Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity
Guanosine 5'-triphosphate (GTP) was found to inhibit guinea pig liver transglutaminase activity as measured by [3H]putrescine incorporation into casein. GDP and GTP-gamma-S also inhibited enzyme activity (GTP-gamma-S greater than GTP greater than GDP). Kinetic studies showed that GTP acted as a...
Gespeichert in:
Veröffentlicht in: | The Journal of biological chemistry 1987-02, Vol.262 (4), p.1901-1906 |
---|---|
Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 1906 |
---|---|
container_issue | 4 |
container_start_page | 1901 |
container_title | The Journal of biological chemistry |
container_volume | 262 |
creator | Achyuthan, K E Greenberg, C S |
description | Guanosine 5'-triphosphate (GTP) was found to inhibit guinea pig liver transglutaminase activity as measured by [3H]putrescine incorporation into casein. GDP and GTP-gamma-S also inhibited enzyme activity (GTP-gamma-S greater than GTP greater than GDP). Kinetic studies showed that GTP acted as a reversible, noncompetitive inhibitor and that CaCl2 partially reversed GTP inhibition. GTP also inhibited rat liver and adult bovine aortic endothelial cell transglutaminase, but did not inhibit Factor XIIIa activity. Guanosine monophosphate (GMP), cyclic GMP, and polyguanylic acid did not inhibit enzyme activity. Guinea pig liver transglutaminase adsorbed well to GTP-agarose affinity columns, but not to CTP-agarose columns, and the binding was inhibited by the presence of calcium ions. Specific binding of GTP to transglutaminase was demonstrated by photoaffinity labeling with 8-azidoguanosine 5'-[gamma-32P] triphosphate, which was inhibited by the presence of GTP or CaCl2. GTP inhibited trypsin proteolysis of guinea pig liver transglutaminase without affecting the trypsin proteolysis of chromogenic substrates. Proteolytic protection was reversed by the addition of calcium. This study demonstrates that GTP binds to transglutaminase and that both GTP and calcium ions function in concert to regulate transglutaminase structure and function. |
doi_str_mv | 10.1016/S0021-9258(19)75724-X |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_77374175</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S002192581975724X</els_id><sourcerecordid>77374175</sourcerecordid><originalsourceid>FETCH-LOGICAL-c560t-c5f3da07366c25d148979de11722338d53d0284e5240be6164e59669a22d8f1b3</originalsourceid><addsrcrecordid>eNqFkdGK1DAUhoMo6-zoIywEEVkvuiZpm7ZXIouuCwuKrjB3IU1O2yNtMjbpyD6Gb2xmZ5jbzUUSON85_-H_Cbng7IozLj_8ZEzwrBFlfcmb91VZiSLbPCMrzuo8y0u-eU5WJ-QlOQ_hN0unaPgZORN11dRFsSL_bi24iB0aHdE76juqab9o5wM6oHHG7eDDdtARshadRdfTgBFoYvslIZpusacj7mBOtHahH5eoJ3Q6wBX94UfYz7y5_061s9To0eAy0SQVKDo6ebuMSTlN1SbiDuPDK_Ki02OA18d3TX59-Xx__TW7-3Zze_3pLjOlZDHdXW41q3IpjSgtL-qmaixwXgmR57Utc8tEXUApCtaC5DJ9GykbLYStO97ma_LuMHc7-z8LhKgmDAbGUTvwS1BVlVcFr8onQV7ImiU_E1geQDP7EGbo1HbGSc8PijO1z0w9Zqb2gSjeqMfM1Cb1XRwFlnYCe-o6hpTqb491HZKBXXLZYDhhdc5lk7ZdkzcHbMB--IszqBa9GWBSQgpVJEXGE_TxAEGydocwq2AQnAGbGkxU1uMT2_4HpWrAGg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>14680879</pqid></control><display><type>article</type><title>Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity</title><source>MEDLINE</source><source>Free E-Journal (出版社公開部分のみ)</source><source>Alma/SFX Local Collection</source><creator>Achyuthan, K E ; Greenberg, C S</creator><creatorcontrib>Achyuthan, K E ; Greenberg, C S</creatorcontrib><description>Guanosine 5'-triphosphate (GTP) was found to inhibit guinea pig liver transglutaminase activity as measured by [3H]putrescine incorporation into casein. GDP and GTP-gamma-S also inhibited enzyme activity (GTP-gamma-S greater than GTP greater than GDP). Kinetic studies showed that GTP acted as a reversible, noncompetitive inhibitor and that CaCl2 partially reversed GTP inhibition. GTP also inhibited rat liver and adult bovine aortic endothelial cell transglutaminase, but did not inhibit Factor XIIIa activity. Guanosine monophosphate (GMP), cyclic GMP, and polyguanylic acid did not inhibit enzyme activity. Guinea pig liver transglutaminase adsorbed well to GTP-agarose affinity columns, but not to CTP-agarose columns, and the binding was inhibited by the presence of calcium ions. Specific binding of GTP to transglutaminase was demonstrated by photoaffinity labeling with 8-azidoguanosine 5'-[gamma-32P] triphosphate, which was inhibited by the presence of GTP or CaCl2. GTP inhibited trypsin proteolysis of guinea pig liver transglutaminase without affecting the trypsin proteolysis of chromogenic substrates. Proteolytic protection was reversed by the addition of calcium. This study demonstrates that GTP binds to transglutaminase and that both GTP and calcium ions function in concert to regulate transglutaminase structure and function.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)75724-X</identifier><identifier>PMID: 2879844</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Affinity Labels - metabolism ; Analytical, structural and metabolic biochemistry ; Animals ; Azides - metabolism ; Biological and medical sciences ; Calcium - metabolism ; Calcium Chloride - pharmacology ; Chromatography, Affinity ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; GTP ; Guanosine Triphosphate - analogs & derivatives ; Guanosine Triphosphate - metabolism ; Guinea Pigs ; liver ; Liver - enzymology ; Magnesium - metabolism ; Transferases ; transglutaminase ; Transglutaminases - metabolism ; Trypsin - metabolism</subject><ispartof>The Journal of biological chemistry, 1987-02, Vol.262 (4), p.1901-1906</ispartof><rights>1987 © 1987 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c560t-c5f3da07366c25d148979de11722338d53d0284e5240be6164e59669a22d8f1b3</citedby><cites>FETCH-LOGICAL-c560t-c5f3da07366c25d148979de11722338d53d0284e5240be6164e59669a22d8f1b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8316977$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2879844$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Achyuthan, K E</creatorcontrib><creatorcontrib>Greenberg, C S</creatorcontrib><title>Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Guanosine 5'-triphosphate (GTP) was found to inhibit guinea pig liver transglutaminase activity as measured by [3H]putrescine incorporation into casein. GDP and GTP-gamma-S also inhibited enzyme activity (GTP-gamma-S greater than GTP greater than GDP). Kinetic studies showed that GTP acted as a reversible, noncompetitive inhibitor and that CaCl2 partially reversed GTP inhibition. GTP also inhibited rat liver and adult bovine aortic endothelial cell transglutaminase, but did not inhibit Factor XIIIa activity. Guanosine monophosphate (GMP), cyclic GMP, and polyguanylic acid did not inhibit enzyme activity. Guinea pig liver transglutaminase adsorbed well to GTP-agarose affinity columns, but not to CTP-agarose columns, and the binding was inhibited by the presence of calcium ions. Specific binding of GTP to transglutaminase was demonstrated by photoaffinity labeling with 8-azidoguanosine 5'-[gamma-32P] triphosphate, which was inhibited by the presence of GTP or CaCl2. GTP inhibited trypsin proteolysis of guinea pig liver transglutaminase without affecting the trypsin proteolysis of chromogenic substrates. Proteolytic protection was reversed by the addition of calcium. This study demonstrates that GTP binds to transglutaminase and that both GTP and calcium ions function in concert to regulate transglutaminase structure and function.</description><subject>Affinity Labels - metabolism</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Azides - metabolism</subject><subject>Biological and medical sciences</subject><subject>Calcium - metabolism</subject><subject>Calcium Chloride - pharmacology</subject><subject>Chromatography, Affinity</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GTP</subject><subject>Guanosine Triphosphate - analogs & derivatives</subject><subject>Guanosine Triphosphate - metabolism</subject><subject>Guinea Pigs</subject><subject>liver</subject><subject>Liver - enzymology</subject><subject>Magnesium - metabolism</subject><subject>Transferases</subject><subject>transglutaminase</subject><subject>Transglutaminases - metabolism</subject><subject>Trypsin - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkdGK1DAUhoMo6-zoIywEEVkvuiZpm7ZXIouuCwuKrjB3IU1O2yNtMjbpyD6Gb2xmZ5jbzUUSON85_-H_Cbng7IozLj_8ZEzwrBFlfcmb91VZiSLbPCMrzuo8y0u-eU5WJ-QlOQ_hN0unaPgZORN11dRFsSL_bi24iB0aHdE76juqab9o5wM6oHHG7eDDdtARshadRdfTgBFoYvslIZpusacj7mBOtHahH5eoJ3Q6wBX94UfYz7y5_061s9To0eAy0SQVKDo6ebuMSTlN1SbiDuPDK_Ki02OA18d3TX59-Xx__TW7-3Zze_3pLjOlZDHdXW41q3IpjSgtL-qmaixwXgmR57Utc8tEXUApCtaC5DJ9GykbLYStO97ma_LuMHc7-z8LhKgmDAbGUTvwS1BVlVcFr8onQV7ImiU_E1geQDP7EGbo1HbGSc8PijO1z0w9Zqb2gSjeqMfM1Cb1XRwFlnYCe-o6hpTqb491HZKBXXLZYDhhdc5lk7ZdkzcHbMB--IszqBa9GWBSQgpVJEXGE_TxAEGydocwq2AQnAGbGkxU1uMT2_4HpWrAGg</recordid><startdate>19870205</startdate><enddate>19870205</enddate><creator>Achyuthan, K E</creator><creator>Greenberg, C S</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19870205</creationdate><title>Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity</title><author>Achyuthan, K E ; Greenberg, C S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c560t-c5f3da07366c25d148979de11722338d53d0284e5240be6164e59669a22d8f1b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Affinity Labels - metabolism</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Azides - metabolism</topic><topic>Biological and medical sciences</topic><topic>Calcium - metabolism</topic><topic>Calcium Chloride - pharmacology</topic><topic>Chromatography, Affinity</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GTP</topic><topic>Guanosine Triphosphate - analogs & derivatives</topic><topic>Guanosine Triphosphate - metabolism</topic><topic>Guinea Pigs</topic><topic>liver</topic><topic>Liver - enzymology</topic><topic>Magnesium - metabolism</topic><topic>Transferases</topic><topic>transglutaminase</topic><topic>Transglutaminases - metabolism</topic><topic>Trypsin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Achyuthan, K E</creatorcontrib><creatorcontrib>Greenberg, C S</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Achyuthan, K E</au><au>Greenberg, C S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1987-02-05</date><risdate>1987</risdate><volume>262</volume><issue>4</issue><spage>1901</spage><epage>1906</epage><pages>1901-1906</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Guanosine 5'-triphosphate (GTP) was found to inhibit guinea pig liver transglutaminase activity as measured by [3H]putrescine incorporation into casein. GDP and GTP-gamma-S also inhibited enzyme activity (GTP-gamma-S greater than GTP greater than GDP). Kinetic studies showed that GTP acted as a reversible, noncompetitive inhibitor and that CaCl2 partially reversed GTP inhibition. GTP also inhibited rat liver and adult bovine aortic endothelial cell transglutaminase, but did not inhibit Factor XIIIa activity. Guanosine monophosphate (GMP), cyclic GMP, and polyguanylic acid did not inhibit enzyme activity. Guinea pig liver transglutaminase adsorbed well to GTP-agarose affinity columns, but not to CTP-agarose columns, and the binding was inhibited by the presence of calcium ions. Specific binding of GTP to transglutaminase was demonstrated by photoaffinity labeling with 8-azidoguanosine 5'-[gamma-32P] triphosphate, which was inhibited by the presence of GTP or CaCl2. GTP inhibited trypsin proteolysis of guinea pig liver transglutaminase without affecting the trypsin proteolysis of chromogenic substrates. Proteolytic protection was reversed by the addition of calcium. This study demonstrates that GTP binds to transglutaminase and that both GTP and calcium ions function in concert to regulate transglutaminase structure and function.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>2879844</pmid><doi>10.1016/S0021-9258(19)75724-X</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0021-9258 |
ispartof | The Journal of biological chemistry, 1987-02, Vol.262 (4), p.1901-1906 |
issn | 0021-9258 1083-351X |
language | eng |
recordid | cdi_proquest_miscellaneous_77374175 |
source | MEDLINE; Free E-Journal (出版社公開部分のみ); Alma/SFX Local Collection |
subjects | Affinity Labels - metabolism Analytical, structural and metabolic biochemistry Animals Azides - metabolism Biological and medical sciences Calcium - metabolism Calcium Chloride - pharmacology Chromatography, Affinity Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology GTP Guanosine Triphosphate - analogs & derivatives Guanosine Triphosphate - metabolism Guinea Pigs liver Liver - enzymology Magnesium - metabolism Transferases transglutaminase Transglutaminases - metabolism Trypsin - metabolism |
title | Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-25T10%3A41%3A57IST&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=Identification%20of%20a%20guanosine%20triphosphate-binding%20site%20on%20guinea%20pig%20liver%20transglutaminase.%20Role%20of%20GTP%20and%20calcium%20ions%20in%20modulating%20activity&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Achyuthan,%20K%20E&rft.date=1987-02-05&rft.volume=262&rft.issue=4&rft.spage=1901&rft.epage=1906&rft.pages=1901-1906&rft.issn=0021-9258&rft.eissn=1083-351X&rft.coden=JBCHA3&rft_id=info:doi/10.1016/S0021-9258(19)75724-X&rft_dat=%3Cproquest_cross%3E77374175%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=14680879&rft_id=info:pmid/2879844&rft_els_id=S002192581975724X&rfr_iscdi=true |