Two distinct receptor subtypes for mammalian bombesin-like peptides
The mammalian bombesin-like peptides, gastrinreleasing peptide (GRP) and neuromedin B (NMB), are structurally related neuropeptides that elicit a wide spectrum of biological activities including regulation of smooth muscle contraction, stimulation of secretion, modulation of neural activity, and gro...
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Veröffentlicht in: | Trends in neurosciences (Regular ed.) 1991-12, Vol.14 (12), p.524-528 |
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description | The mammalian bombesin-like peptides, gastrinreleasing peptide (GRP) and neuromedin B (NMB), are structurally related neuropeptides that elicit a wide spectrum of biological activities including regulation of smooth muscle contraction, stimulation of secretion, modulation of neural activity, and growth regulation. Earlier studies have shown that GRP and NMB are expressed in different regions of both the CNS and peripheral organs. Recent ligand-binding and molecular-cloning studies have revealed two pharmacologically distinct G- protein-coupled receptor subtypes for mammalian bombesin-like peptides that have different relative affinities for GRP, NMB and bombesin receptor antagonists. Similar to the peptide ligands, the two receptor subtypes are expressed in a distinct but overlapping set of CNS regions, some of which have been identified in functional studies as sites where bombesin peptides elicit defined biological responses. Delineation of these peptide ligands and receptor subtypes will be important in future studies that explore the molecular basis for the heterogeneous nature of the responses to bombesin observed in mammalian systems. |
doi_str_mv | 10.1016/0166-2236(91)90005-F |
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Earlier studies have shown that GRP and NMB are expressed in different regions of both the CNS and peripheral organs. Recent ligand-binding and molecular-cloning studies have revealed two pharmacologically distinct G- protein-coupled receptor subtypes for mammalian bombesin-like peptides that have different relative affinities for GRP, NMB and bombesin receptor antagonists. Similar to the peptide ligands, the two receptor subtypes are expressed in a distinct but overlapping set of CNS regions, some of which have been identified in functional studies as sites where bombesin peptides elicit defined biological responses. Delineation of these peptide ligands and receptor subtypes will be important in future studies that explore the molecular basis for the heterogeneous nature of the responses to bombesin observed in mammalian systems.</description><identifier>ISSN: 0166-2236</identifier><identifier>EISSN: 1878-108X</identifier><identifier>DOI: 10.1016/0166-2236(91)90005-F</identifier><identifier>PMID: 1726343</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Bombesin - genetics ; Brain Chemistry ; Brain Mapping ; Cloning, Molecular ; DNA - genetics ; Gastrin-Releasing Peptide ; Mice ; Molecular Sequence Data ; Neurokinin B - analogs & derivatives ; Neurokinin B - genetics ; Neurokinin B - physiology ; Oligopeptides - genetics ; Peptides - genetics ; Peptides - physiology ; Protein Binding ; Pyrrolidonecarboxylic Acid - analogs & derivatives ; Rats ; Receptors, Bombesin ; Receptors, Neurotransmitter - classification ; Receptors, Neurotransmitter - drug effects ; Receptors, Neurotransmitter - genetics ; Receptors, Neurotransmitter - metabolism ; Sequence Homology, Nucleic Acid</subject><ispartof>Trends in neurosciences (Regular ed.), 1991-12, Vol.14 (12), p.524-528</ispartof><rights>1991</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c338t-25b439da763c9c31f7ce8a26738d94af6fba88e9de0d59f82cf8400caa6b88773</citedby><cites>FETCH-LOGICAL-c338t-25b439da763c9c31f7ce8a26738d94af6fba88e9de0d59f82cf8400caa6b88773</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/016622369190005F$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1726343$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Battey, James</creatorcontrib><creatorcontrib>Wada, Etsuko</creatorcontrib><title>Two distinct receptor subtypes for mammalian bombesin-like peptides</title><title>Trends in neurosciences (Regular ed.)</title><addtitle>Trends Neurosci</addtitle><description>The mammalian bombesin-like peptides, gastrinreleasing peptide (GRP) and neuromedin B (NMB), are structurally related neuropeptides that elicit a wide spectrum of biological activities including regulation of smooth muscle contraction, stimulation of secretion, modulation of neural activity, and growth regulation. Earlier studies have shown that GRP and NMB are expressed in different regions of both the CNS and peripheral organs. Recent ligand-binding and molecular-cloning studies have revealed two pharmacologically distinct G- protein-coupled receptor subtypes for mammalian bombesin-like peptides that have different relative affinities for GRP, NMB and bombesin receptor antagonists. Similar to the peptide ligands, the two receptor subtypes are expressed in a distinct but overlapping set of CNS regions, some of which have been identified in functional studies as sites where bombesin peptides elicit defined biological responses. Delineation of these peptide ligands and receptor subtypes will be important in future studies that explore the molecular basis for the heterogeneous nature of the responses to bombesin observed in mammalian systems.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Bombesin - genetics</subject><subject>Brain Chemistry</subject><subject>Brain Mapping</subject><subject>Cloning, Molecular</subject><subject>DNA - genetics</subject><subject>Gastrin-Releasing Peptide</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Neurokinin B - analogs & derivatives</subject><subject>Neurokinin B - genetics</subject><subject>Neurokinin B - physiology</subject><subject>Oligopeptides - genetics</subject><subject>Peptides - genetics</subject><subject>Peptides - physiology</subject><subject>Protein Binding</subject><subject>Pyrrolidonecarboxylic Acid - analogs & derivatives</subject><subject>Rats</subject><subject>Receptors, Bombesin</subject><subject>Receptors, Neurotransmitter - classification</subject><subject>Receptors, Neurotransmitter - drug effects</subject><subject>Receptors, Neurotransmitter - genetics</subject><subject>Receptors, Neurotransmitter - metabolism</subject><subject>Sequence Homology, Nucleic Acid</subject><issn>0166-2236</issn><issn>1878-108X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LAzEQhoMotVb_gcKeRA-r-Wo-LoIUq0LBSwVvIZvMQnS_3GyV_ntTV_TmYRiG931nmAehU4KvCCbiOpXIKWXiQpNLjTGe58s9NCVKqpxg9bKPpr-WQ3QU4yvGhCvCJ2hCJBWMsylarD_bzIc4hMYNWQ8OuqHts7gphm0HMSvTUNu6tlWwTVa0dQExNHkV3iDrkjd4iMfooLRVhJOfPkPPy7v14iFfPd0_Lm5XuWNMDTmdF5xpb6VgTjtGSulAWSokU15zW4qysEqB9oD9XJeKulJxjJ21olBKSjZD5-Perm_fNxAHU4fooKpsA-0mGkklJ1LQZOSj0fVtjD2UputDbfutIdjs2JkdGLMDYzQx3-zMMsXOfvZvihr8X2iElfSbUYf05EeA3kQXoHHgQwI3GN-G_w98Ae4pfpI</recordid><startdate>199112</startdate><enddate>199112</enddate><creator>Battey, James</creator><creator>Wada, Etsuko</creator><general>Elsevier Ltd</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>199112</creationdate><title>Two distinct receptor subtypes for mammalian bombesin-like peptides</title><author>Battey, James ; Wada, Etsuko</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c338t-25b439da763c9c31f7ce8a26738d94af6fba88e9de0d59f82cf8400caa6b88773</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Bombesin - genetics</topic><topic>Brain Chemistry</topic><topic>Brain Mapping</topic><topic>Cloning, Molecular</topic><topic>DNA - genetics</topic><topic>Gastrin-Releasing Peptide</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Neurokinin B - analogs & derivatives</topic><topic>Neurokinin B - genetics</topic><topic>Neurokinin B - physiology</topic><topic>Oligopeptides - genetics</topic><topic>Peptides - genetics</topic><topic>Peptides - physiology</topic><topic>Protein Binding</topic><topic>Pyrrolidonecarboxylic Acid - analogs & derivatives</topic><topic>Rats</topic><topic>Receptors, Bombesin</topic><topic>Receptors, Neurotransmitter - classification</topic><topic>Receptors, Neurotransmitter - drug effects</topic><topic>Receptors, Neurotransmitter - genetics</topic><topic>Receptors, Neurotransmitter - metabolism</topic><topic>Sequence Homology, Nucleic Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Battey, James</creatorcontrib><creatorcontrib>Wada, Etsuko</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>Trends in neurosciences (Regular ed.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Battey, James</au><au>Wada, Etsuko</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Two distinct receptor subtypes for mammalian bombesin-like peptides</atitle><jtitle>Trends in neurosciences (Regular ed.)</jtitle><addtitle>Trends Neurosci</addtitle><date>1991-12</date><risdate>1991</risdate><volume>14</volume><issue>12</issue><spage>524</spage><epage>528</epage><pages>524-528</pages><issn>0166-2236</issn><eissn>1878-108X</eissn><abstract>The mammalian bombesin-like peptides, gastrinreleasing peptide (GRP) and neuromedin B (NMB), are structurally related neuropeptides that elicit a wide spectrum of biological activities including regulation of smooth muscle contraction, stimulation of secretion, modulation of neural activity, and growth regulation. Earlier studies have shown that GRP and NMB are expressed in different regions of both the CNS and peripheral organs. Recent ligand-binding and molecular-cloning studies have revealed two pharmacologically distinct G- protein-coupled receptor subtypes for mammalian bombesin-like peptides that have different relative affinities for GRP, NMB and bombesin receptor antagonists. Similar to the peptide ligands, the two receptor subtypes are expressed in a distinct but overlapping set of CNS regions, some of which have been identified in functional studies as sites where bombesin peptides elicit defined biological responses. Delineation of these peptide ligands and receptor subtypes will be important in future studies that explore the molecular basis for the heterogeneous nature of the responses to bombesin observed in mammalian systems.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>1726343</pmid><doi>10.1016/0166-2236(91)90005-F</doi><tpages>5</tpages></addata></record> |
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subjects | Amino Acid Sequence Animals Bombesin - genetics Brain Chemistry Brain Mapping Cloning, Molecular DNA - genetics Gastrin-Releasing Peptide Mice Molecular Sequence Data Neurokinin B - analogs & derivatives Neurokinin B - genetics Neurokinin B - physiology Oligopeptides - genetics Peptides - genetics Peptides - physiology Protein Binding Pyrrolidonecarboxylic Acid - analogs & derivatives Rats Receptors, Bombesin Receptors, Neurotransmitter - classification Receptors, Neurotransmitter - drug effects Receptors, Neurotransmitter - genetics Receptors, Neurotransmitter - metabolism Sequence Homology, Nucleic Acid |
title | Two distinct receptor subtypes for mammalian bombesin-like peptides |
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