Glucagon-like peptide-1 binding to rat skeletal muscle
We have found [ 125I]glucagon-like peptide-1(7–36)-amide-specific binding activity in rat skeletal muscle plasma membranes, with an estimated M r of 63,000 by cross-linking and SDS-PAGE. The specific binding was time and membrane protein concentration dependent, and displaceable by unlabeled GLP-1(7...
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Veröffentlicht in: | Peptides (New York, N.Y. : 1980) N.Y. : 1980), 1995, Vol.16 (2), p.225-229 |
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container_title | Peptides (New York, N.Y. : 1980) |
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creator | Delgado, E. Luque, M.A. Alcántara, A. Trapote, M.A. Clemente, F. Galera, C. Valverde, I. Villanueva-Peñacarrillo, M.L. |
description | We have found [
125I]glucagon-like peptide-1(7–36)-amide-specific binding activity in rat skeletal muscle plasma membranes, with an estimated
M
r
of 63,000 by cross-linking and SDS-PAGE. The specific binding was time and membrane protein concentration dependent, and displaceable by unlabeled GLP-1(7–36)-amide with an ID
50 of 3 × 10
−9
M of the peptide; GLP-1(1–36)-amide also competed, whereas glucagon and insulin did not. GLP-1(7–36)-amide did not modify the basal adenylate cyclase activity in skeletal muscle plasma membranes. These data, together with our previous finding of a potent glycogenic effect of GLP-1(7–36)-amide in rat soleus muscle, and also in isolated hepatocytes, which was not accompanied by a rise in the cell cyclic AMP content, lead us to believe that the insulin-like effects of this peptide on glucose metabolism in the muscle could be mediated by a type of receptor somehow different to that described for GLP-1 in pancreatic B cells, where GLP-1 action is mediated by the cyclic AMP-adenylate cyclase system. |
doi_str_mv | 10.1016/0196-9781(94)00175-8 |
format | Article |
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125I]glucagon-like peptide-1(7–36)-amide-specific binding activity in rat skeletal muscle plasma membranes, with an estimated
M
r
of 63,000 by cross-linking and SDS-PAGE. The specific binding was time and membrane protein concentration dependent, and displaceable by unlabeled GLP-1(7–36)-amide with an ID
50 of 3 × 10
−9
M of the peptide; GLP-1(1–36)-amide also competed, whereas glucagon and insulin did not. GLP-1(7–36)-amide did not modify the basal adenylate cyclase activity in skeletal muscle plasma membranes. These data, together with our previous finding of a potent glycogenic effect of GLP-1(7–36)-amide in rat soleus muscle, and also in isolated hepatocytes, which was not accompanied by a rise in the cell cyclic AMP content, lead us to believe that the insulin-like effects of this peptide on glucose metabolism in the muscle could be mediated by a type of receptor somehow different to that described for GLP-1 in pancreatic B cells, where GLP-1 action is mediated by the cyclic AMP-adenylate cyclase system.</description><identifier>ISSN: 0196-9781</identifier><identifier>EISSN: 1873-5169</identifier><identifier>DOI: 10.1016/0196-9781(94)00175-8</identifier><identifier>PMID: 7784253</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adenylyl Cyclases - metabolism ; Animals ; Binding ; Binding, Competitive ; Cell Membrane ; GLP-1(7–36)-amide ; Glucagon - metabolism ; Glucagon-Like Peptide 1 ; Glucagon-Like Peptide-1 Receptor ; Glucagon-Like Peptides ; Insulin - metabolism ; Membranes ; Muscle, Skeletal - metabolism ; Peptide Fragments - metabolism ; Protein Precursors - metabolism ; Rat skeletal muscle ; Rats ; Rats, Wistar ; Receptor, Insulin - drug effects ; Receptor, Insulin - metabolism ; Receptors, Glucagon - isolation & purification ; Receptors, Glucagon - metabolism</subject><ispartof>Peptides (New York, N.Y. : 1980), 1995, Vol.16 (2), p.225-229</ispartof><rights>1995</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-10393adc77ccef415b574211c55b28f9a6dd41ac4de2979a79e4843add8d80a33</citedby><cites>FETCH-LOGICAL-c357t-10393adc77ccef415b574211c55b28f9a6dd41ac4de2979a79e4843add8d80a33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0196-9781(94)00175-8$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,4024,27923,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7784253$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Delgado, E.</creatorcontrib><creatorcontrib>Luque, M.A.</creatorcontrib><creatorcontrib>Alcántara, A.</creatorcontrib><creatorcontrib>Trapote, M.A.</creatorcontrib><creatorcontrib>Clemente, F.</creatorcontrib><creatorcontrib>Galera, C.</creatorcontrib><creatorcontrib>Valverde, I.</creatorcontrib><creatorcontrib>Villanueva-Peñacarrillo, M.L.</creatorcontrib><title>Glucagon-like peptide-1 binding to rat skeletal muscle</title><title>Peptides (New York, N.Y. : 1980)</title><addtitle>Peptides</addtitle><description>We have found [
125I]glucagon-like peptide-1(7–36)-amide-specific binding activity in rat skeletal muscle plasma membranes, with an estimated
M
r
of 63,000 by cross-linking and SDS-PAGE. The specific binding was time and membrane protein concentration dependent, and displaceable by unlabeled GLP-1(7–36)-amide with an ID
50 of 3 × 10
−9
M of the peptide; GLP-1(1–36)-amide also competed, whereas glucagon and insulin did not. GLP-1(7–36)-amide did not modify the basal adenylate cyclase activity in skeletal muscle plasma membranes. These data, together with our previous finding of a potent glycogenic effect of GLP-1(7–36)-amide in rat soleus muscle, and also in isolated hepatocytes, which was not accompanied by a rise in the cell cyclic AMP content, lead us to believe that the insulin-like effects of this peptide on glucose metabolism in the muscle could be mediated by a type of receptor somehow different to that described for GLP-1 in pancreatic B cells, where GLP-1 action is mediated by the cyclic AMP-adenylate cyclase system.</description><subject>Adenylyl Cyclases - metabolism</subject><subject>Animals</subject><subject>Binding</subject><subject>Binding, Competitive</subject><subject>Cell Membrane</subject><subject>GLP-1(7–36)-amide</subject><subject>Glucagon - metabolism</subject><subject>Glucagon-Like Peptide 1</subject><subject>Glucagon-Like Peptide-1 Receptor</subject><subject>Glucagon-Like Peptides</subject><subject>Insulin - metabolism</subject><subject>Membranes</subject><subject>Muscle, Skeletal - metabolism</subject><subject>Peptide Fragments - metabolism</subject><subject>Protein Precursors - metabolism</subject><subject>Rat skeletal muscle</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Receptor, Insulin - drug effects</subject><subject>Receptor, Insulin - metabolism</subject><subject>Receptors, Glucagon - isolation & purification</subject><subject>Receptors, Glucagon - metabolism</subject><issn>0196-9781</issn><issn>1873-5169</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LwzAYx4Moc06_gUJPoodq0qRNchFk6BQGXvQc0uTpiEtfTFrBb2_rxo6ensP_jeeH0CXBdwST4h4TWaSSC3Ij2S3GhOepOEJzIjhNc1LIYzQ_WE7RWYyfGGPGpJihGeeCZTmdo2LlB6M3bZN6t4Wkg653FlKSlK6xrtkkfZsE3SdxCx567ZN6iMbDOTqptI9wsb8L9PH89L58Sddvq9fl4zo1NOd9SjCVVFvDuTFQMZKXOWcZISbPy0xUUhfWMqINs5BJLjWXwAQbE1ZYgTWlC3S96-1C-zVA7FXtogHvdQPtEBXnlOFMTEa2M5rQxhigUl1wtQ4_imA14VITCzWxUJKpP1xKjLGrff9Q1mAPoT2fUX_Y6TA--e0gqGgcNAasC2B6ZVv3_8Avwwt4Yg</recordid><startdate>1995</startdate><enddate>1995</enddate><creator>Delgado, E.</creator><creator>Luque, M.A.</creator><creator>Alcántara, A.</creator><creator>Trapote, M.A.</creator><creator>Clemente, F.</creator><creator>Galera, C.</creator><creator>Valverde, I.</creator><creator>Villanueva-Peñacarrillo, M.L.</creator><general>Elsevier Inc</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>1995</creationdate><title>Glucagon-like peptide-1 binding to rat skeletal muscle</title><author>Delgado, E. ; Luque, M.A. ; Alcántara, A. ; Trapote, M.A. ; Clemente, F. ; Galera, C. ; Valverde, I. ; Villanueva-Peñacarrillo, M.L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-10393adc77ccef415b574211c55b28f9a6dd41ac4de2979a79e4843add8d80a33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Adenylyl Cyclases - metabolism</topic><topic>Animals</topic><topic>Binding</topic><topic>Binding, Competitive</topic><topic>Cell Membrane</topic><topic>GLP-1(7–36)-amide</topic><topic>Glucagon - metabolism</topic><topic>Glucagon-Like Peptide 1</topic><topic>Glucagon-Like Peptide-1 Receptor</topic><topic>Glucagon-Like Peptides</topic><topic>Insulin - metabolism</topic><topic>Membranes</topic><topic>Muscle, Skeletal - metabolism</topic><topic>Peptide Fragments - metabolism</topic><topic>Protein Precursors - metabolism</topic><topic>Rat skeletal muscle</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Receptor, Insulin - drug effects</topic><topic>Receptor, Insulin - metabolism</topic><topic>Receptors, Glucagon - isolation & purification</topic><topic>Receptors, Glucagon - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Delgado, E.</creatorcontrib><creatorcontrib>Luque, M.A.</creatorcontrib><creatorcontrib>Alcántara, A.</creatorcontrib><creatorcontrib>Trapote, M.A.</creatorcontrib><creatorcontrib>Clemente, F.</creatorcontrib><creatorcontrib>Galera, C.</creatorcontrib><creatorcontrib>Valverde, I.</creatorcontrib><creatorcontrib>Villanueva-Peñacarrillo, M.L.</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>Peptides (New York, N.Y. : 1980)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Delgado, E.</au><au>Luque, M.A.</au><au>Alcántara, A.</au><au>Trapote, M.A.</au><au>Clemente, F.</au><au>Galera, C.</au><au>Valverde, I.</au><au>Villanueva-Peñacarrillo, M.L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Glucagon-like peptide-1 binding to rat skeletal muscle</atitle><jtitle>Peptides (New York, N.Y. : 1980)</jtitle><addtitle>Peptides</addtitle><date>1995</date><risdate>1995</risdate><volume>16</volume><issue>2</issue><spage>225</spage><epage>229</epage><pages>225-229</pages><issn>0196-9781</issn><eissn>1873-5169</eissn><abstract>We have found [
125I]glucagon-like peptide-1(7–36)-amide-specific binding activity in rat skeletal muscle plasma membranes, with an estimated
M
r
of 63,000 by cross-linking and SDS-PAGE. The specific binding was time and membrane protein concentration dependent, and displaceable by unlabeled GLP-1(7–36)-amide with an ID
50 of 3 × 10
−9
M of the peptide; GLP-1(1–36)-amide also competed, whereas glucagon and insulin did not. GLP-1(7–36)-amide did not modify the basal adenylate cyclase activity in skeletal muscle plasma membranes. These data, together with our previous finding of a potent glycogenic effect of GLP-1(7–36)-amide in rat soleus muscle, and also in isolated hepatocytes, which was not accompanied by a rise in the cell cyclic AMP content, lead us to believe that the insulin-like effects of this peptide on glucose metabolism in the muscle could be mediated by a type of receptor somehow different to that described for GLP-1 in pancreatic B cells, where GLP-1 action is mediated by the cyclic AMP-adenylate cyclase system.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7784253</pmid><doi>10.1016/0196-9781(94)00175-8</doi><tpages>5</tpages></addata></record> |
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subjects | Adenylyl Cyclases - metabolism Animals Binding Binding, Competitive Cell Membrane GLP-1(7–36)-amide Glucagon - metabolism Glucagon-Like Peptide 1 Glucagon-Like Peptide-1 Receptor Glucagon-Like Peptides Insulin - metabolism Membranes Muscle, Skeletal - metabolism Peptide Fragments - metabolism Protein Precursors - metabolism Rat skeletal muscle Rats Rats, Wistar Receptor, Insulin - drug effects Receptor, Insulin - metabolism Receptors, Glucagon - isolation & purification Receptors, Glucagon - metabolism |
title | Glucagon-like peptide-1 binding to rat skeletal muscle |
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