><subject>Neuropharmacology</subject><subject>Neurotransmitters. Neurotransmission. Receptors</subject><subject>Nociceptin</subject><subject>Nociceptin Receptor</subject><subject>Opioid Peptides - metabolism</subject><subject>Opioid Peptides - pharmacology</subject><subject>Orphan opioid receptor-like receptor</subject><subject>Peptidergic system (neuropeptide, opioid peptide, opiates...). Adenosinergic and purinergic systems</subject><subject>Pharmacology. Drug treatments</subject><subject>Radioligand Assay</subject><subject>Receptors, Opioid - chemistry</subject><subject>Receptors, Opioid - drug effects</subject><subject>Receptors, Opioid - metabolism</subject><subject>Receptors, Opioid, kappa - chemistry</subject><subject>Receptors, Opioid, kappa - drug effects</subject><subject>Receptors, Opioid, kappa - metabolism</subject><subject>Subcellular Fractions - drug effects</subject><subject>Subcellular Fractions - metabolism</subject><subject>Tumor Cells, Cultured - drug effects</subject><subject>Tumor Cells, Cultured - metabolism</subject><issn>0304-3940</issn><issn>1872-7972</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkd9rFDEQx4Mo9qz-CUpAkPZhbSabH7tPRY9WhUIR-x5yySwX2U3OZLd4_evd7R31sU9hhs83M8yHkPfAPgMDdfGL1UxUdSvYGYNzBpKLSr4gK2g0r3Sr-UuyekJOyJtSfjPGJEjxmpwAgJJa1Ssy3ebd1sYQ6fXPi5hccLgb58pGT6Pt098UkW4wPqR9v937bB-WhnVjuLcjUh_KTLuRZlyCKRc6h79enfHzak2302AjjTjltOltGdNgqcO-L2_Jq872Bd8d31Nyd311t_5e3dx--7H-clM5wdlYAW9k2yG3HW_b1kkLtWo7UA6bBn1nPVNzzyM47qTnyoMQ3rHO11oKwepT8unw7S6nPxOW0QyhLAvYiGkqRjPFNZfyWRB0o4DxZgblAXQ5lZKxM7scBpv3BphZvJhHL2Y5umFgHr2YZcCH44BpM6D_nzqKmIGPR8AWZ_su2-hCeeIa3YpGzNTlgcL5aPcBsykuYHTowyxgND6FZxb5B2j2qpY</recordid><startdate>20010223</startdate><enddate>20010223</enddate><creator>Mathis, John P</creator><creator>Mandyam, Chitra D</creator><creator>Altememi, Ghazi F</creator><creator>Pasternak, Gavril W</creator><creator>Standifer, Kelly M</creator><general>Elsevier Ireland Ltd</general><general>Elsevier</general><scope>IQODW</scope><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>7TK</scope><scope>7X8</scope></search><sort><creationdate>20010223</creationdate><title>Orphanin FQ/nociceptin and naloxone benzoylhydrazone activate distinct receptors in BE(2)-C human neuroblastoma cells</title><author>Mathis, John P ; Mandyam, Chitra D ; Altememi, Ghazi F ; Pasternak, Gavril W ; Standifer, Kelly M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c420t-12859fe2af2999c5a1369f16ce88edfad065a1de1c2c5d26d144dc0fd3754403</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Antisense Elements (Genetics) - pharmacology</topic><topic>Binding Sites - drug effects</topic><topic>Binding Sites - physiology</topic><topic>Binding, Competitive - drug effects</topic><topic>Binding, Competitive - physiology</topic><topic>Biological and medical sciences</topic><topic>cAMP</topic><topic>Cell Membrane - drug effects</topic><topic>Cell Membrane - metabolism</topic><topic>Cyclic AMP - metabolism</topic><topic>Homologous desensitization</topic><topic>Humans</topic><topic>Kappa 3 opioid receptor</topic><topic>Medical sciences</topic><topic>Naloxone - analogs & derivatives</topic><topic>Naloxone - pharmacology</topic><topic>Neuroblastoma</topic><topic>Neuropharmacology</topic><topic>Neurotransmitters. Neurotransmission. Receptors</topic><topic>Nociceptin</topic><topic>Nociceptin Receptor</topic><topic>Opioid Peptides - metabolism</topic><topic>Opioid Peptides - pharmacology</topic><topic>Orphan opioid receptor-like receptor</topic><topic>Peptidergic system (neuropeptide, opioid peptide, opiates...). Adenosinergic and purinergic systems</topic><topic>Pharmacology. Drug treatments</topic><topic>Radioligand Assay</topic><topic>Receptors, Opioid - chemistry</topic><topic>Receptors, Opioid - drug effects</topic><topic>Receptors, Opioid - metabolism</topic><topic>Receptors, Opioid, kappa - chemistry</topic><topic>Receptors, Opioid, kappa - drug effects</topic><topic>Receptors, Opioid, kappa - metabolism</topic><topic>Subcellular Fractions - drug effects</topic><topic>Subcellular Fractions - metabolism</topic><topic>Tumor Cells, Cultured - drug effects</topic><topic>Tumor Cells, Cultured - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mathis, John P</creatorcontrib><creatorcontrib>Mandyam, Chitra D</creatorcontrib><creatorcontrib>Altememi, Ghazi F</creatorcontrib><creatorcontrib>Pasternak, Gavril W</creatorcontrib><creatorcontrib>Standifer, Kelly M</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Neuroscience letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mathis, John P</au><au>Mandyam, Chitra D</au><au>Altememi, Ghazi F</au><au>Pasternak, Gavril W</au><au>Standifer, Kelly M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Orphanin FQ/nociceptin and naloxone benzoylhydrazone activate distinct receptors in BE(2)-C human neuroblastoma cells</atitle><jtitle>Neuroscience letters</jtitle><addtitle>Neurosci Lett</addtitle><date>2001-02-23</date><risdate>2001</risdate><volume>299</volume><issue>3</issue><spage>173</spage><epage>176</epage><pages>173-176</pages><issn>0304-3940</issn><eissn>1872-7972</eissn><coden>NELED5</coden><abstract>κ
3 opioid receptors have a unique binding and analgesic profile, as originally defined by naloxone benzoylhydrazone (NalBzoH). Although antisense studies demonstrated the close relationship between
κ
3 opioid and Orphan opioid receptor-like receptor (ORL1) and implied they were generated from the same gene, these studies also revealed differences in the sensitivity profiles of NalBzoH and orphanin FQ/nociceptin (OFQ/N), indicating that they were not identical. To help define the relationship between
κ
3 and ORL1 receptors, we utilized BE(2)-C human neuroblastoma cells that natively express functional ORL1 and
κ
3 opioid receptors.
125I-[Tyr
14]OFQ/N binds to a single population of receptors in BE(2)-C cells. Competition binding and adenylyl cyclase studies clearly illustrated marked selectivity differences between the ORL1 and the
κ
3 sites. Furthermore, antisense DNA targeting ORL1 blocked the inhibition of cAMP by OFQ/N, but not by NalBzoH. Thus, the receptor mechanisms mediating the activity of OFQ/N and NalBzoH in BE(2)-C cells are distinct.</abstract><cop>Shannon</cop><pub>Elsevier Ireland Ltd</pub><pmid>11165763</pmid><doi>10.1016/S0304-3940(01)01524-5</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0304-3940 |
| ispartof | Neuroscience letters, 2001-02, Vol.299 (3), p.173-176 |
| issn | 0304-3940 1872-7972 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_70627255 |
| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Antisense Elements (Genetics) - pharmacology Binding Sites - drug effects Binding Sites - physiology Binding, Competitive - drug effects Binding, Competitive - physiology Biological and medical sciences cAMP Cell Membrane - drug effects Cell Membrane - metabolism Cyclic AMP - metabolism Homologous desensitization Humans Kappa 3 opioid receptor Medical sciences Naloxone - analogs & derivatives Naloxone - pharmacology Neuroblastoma Neuropharmacology Neurotransmitters. Neurotransmission. Receptors Nociceptin Nociceptin Receptor Opioid Peptides - metabolism Opioid Peptides - pharmacology Orphan opioid receptor-like receptor Peptidergic system (neuropeptide, opioid peptide, opiates...). Adenosinergic and purinergic systems Pharmacology. Drug treatments Radioligand Assay Receptors, Opioid - chemistry Receptors, Opioid - drug effects Receptors, Opioid - metabolism Receptors, Opioid, kappa - chemistry Receptors, Opioid, kappa - drug effects Receptors, Opioid, kappa - metabolism Subcellular Fractions - drug effects Subcellular Fractions - metabolism Tumor Cells, Cultured - drug effects Tumor Cells, Cultured - metabolism |
| title | Orphanin FQ/nociceptin and naloxone benzoylhydrazone activate distinct receptors in BE(2)-C human neuroblastoma cells |
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