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Inhibition of calmodulin-dependent myosin light-chain kinase by growth-hormone-releasing factor and vasoactive intestinal peptide
In view of the ability of calmodulin to bind vasoactive intestinal peptide (VIP) and growth-hormone-releasing factor (GRF) with high affinity [Stallwood, Brugger, Baggenstoss, Stemmer, Shiraga, Landers and Paul (1992) J. Biol. Chem. 267, 19617-19621], the effects of these neuropeptides on a model ca...
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Published in: | Biochemical journal 1994-06, Vol.300 (3), p.901-905 |
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creator | SHIRAGA, H STALLWOOD, D EBADI, M PFEIFFER, R LANDERS, D PAUL, S |
description | In view of the ability of calmodulin to bind vasoactive intestinal peptide (VIP) and growth-hormone-releasing factor (GRF) with high affinity [Stallwood, Brugger, Baggenstoss, Stemmer, Shiraga, Landers and Paul (1992) J. Biol. Chem. 267, 19617-19621], the effects of these neuropeptides on a model calmodulin-dependent enzyme, myosin light-chain kinase (MLCK), were studied. Both peptides were potent inhibitors of MLCK activity. The inhibition of enzyme activity by VIP and GRF was progressively overcome with increasing calmodulin concentrations, with no inhibition observed at a saturating calmodulin concentration. Nanomolar concentrations of MLCK blocked the formation of calmodulin-[125I-Tyr10]VIP complexes. These data provide support for a functional role of VIP and GRF binding by calmodulin. |
doi_str_mv | 10.1042/bj3000901 |
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Biol. Chem. 267, 19617-19621], the effects of these neuropeptides on a model calmodulin-dependent enzyme, myosin light-chain kinase (MLCK), were studied. Both peptides were potent inhibitors of MLCK activity. The inhibition of enzyme activity by VIP and GRF was progressively overcome with increasing calmodulin concentrations, with no inhibition observed at a saturating calmodulin concentration. Nanomolar concentrations of MLCK blocked the formation of calmodulin-[125I-Tyr10]VIP complexes. 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Biol. Chem. 267, 19617-19621], the effects of these neuropeptides on a model calmodulin-dependent enzyme, myosin light-chain kinase (MLCK), were studied. Both peptides were potent inhibitors of MLCK activity. The inhibition of enzyme activity by VIP and GRF was progressively overcome with increasing calmodulin concentrations, with no inhibition observed at a saturating calmodulin concentration. Nanomolar concentrations of MLCK blocked the formation of calmodulin-[125I-Tyr10]VIP complexes. These data provide support for a functional role of VIP and GRF binding by calmodulin.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Calmodulin - physiology</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Growth Hormone-Releasing Hormone - pharmacology</subject><subject>Molecular Sequence Data</subject><subject>Myosin-Light-Chain Kinase - antagonists & inhibitors</subject><subject>Oligopeptides - chemistry</subject><subject>Oligopeptides - metabolism</subject><subject>Rats</subject><subject>Signal Transduction</subject><subject>Transferases</subject><subject>Vasoactive Intestinal Peptide - pharmacology</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><recordid>eNpVkU9v1DAQxS0EKtvCgQ-A5ANC4pDWdpw4uSChCkqlSlzKOZrY441LYgfbu2iPfHNcdbWiB8t_3m-eZ_QIecfZJWdSXI0PNWOsZ_wF2XCpWNUp0b0kGyZaWbVM8NfkPKUHxrhkkp2Rs45x1qt2Q_7e-smNLrvgabBUw7wEs5udrwyu6A36TJdDSM7T2W2nXOkJyvmX85CQjge6jeFPnqopxCV4rCLOCIXeUgs6h0jBG7qHFMrN7ZE6nzHlUj3TFdfsDL4hryzMCd8e9wvy89vX--vv1d2Pm9vrL3eVrvs-VxYtl8CFkpa30jZjU6Oxo1HC6pGrWrdYG9D9KG0Lqmsb0AJUw43QrCmP9QX5_OS77sYFjS6TRZiHNboF4mEI4IbninfTsA37gfO6Ew0rBh-PBjH83pUphsUljfMMHsMuDaptZFmP4KcnUMeQUkR7-oSz4TGv4ZRXYd__39WJPAZU9A9HHVIJx0bw2qUTJktvXIn6HzKVok8</recordid><startdate>19940615</startdate><enddate>19940615</enddate><creator>SHIRAGA, H</creator><creator>STALLWOOD, D</creator><creator>EBADI, M</creator><creator>PFEIFFER, R</creator><creator>LANDERS, D</creator><creator>PAUL, S</creator><general>Portland Press</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>19940615</creationdate><title>Inhibition of calmodulin-dependent myosin light-chain kinase by growth-hormone-releasing factor and vasoactive intestinal peptide</title><author>SHIRAGA, H ; STALLWOOD, D ; EBADI, M ; PFEIFFER, R ; LANDERS, D ; PAUL, S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c399t-fef14a1274f164f5b53edfbd72fcb173c6e3dac9b4f6a7865ac2a751d2c05b4f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Calmodulin - physiology</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Growth Hormone-Releasing Hormone - pharmacology</topic><topic>Molecular Sequence Data</topic><topic>Myosin-Light-Chain Kinase - antagonists & inhibitors</topic><topic>Oligopeptides - chemistry</topic><topic>Oligopeptides - metabolism</topic><topic>Rats</topic><topic>Signal Transduction</topic><topic>Transferases</topic><topic>Vasoactive Intestinal Peptide - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SHIRAGA, H</creatorcontrib><creatorcontrib>STALLWOOD, D</creatorcontrib><creatorcontrib>EBADI, M</creatorcontrib><creatorcontrib>PFEIFFER, R</creatorcontrib><creatorcontrib>LANDERS, D</creatorcontrib><creatorcontrib>PAUL, S</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>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>SHIRAGA, H</au><au>STALLWOOD, D</au><au>EBADI, M</au><au>PFEIFFER, R</au><au>LANDERS, D</au><au>PAUL, S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Inhibition of calmodulin-dependent myosin light-chain kinase by growth-hormone-releasing factor and vasoactive intestinal peptide</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1994-06-15</date><risdate>1994</risdate><volume>300</volume><issue>3</issue><spage>901</spage><epage>905</epage><pages>901-905</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>In view of the ability of calmodulin to bind vasoactive intestinal peptide (VIP) and growth-hormone-releasing factor (GRF) with high affinity [Stallwood, Brugger, Baggenstoss, Stemmer, Shiraga, Landers and Paul (1992) J. Biol. Chem. 267, 19617-19621], the effects of these neuropeptides on a model calmodulin-dependent enzyme, myosin light-chain kinase (MLCK), were studied. Both peptides were potent inhibitors of MLCK activity. The inhibition of enzyme activity by VIP and GRF was progressively overcome with increasing calmodulin concentrations, with no inhibition observed at a saturating calmodulin concentration. Nanomolar concentrations of MLCK blocked the formation of calmodulin-[125I-Tyr10]VIP complexes. These data provide support for a functional role of VIP and GRF binding by calmodulin.</abstract><cop>Colchester</cop><pub>Portland Press</pub><pmid>8010976</pmid><doi>10.1042/bj3000901</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Calmodulin - physiology Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Growth Hormone-Releasing Hormone - pharmacology Molecular Sequence Data Myosin-Light-Chain Kinase - antagonists & inhibitors Oligopeptides - chemistry Oligopeptides - metabolism Rats Signal Transduction Transferases Vasoactive Intestinal Peptide - pharmacology |
title | Inhibition of calmodulin-dependent myosin light-chain kinase by growth-hormone-releasing factor and vasoactive intestinal peptide |
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