Loading…
Biological importance of the peptides of the calcitonin family as revealed by disruption and transfer of corresponding genes
The hormone calcitonin (CT) of thyroid C-cell origin, the neuropeptides α- and β-calcitonin gene-related peptide (CGRP), the widely expressed hormone and tissue factor adrenomedullin (AM), and amylin (AMY) that is co-produced with insulin in pancreatic β-cells, are structurally related peptides. The...
Saved in:
Published in: | Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2004-11, Vol.25 (11), p.2027-2038 |
---|---|
Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c425t-e4ec1d7d260b7d174842388dd6452677525dddac20baf925dbe56974d5437e803 |
---|---|
cites | cdi_FETCH-LOGICAL-c425t-e4ec1d7d260b7d174842388dd6452677525dddac20baf925dbe56974d5437e803 |
container_end_page | 2038 |
container_issue | 11 |
container_start_page | 2027 |
container_title | Peptides (New York, N.Y. : 1980) |
container_volume | 25 |
creator | Muff, Roman Born, Walter Lutz, Thomas A. Fischer, Jan A. |
description | The hormone calcitonin (CT) of thyroid C-cell origin, the neuropeptides α- and β-calcitonin gene-related peptide (CGRP), the widely expressed hormone and tissue factor adrenomedullin (AM), and amylin (AMY) that is co-produced with insulin in pancreatic β-cells, are structurally related peptides. They have in common six or seven amino acid ring structures, linked by disulfide bridges between cysteine residues, and amidated carboxyl termini that are both required for biological activity. The actions of the peptides in vivo have traditionally been studied after intravenous and intracerebroventricular administration. As a result, CT lowers serum calcium and reduces pain perception. α- and βCGRP and AM are highly potent vasodilatory peptides. AMY inhibits food intake through its action in the area postrema of the brain. Physiological actions of the peptides summarized in the present review have been defined through gene knockout and overexpression strategies. |
doi_str_mv | 10.1016/j.peptides.2004.08.007 |
format | article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_67006650</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S019697810400364X</els_id><sourcerecordid>17280152</sourcerecordid><originalsourceid>FETCH-LOGICAL-c425t-e4ec1d7d260b7d174842388dd6452677525dddac20baf925dbe56974d5437e803</originalsourceid><addsrcrecordid>eNqFkc1u1DAURi0EotPCK1TewC7BdvyXHVABRarEBtaWY98MHiV2sDOVRurD49HMqMuurCud717rOwjdUtJSQuWnXbvAsgYPpWWE8JbolhD1Cm2oVl0jqOxfow2hvWx6pekVui5lRyrIe_0WXVEhCBWd2qCnryFNaRucnXCYl5RXGx3gNOL1L-DLjctcKRfWFEPEo53DdMC24AyPYCfweDhgH0re10yK2EaP12xjGSEf8y7lDGVJ0Ye4xVuIUN6hN6OdCrw_vzfoz_dvv-_um4dfP37efXloHGdibYCDo155JsmgPFVcc9Zp7b3kgkmlBBPee-sYGezY12EAIXvFveCdAk26G_TxtHfJ6d8eymrmUBxMk42Q9sVIRYiU4mWQKqZrcayC8gS6nErJMJolh9nmg6HEHAWZnbmUZ46CDNGmCqrB2_OF_TCDf46djVTgwxmwpdY91gZdKM-cZJwr0lfu84mDWtxjgGyKC1Dd-ZDBrcan8NJf_gNohrQT</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17280152</pqid></control><display><type>article</type><title>Biological importance of the peptides of the calcitonin family as revealed by disruption and transfer of corresponding genes</title><source>Elsevier</source><creator>Muff, Roman ; Born, Walter ; Lutz, Thomas A. ; Fischer, Jan A.</creator><creatorcontrib>Muff, Roman ; Born, Walter ; Lutz, Thomas A. ; Fischer, Jan A.</creatorcontrib><description>The hormone calcitonin (CT) of thyroid C-cell origin, the neuropeptides α- and β-calcitonin gene-related peptide (CGRP), the widely expressed hormone and tissue factor adrenomedullin (AM), and amylin (AMY) that is co-produced with insulin in pancreatic β-cells, are structurally related peptides. They have in common six or seven amino acid ring structures, linked by disulfide bridges between cysteine residues, and amidated carboxyl termini that are both required for biological activity. The actions of the peptides in vivo have traditionally been studied after intravenous and intracerebroventricular administration. As a result, CT lowers serum calcium and reduces pain perception. α- and βCGRP and AM are highly potent vasodilatory peptides. AMY inhibits food intake through its action in the area postrema of the brain. Physiological actions of the peptides summarized in the present review have been defined through gene knockout and overexpression strategies.</description><identifier>ISSN: 0196-9781</identifier><identifier>EISSN: 1873-5169</identifier><identifier>DOI: 10.1016/j.peptides.2004.08.007</identifier><identifier>PMID: 15501537</identifier><identifier>CODEN: PPTDD5</identifier><language>eng</language><publisher>New York, NY: Elsevier Inc</publisher><subject>Adenoviridae - genetics ; Adrenomedullin ; Amylin ; Amyloid - chemistry ; Amyloid - physiology ; Animals ; Apud cells. Peptide and protein hormones. Growth factors ; Biological and medical sciences ; Calcitonin - chemistry ; Calcitonin - genetics ; Calcitonin - physiology ; Calcitonin Gene-Related Peptide ; Fundamental and applied biological sciences. Psychology ; Gene Expression ; Gene Transfer Techniques ; Genetic Therapy ; Humans ; Knockout ; Mice ; Mice, Knockout ; Peptides - chemistry ; Peptides - genetics ; Peptides - physiology ; Transgene ; Transgenes ; Vertebrates: endocrinology</subject><ispartof>Peptides (New York, N.Y. : 1980), 2004-11, Vol.25 (11), p.2027-2038</ispartof><rights>2004 Elsevier Inc.</rights><rights>2005 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c425t-e4ec1d7d260b7d174842388dd6452677525dddac20baf925dbe56974d5437e803</citedby><cites>FETCH-LOGICAL-c425t-e4ec1d7d260b7d174842388dd6452677525dddac20baf925dbe56974d5437e803</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>309,310,314,780,784,789,790,23930,23931,25140,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16244709$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15501537$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Muff, Roman</creatorcontrib><creatorcontrib>Born, Walter</creatorcontrib><creatorcontrib>Lutz, Thomas A.</creatorcontrib><creatorcontrib>Fischer, Jan A.</creatorcontrib><title>Biological importance of the peptides of the calcitonin family as revealed by disruption and transfer of corresponding genes</title><title>Peptides (New York, N.Y. : 1980)</title><addtitle>Peptides</addtitle><description>The hormone calcitonin (CT) of thyroid C-cell origin, the neuropeptides α- and β-calcitonin gene-related peptide (CGRP), the widely expressed hormone and tissue factor adrenomedullin (AM), and amylin (AMY) that is co-produced with insulin in pancreatic β-cells, are structurally related peptides. They have in common six or seven amino acid ring structures, linked by disulfide bridges between cysteine residues, and amidated carboxyl termini that are both required for biological activity. The actions of the peptides in vivo have traditionally been studied after intravenous and intracerebroventricular administration. As a result, CT lowers serum calcium and reduces pain perception. α- and βCGRP and AM are highly potent vasodilatory peptides. AMY inhibits food intake through its action in the area postrema of the brain. Physiological actions of the peptides summarized in the present review have been defined through gene knockout and overexpression strategies.</description><subject>Adenoviridae - genetics</subject><subject>Adrenomedullin</subject><subject>Amylin</subject><subject>Amyloid - chemistry</subject><subject>Amyloid - physiology</subject><subject>Animals</subject><subject>Apud cells. Peptide and protein hormones. Growth factors</subject><subject>Biological and medical sciences</subject><subject>Calcitonin - chemistry</subject><subject>Calcitonin - genetics</subject><subject>Calcitonin - physiology</subject><subject>Calcitonin Gene-Related Peptide</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression</subject><subject>Gene Transfer Techniques</subject><subject>Genetic Therapy</subject><subject>Humans</subject><subject>Knockout</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Peptides - chemistry</subject><subject>Peptides - genetics</subject><subject>Peptides - physiology</subject><subject>Transgene</subject><subject>Transgenes</subject><subject>Vertebrates: endocrinology</subject><issn>0196-9781</issn><issn>1873-5169</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><recordid>eNqFkc1u1DAURi0EotPCK1TewC7BdvyXHVABRarEBtaWY98MHiV2sDOVRurD49HMqMuurCud717rOwjdUtJSQuWnXbvAsgYPpWWE8JbolhD1Cm2oVl0jqOxfow2hvWx6pekVui5lRyrIe_0WXVEhCBWd2qCnryFNaRucnXCYl5RXGx3gNOL1L-DLjctcKRfWFEPEo53DdMC24AyPYCfweDhgH0re10yK2EaP12xjGSEf8y7lDGVJ0Ye4xVuIUN6hN6OdCrw_vzfoz_dvv-_um4dfP37efXloHGdibYCDo155JsmgPFVcc9Zp7b3kgkmlBBPee-sYGezY12EAIXvFveCdAk26G_TxtHfJ6d8eymrmUBxMk42Q9sVIRYiU4mWQKqZrcayC8gS6nErJMJolh9nmg6HEHAWZnbmUZ46CDNGmCqrB2_OF_TCDf46djVTgwxmwpdY91gZdKM-cZJwr0lfu84mDWtxjgGyKC1Dd-ZDBrcan8NJf_gNohrQT</recordid><startdate>20041101</startdate><enddate>20041101</enddate><creator>Muff, Roman</creator><creator>Born, Walter</creator><creator>Lutz, Thomas A.</creator><creator>Fischer, Jan A.</creator><general>Elsevier Inc</general><general>Elsevier Science</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>7QP</scope><scope>7TK</scope><scope>7X8</scope></search><sort><creationdate>20041101</creationdate><title>Biological importance of the peptides of the calcitonin family as revealed by disruption and transfer of corresponding genes</title><author>Muff, Roman ; Born, Walter ; Lutz, Thomas A. ; Fischer, Jan A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c425t-e4ec1d7d260b7d174842388dd6452677525dddac20baf925dbe56974d5437e803</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Adenoviridae - genetics</topic><topic>Adrenomedullin</topic><topic>Amylin</topic><topic>Amyloid - chemistry</topic><topic>Amyloid - physiology</topic><topic>Animals</topic><topic>Apud cells. Peptide and protein hormones. Growth factors</topic><topic>Biological and medical sciences</topic><topic>Calcitonin - chemistry</topic><topic>Calcitonin - genetics</topic><topic>Calcitonin - physiology</topic><topic>Calcitonin Gene-Related Peptide</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression</topic><topic>Gene Transfer Techniques</topic><topic>Genetic Therapy</topic><topic>Humans</topic><topic>Knockout</topic><topic>Mice</topic><topic>Mice, Knockout</topic><topic>Peptides - chemistry</topic><topic>Peptides - genetics</topic><topic>Peptides - physiology</topic><topic>Transgene</topic><topic>Transgenes</topic><topic>Vertebrates: endocrinology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Muff, Roman</creatorcontrib><creatorcontrib>Born, Walter</creatorcontrib><creatorcontrib>Lutz, Thomas A.</creatorcontrib><creatorcontrib>Fischer, Jan A.</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>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Peptides (New York, N.Y. : 1980)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Muff, Roman</au><au>Born, Walter</au><au>Lutz, Thomas A.</au><au>Fischer, Jan A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biological importance of the peptides of the calcitonin family as revealed by disruption and transfer of corresponding genes</atitle><jtitle>Peptides (New York, N.Y. : 1980)</jtitle><addtitle>Peptides</addtitle><date>2004-11-01</date><risdate>2004</risdate><volume>25</volume><issue>11</issue><spage>2027</spage><epage>2038</epage><pages>2027-2038</pages><issn>0196-9781</issn><eissn>1873-5169</eissn><coden>PPTDD5</coden><abstract>The hormone calcitonin (CT) of thyroid C-cell origin, the neuropeptides α- and β-calcitonin gene-related peptide (CGRP), the widely expressed hormone and tissue factor adrenomedullin (AM), and amylin (AMY) that is co-produced with insulin in pancreatic β-cells, are structurally related peptides. They have in common six or seven amino acid ring structures, linked by disulfide bridges between cysteine residues, and amidated carboxyl termini that are both required for biological activity. The actions of the peptides in vivo have traditionally been studied after intravenous and intracerebroventricular administration. As a result, CT lowers serum calcium and reduces pain perception. α- and βCGRP and AM are highly potent vasodilatory peptides. AMY inhibits food intake through its action in the area postrema of the brain. Physiological actions of the peptides summarized in the present review have been defined through gene knockout and overexpression strategies.</abstract><cop>New York, NY</cop><pub>Elsevier Inc</pub><pmid>15501537</pmid><doi>10.1016/j.peptides.2004.08.007</doi><tpages>12</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0196-9781 |
ispartof | Peptides (New York, N.Y. : 1980), 2004-11, Vol.25 (11), p.2027-2038 |
issn | 0196-9781 1873-5169 |
language | eng |
recordid | cdi_proquest_miscellaneous_67006650 |
source | Elsevier |
subjects | Adenoviridae - genetics Adrenomedullin Amylin Amyloid - chemistry Amyloid - physiology Animals Apud cells. Peptide and protein hormones. Growth factors Biological and medical sciences Calcitonin - chemistry Calcitonin - genetics Calcitonin - physiology Calcitonin Gene-Related Peptide Fundamental and applied biological sciences. Psychology Gene Expression Gene Transfer Techniques Genetic Therapy Humans Knockout Mice Mice, Knockout Peptides - chemistry Peptides - genetics Peptides - physiology Transgene Transgenes Vertebrates: endocrinology |
title | Biological importance of the peptides of the calcitonin family as revealed by disruption and transfer of corresponding genes |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-21T12%3A49%3A04IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Biological%20importance%20of%20the%20peptides%20of%20the%20calcitonin%20family%20as%20revealed%20by%20disruption%20and%20transfer%20of%20corresponding%20genes&rft.jtitle=Peptides%20(New%20York,%20N.Y.%20:%201980)&rft.au=Muff,%20Roman&rft.date=2004-11-01&rft.volume=25&rft.issue=11&rft.spage=2027&rft.epage=2038&rft.pages=2027-2038&rft.issn=0196-9781&rft.eissn=1873-5169&rft.coden=PPTDD5&rft_id=info:doi/10.1016/j.peptides.2004.08.007&rft_dat=%3Cproquest_cross%3E17280152%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c425t-e4ec1d7d260b7d174842388dd6452677525dddac20baf925dbe56974d5437e803%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=17280152&rft_id=info:pmid/15501537&rfr_iscdi=true |