The rat dermorphin-like immunoreactivity is supported by an aminopeptidase resistant peptide
Site-directed antibodies against synthetic related dermorphin peptides were previously produced and characterized. One of them, which specifically recognizes the crucial `opioid message' (the N-terminal part of the dermorphin molecule (i.e. Tyr– d-Ala–Phe–Gly) was selected in order to detect an...
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| Veröffentlicht in: | Journal of neuroimmunology 1998, Vol.81 (1), p.211-224 |
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| creator | Cucumel, K Bagnol, D Moinier, D Fischer, J Conrath, M Cupo, A |
| description | Site-directed antibodies against synthetic related dermorphin peptides were previously produced and characterized. One of them, which specifically recognizes the crucial `opioid message' (the N-terminal part of the dermorphin molecule (i.e. Tyr–
d-Ala–Phe–Gly) was selected in order to detect and locate endogenous dermorphin-like molecules in rat, mouse and guinea pig tissues. Dermorphin-like peptides were found to be present in tissues known to contain peptides such as neurons in the central nervous system, nerve fibers in the gut and B and T immune cells. With all the tissues assayed, the HPLC profile obtained on the immunoreactive material showed the same main peak eluted at a retention time of 32±1 min. The results of biochemical experiments in which enzymatic treatments were performed on the dermorphin-like immunoreactivity indicate the immunoreactivity is a peptide resistant to aminopeptidase hydrolysis. This finding suggests the presence of a residue conferring resistance to proteolytic processes of this kind, which is likely to be a
d-amino acid residue. |
| doi_str_mv | 10.1016/S0165-5728(97)00182-3 |
| format | Article |
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d-Ala–Phe–Gly) was selected in order to detect and locate endogenous dermorphin-like molecules in rat, mouse and guinea pig tissues. Dermorphin-like peptides were found to be present in tissues known to contain peptides such as neurons in the central nervous system, nerve fibers in the gut and B and T immune cells. With all the tissues assayed, the HPLC profile obtained on the immunoreactive material showed the same main peak eluted at a retention time of 32±1 min. The results of biochemical experiments in which enzymatic treatments were performed on the dermorphin-like immunoreactivity indicate the immunoreactivity is a peptide resistant to aminopeptidase hydrolysis. This finding suggests the presence of a residue conferring resistance to proteolytic processes of this kind, which is likely to be a
d-amino acid residue.</description><identifier>ISSN: 0165-5728</identifier><identifier>EISSN: 1872-8421</identifier><identifier>DOI: 10.1016/S0165-5728(97)00182-3</identifier><identifier>PMID: 9521624</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Aminopeptidase resistance ; Aminopeptidases - pharmacology ; Animals ; Brain Chemistry ; Chromatography, High Pressure Liquid ; Colon - chemistry ; Colon - cytology ; Dermorphin-like immunoreactivity ; Digestive System - chemistry ; Endopeptidases - metabolism ; Guinea Pigs ; Gut ; HPLC characterization ; Immune tissues ; Immunoenzyme Techniques ; Lymphocyte Subsets - chemistry ; Male ; Methionyl Aminopeptidases ; Mice ; Mice, Inbred BALB C ; Nerve Tissue Proteins - analysis ; Nerve Tissue Proteins - chemistry ; Nerve Tissue Proteins - metabolism ; Neuroimmunomodulation ; Neurons - chemistry ; Neuropeptides - analysis ; Oligopeptides - analysis ; Oligopeptides - chemistry ; Oligopeptides - metabolism ; Opioid Peptides ; Organ Specificity ; Peptide Fragments - chemical synthesis ; Peptide Fragments - immunology ; Peripheral Nerves - chemistry ; Pituitary gland ; Pituitary Gland - chemistry ; Radioimmunoassay ; Rats ; Rats, Sprague-Dawley ; Rats, Wistar ; Site-directed dermorphin antibodies ; Species Specificity ; Spleen - chemistry</subject><ispartof>Journal of neuroimmunology, 1998, Vol.81 (1), p.211-224</ispartof><rights>1998 Elsevier Science B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c391t-35fcb8be2ce235f0b50a4f554ea44a8f02a21bf8215ea6a4f8135ea8e9b34423</citedby><cites>FETCH-LOGICAL-c391t-35fcb8be2ce235f0b50a4f554ea44a8f02a21bf8215ea6a4f8135ea8e9b34423</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0165-5728(97)00182-3$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,4010,27904,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9521624$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cucumel, K</creatorcontrib><creatorcontrib>Bagnol, D</creatorcontrib><creatorcontrib>Moinier, D</creatorcontrib><creatorcontrib>Fischer, J</creatorcontrib><creatorcontrib>Conrath, M</creatorcontrib><creatorcontrib>Cupo, A</creatorcontrib><title>The rat dermorphin-like immunoreactivity is supported by an aminopeptidase resistant peptide</title><title>Journal of neuroimmunology</title><addtitle>J Neuroimmunol</addtitle><description>Site-directed antibodies against synthetic related dermorphin peptides were previously produced and characterized. One of them, which specifically recognizes the crucial `opioid message' (the N-terminal part of the dermorphin molecule (i.e. Tyr–
d-Ala–Phe–Gly) was selected in order to detect and locate endogenous dermorphin-like molecules in rat, mouse and guinea pig tissues. Dermorphin-like peptides were found to be present in tissues known to contain peptides such as neurons in the central nervous system, nerve fibers in the gut and B and T immune cells. With all the tissues assayed, the HPLC profile obtained on the immunoreactive material showed the same main peak eluted at a retention time of 32±1 min. The results of biochemical experiments in which enzymatic treatments were performed on the dermorphin-like immunoreactivity indicate the immunoreactivity is a peptide resistant to aminopeptidase hydrolysis. This finding suggests the presence of a residue conferring resistance to proteolytic processes of this kind, which is likely to be a
d-amino acid residue.</description><subject>Aminopeptidase resistance</subject><subject>Aminopeptidases - pharmacology</subject><subject>Animals</subject><subject>Brain Chemistry</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Colon - chemistry</subject><subject>Colon - cytology</subject><subject>Dermorphin-like immunoreactivity</subject><subject>Digestive System - chemistry</subject><subject>Endopeptidases - metabolism</subject><subject>Guinea Pigs</subject><subject>Gut</subject><subject>HPLC characterization</subject><subject>Immune tissues</subject><subject>Immunoenzyme Techniques</subject><subject>Lymphocyte Subsets - chemistry</subject><subject>Male</subject><subject>Methionyl Aminopeptidases</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Nerve Tissue Proteins - analysis</subject><subject>Nerve Tissue Proteins - chemistry</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neuroimmunomodulation</subject><subject>Neurons - chemistry</subject><subject>Neuropeptides - analysis</subject><subject>Oligopeptides - analysis</subject><subject>Oligopeptides - chemistry</subject><subject>Oligopeptides - metabolism</subject><subject>Opioid Peptides</subject><subject>Organ Specificity</subject><subject>Peptide Fragments - chemical synthesis</subject><subject>Peptide Fragments - immunology</subject><subject>Peripheral Nerves - chemistry</subject><subject>Pituitary gland</subject><subject>Pituitary Gland - chemistry</subject><subject>Radioimmunoassay</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Rats, Wistar</subject><subject>Site-directed dermorphin antibodies</subject><subject>Species Specificity</subject><subject>Spleen - chemistry</subject><issn>0165-5728</issn><issn>1872-8421</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LAzEURYMotVZ_QiEr0cXoJJN0kpVI8QsKLuxSCJnMGxrtfJhkCv33pp3SbTfJI_fkXTgITUn6QFIye_yKB094TsWdzO_TlAiaZGdoTEROE8EoOUfjI3KJrrz_iRDPmByhkeSUzCgbo-_lCrDTAZfg6tZ1K9ska_sL2NZ137QOtAl2Y8MWW49933WtC1DiYot1g3Vtm7aDLthS-7gGvPVBNwEPb3CNLiq99nBzuCdo-fqynL8ni8-3j_nzIjGZJCHJeGUKUQA1QOOcFjzVrOKcgWZMiyqlmpKiEpRw0LMYCZLFSYAsMsZoNkG3w9rOtX89-KBq6w2s17qBtvcqlzlnhGYnwahEzISUEeQDaFzrvYNKdc7W2m0VSdXOvtrbVzu1SuZqb1_tCqaHgr6ooTz-OuiO-dOQQ7SxseCUNxYaA6V1YIIqW3ui4R9Qq5Yr</recordid><startdate>1998</startdate><enddate>1998</enddate><creator>Cucumel, K</creator><creator>Bagnol, D</creator><creator>Moinier, D</creator><creator>Fischer, J</creator><creator>Conrath, M</creator><creator>Cupo, A</creator><general>Elsevier B.V</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>7TK</scope><scope>7X8</scope></search><sort><creationdate>1998</creationdate><title>The rat dermorphin-like immunoreactivity is supported by an aminopeptidase resistant peptide</title><author>Cucumel, K ; Bagnol, D ; Moinier, D ; Fischer, J ; Conrath, M ; Cupo, A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c391t-35fcb8be2ce235f0b50a4f554ea44a8f02a21bf8215ea6a4f8135ea8e9b34423</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Aminopeptidase resistance</topic><topic>Aminopeptidases - pharmacology</topic><topic>Animals</topic><topic>Brain Chemistry</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Colon - chemistry</topic><topic>Colon - cytology</topic><topic>Dermorphin-like immunoreactivity</topic><topic>Digestive System - chemistry</topic><topic>Endopeptidases - metabolism</topic><topic>Guinea Pigs</topic><topic>Gut</topic><topic>HPLC characterization</topic><topic>Immune tissues</topic><topic>Immunoenzyme Techniques</topic><topic>Lymphocyte Subsets - chemistry</topic><topic>Male</topic><topic>Methionyl Aminopeptidases</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Nerve Tissue Proteins - analysis</topic><topic>Nerve Tissue Proteins - chemistry</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Neuroimmunomodulation</topic><topic>Neurons - chemistry</topic><topic>Neuropeptides - analysis</topic><topic>Oligopeptides - analysis</topic><topic>Oligopeptides - chemistry</topic><topic>Oligopeptides - metabolism</topic><topic>Opioid Peptides</topic><topic>Organ Specificity</topic><topic>Peptide Fragments - chemical synthesis</topic><topic>Peptide Fragments - immunology</topic><topic>Peripheral Nerves - chemistry</topic><topic>Pituitary gland</topic><topic>Pituitary Gland - chemistry</topic><topic>Radioimmunoassay</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>Rats, Wistar</topic><topic>Site-directed dermorphin antibodies</topic><topic>Species Specificity</topic><topic>Spleen - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cucumel, K</creatorcontrib><creatorcontrib>Bagnol, D</creatorcontrib><creatorcontrib>Moinier, D</creatorcontrib><creatorcontrib>Fischer, J</creatorcontrib><creatorcontrib>Conrath, M</creatorcontrib><creatorcontrib>Cupo, A</creatorcontrib><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>Journal of neuroimmunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cucumel, K</au><au>Bagnol, D</au><au>Moinier, D</au><au>Fischer, J</au><au>Conrath, M</au><au>Cupo, A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The rat dermorphin-like immunoreactivity is supported by an aminopeptidase resistant peptide</atitle><jtitle>Journal of neuroimmunology</jtitle><addtitle>J Neuroimmunol</addtitle><date>1998</date><risdate>1998</risdate><volume>81</volume><issue>1</issue><spage>211</spage><epage>224</epage><pages>211-224</pages><issn>0165-5728</issn><eissn>1872-8421</eissn><abstract>Site-directed antibodies against synthetic related dermorphin peptides were previously produced and characterized. One of them, which specifically recognizes the crucial `opioid message' (the N-terminal part of the dermorphin molecule (i.e. Tyr–
d-Ala–Phe–Gly) was selected in order to detect and locate endogenous dermorphin-like molecules in rat, mouse and guinea pig tissues. Dermorphin-like peptides were found to be present in tissues known to contain peptides such as neurons in the central nervous system, nerve fibers in the gut and B and T immune cells. With all the tissues assayed, the HPLC profile obtained on the immunoreactive material showed the same main peak eluted at a retention time of 32±1 min. The results of biochemical experiments in which enzymatic treatments were performed on the dermorphin-like immunoreactivity indicate the immunoreactivity is a peptide resistant to aminopeptidase hydrolysis. This finding suggests the presence of a residue conferring resistance to proteolytic processes of this kind, which is likely to be a
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| fulltext | fulltext |
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| ispartof | Journal of neuroimmunology, 1998, Vol.81 (1), p.211-224 |
| issn | 0165-5728 1872-8421 |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Aminopeptidase resistance Aminopeptidases - pharmacology Animals Brain Chemistry Chromatography, High Pressure Liquid Colon - chemistry Colon - cytology Dermorphin-like immunoreactivity Digestive System - chemistry Endopeptidases - metabolism Guinea Pigs Gut HPLC characterization Immune tissues Immunoenzyme Techniques Lymphocyte Subsets - chemistry Male Methionyl Aminopeptidases Mice Mice, Inbred BALB C Nerve Tissue Proteins - analysis Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - metabolism Neuroimmunomodulation Neurons - chemistry Neuropeptides - analysis Oligopeptides - analysis Oligopeptides - chemistry Oligopeptides - metabolism Opioid Peptides Organ Specificity Peptide Fragments - chemical synthesis Peptide Fragments - immunology Peripheral Nerves - chemistry Pituitary gland Pituitary Gland - chemistry Radioimmunoassay Rats Rats, Sprague-Dawley Rats, Wistar Site-directed dermorphin antibodies Species Specificity Spleen - chemistry |
| title | The rat dermorphin-like immunoreactivity is supported by an aminopeptidase resistant peptide |
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