Neurones and Neuropeptides in Coelenterates
The first nervous system probably evolved in coelenterates. Many neurones in coelenterates have morphological characteristics of both sensory and motor neurones, and appear to be multifunctional. Using immunocytochemistry with antisera to the sequence Arg-Phe-NH2 (RFamide), RFamide-like peptides wer...
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| Veröffentlicht in: | Archives of Histology and Cytology 1989, Vol.52(Supplement), pp.265-276 |
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| container_end_page | 276 |
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| container_issue | Supplement |
| container_start_page | 265 |
| container_title | Archives of Histology and Cytology |
| container_volume | 52 |
| creator | GRIMMELIKHUIJZEN, C. J. P. GRAFF, D. MCFARLANE, I. D. |
| description | The first nervous system probably evolved in coelenterates. Many neurones in coelenterates have morphological characteristics of both sensory and motor neurones, and appear to be multifunctional. Using immunocytochemistry with antisera to the sequence Arg-Phe-NH2 (RFamide), RFamide-like peptides were demonstrated in the nervous systems of all classes of coelenterates. Using a radioimmunoassay for RFamide, three such peptides were isolated from the sea anemone Anthopleura elegantissisma and sequenced: |
| doi_str_mv | 10.1679/aohc.52.Suppl_265 |
| format | Article |
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J. P. ; GRAFF, D. ; MCFARLANE, I. D.</creator><creatorcontrib>GRIMMELIKHUIJZEN, C. J. P. ; GRAFF, D. ; MCFARLANE, I. D.</creatorcontrib><description><![CDATA[The first nervous system probably evolved in coelenterates. Many neurones in coelenterates have morphological characteristics of both sensory and motor neurones, and appear to be multifunctional. Using immunocytochemistry with antisera to the sequence Arg-Phe-NH2 (RFamide), RFamide-like peptides were demonstrated in the nervous systems of all classes of coelenterates. Using a radioimmunoassay for RFamide, three such peptides were isolated from the sea anemone Anthopleura elegantissisma and sequenced: <Glu-Gly-Arg-Phe-NH2 (Antho-RFamide), <Glu-Ser-Leu-Arg-Trp-NH2 (Antho-RWamide I) and <Glu-Gly-Leu-Arg-Trp-NH2 (Antho-RWamide II). The general structure of these peptides can be described as <Glu…Arg-X-NH2, where X is an aromatic amino acid. From the hydromedusa Polyorchis penicillatus, the peptide <Glu-Leu-Leu-Gly-Gly-Arg-Phe-NH2 (Pol-RFamide I) was isolated, which also belongs to the <Glu…Arg-X-NH2 family. Using specific antisera it was shown that all four peptides were located in neurones. Application of low doses of Antho-RFamide, or Antho-RWamide I or II induced contractions of endodermal muscles of sea anemones. This indicates that these neuropeptides play a role in neurotransmission.]]></description><identifier>ISSN: 0914-9465</identifier><identifier>EISSN: 1349-1717</identifier><identifier>DOI: 10.1679/aohc.52.Suppl_265</identifier><identifier>PMID: 2573382</identifier><language>eng</language><publisher>Japan: International Society of Histology and Cytology</publisher><subject>Animals ; Cnidaria - physiology ; Immunohistochemistry ; Neurons - cytology ; Neurons - metabolism ; Neuropeptides - metabolism ; Neuropeptides - physiology</subject><ispartof>Archives of Histology and Cytology, 1989, Vol.52(Supplement), pp.265-276</ispartof><rights>International Society of Histology and Cytology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5005-3bb7158a8fc169ff49149883e7d3ddc985107c3ab68e7c6bd5a5c099577390423</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,1876,4009,27902,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2573382$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>GRIMMELIKHUIJZEN, C. J. P.</creatorcontrib><creatorcontrib>GRAFF, D.</creatorcontrib><creatorcontrib>MCFARLANE, I. D.</creatorcontrib><title>Neurones and Neuropeptides in Coelenterates</title><title>Archives of Histology and Cytology</title><addtitle>Arch. Histol. Cytol.</addtitle><description><![CDATA[The first nervous system probably evolved in coelenterates. Many neurones in coelenterates have morphological characteristics of both sensory and motor neurones, and appear to be multifunctional. Using immunocytochemistry with antisera to the sequence Arg-Phe-NH2 (RFamide), RFamide-like peptides were demonstrated in the nervous systems of all classes of coelenterates. Using a radioimmunoassay for RFamide, three such peptides were isolated from the sea anemone Anthopleura elegantissisma and sequenced: <Glu-Gly-Arg-Phe-NH2 (Antho-RFamide), <Glu-Ser-Leu-Arg-Trp-NH2 (Antho-RWamide I) and <Glu-Gly-Leu-Arg-Trp-NH2 (Antho-RWamide II). The general structure of these peptides can be described as <Glu…Arg-X-NH2, where X is an aromatic amino acid. From the hydromedusa Polyorchis penicillatus, the peptide <Glu-Leu-Leu-Gly-Gly-Arg-Phe-NH2 (Pol-RFamide I) was isolated, which also belongs to the <Glu…Arg-X-NH2 family. Using specific antisera it was shown that all four peptides were located in neurones. Application of low doses of Antho-RFamide, or Antho-RWamide I or II induced contractions of endodermal muscles of sea anemones. This indicates that these neuropeptides play a role in neurotransmission.]]></description><subject>Animals</subject><subject>Cnidaria - physiology</subject><subject>Immunohistochemistry</subject><subject>Neurons - cytology</subject><subject>Neurons - metabolism</subject><subject>Neuropeptides - metabolism</subject><subject>Neuropeptides - physiology</subject><issn>0914-9465</issn><issn>1349-1717</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkElPwzAQhS0EKqXwAzgg9cQFpXiJY_uIqrJIFRxYrpZjT2iqbNjJgX-PuygHTqOZN--N_SF0TfCCZELdm3ZjF5wu3oeuqzTN-AmaEpaqhAgiTtEUK5ImKs34OboIYYsxo4ySCZpQLhiTdIruXmHwbQNhbho33zcddH3p4qRs5ssWKmh68KaHcInOClMFuDrWGfp8XH0sn5P129PL8mGdWI4xT1ieC8KlkYUlmSqKND5CSclAOOacVZITLCwzeSZB2Cx33HCLleJCMIVTymbo9pDb-fZngNDrugwWqso00A5BC8UYp5LERXJYtL4NwUOhO1_Wxv9qgvUOkN4B0pzqEVD03BzDh7wGNzqORKL-ddC3oTffMOrG96WtYJ9I4nfGVKgjoH9dPDQa7MZ4DQ37A2XPgvA</recordid><startdate>1989</startdate><enddate>1989</enddate><creator>GRIMMELIKHUIJZEN, C. J. P.</creator><creator>GRAFF, D.</creator><creator>MCFARLANE, I. D.</creator><general>International Society of Histology and Cytology</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>7X8</scope></search><sort><creationdate>1989</creationdate><title>Neurones and Neuropeptides in Coelenterates</title><author>GRIMMELIKHUIJZEN, C. J. P. ; GRAFF, D. ; MCFARLANE, I. D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5005-3bb7158a8fc169ff49149883e7d3ddc985107c3ab68e7c6bd5a5c099577390423</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Animals</topic><topic>Cnidaria - physiology</topic><topic>Immunohistochemistry</topic><topic>Neurons - cytology</topic><topic>Neurons - metabolism</topic><topic>Neuropeptides - metabolism</topic><topic>Neuropeptides - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>GRIMMELIKHUIJZEN, C. J. P.</creatorcontrib><creatorcontrib>GRAFF, D.</creatorcontrib><creatorcontrib>MCFARLANE, I. D.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of Histology and Cytology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>GRIMMELIKHUIJZEN, C. J. P.</au><au>GRAFF, D.</au><au>MCFARLANE, I. D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Neurones and Neuropeptides in Coelenterates</atitle><jtitle>Archives of Histology and Cytology</jtitle><addtitle>Arch. Histol. Cytol.</addtitle><date>1989</date><risdate>1989</risdate><volume>52</volume><issue>Supplement</issue><spage>265</spage><epage>276</epage><pages>265-276</pages><issn>0914-9465</issn><eissn>1349-1717</eissn><abstract><![CDATA[The first nervous system probably evolved in coelenterates. Many neurones in coelenterates have morphological characteristics of both sensory and motor neurones, and appear to be multifunctional. Using immunocytochemistry with antisera to the sequence Arg-Phe-NH2 (RFamide), RFamide-like peptides were demonstrated in the nervous systems of all classes of coelenterates. Using a radioimmunoassay for RFamide, three such peptides were isolated from the sea anemone Anthopleura elegantissisma and sequenced: <Glu-Gly-Arg-Phe-NH2 (Antho-RFamide), <Glu-Ser-Leu-Arg-Trp-NH2 (Antho-RWamide I) and <Glu-Gly-Leu-Arg-Trp-NH2 (Antho-RWamide II). The general structure of these peptides can be described as <Glu…Arg-X-NH2, where X is an aromatic amino acid. From the hydromedusa Polyorchis penicillatus, the peptide <Glu-Leu-Leu-Gly-Gly-Arg-Phe-NH2 (Pol-RFamide I) was isolated, which also belongs to the <Glu…Arg-X-NH2 family. Using specific antisera it was shown that all four peptides were located in neurones. Application of low doses of Antho-RFamide, or Antho-RWamide I or II induced contractions of endodermal muscles of sea anemones. This indicates that these neuropeptides play a role in neurotransmission.]]></abstract><cop>Japan</cop><pub>International Society of Histology and Cytology</pub><pmid>2573382</pmid><doi>10.1679/aohc.52.Suppl_265</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Archives of Histology and Cytology, 1989, Vol.52(Supplement), pp.265-276 |
| issn | 0914-9465 1349-1717 |
| language | eng |
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| source | J-STAGE Free; MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Animals Cnidaria - physiology Immunohistochemistry Neurons - cytology Neurons - metabolism Neuropeptides - metabolism Neuropeptides - physiology |
| title | Neurones and Neuropeptides in Coelenterates |
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