N-Myristoyltransferase 2 expression in human colon cancer: Cross-talk between the calpain and caspase system
A number of viral and eukaryotic proteins which undergo a lipophilic modification by the enzyme N-myristoyltransferase (NMT: NMT1 and NMT2) are required for signal transduction and regulatory functions. To investigate whether NMT2 contributes to the pathogenesis of colorectal carcinoma, we observed...
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| Veröffentlicht in: | FEBS letters 2006-04, Vol.580 (8), p.2021-2026 |
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| creator | Selvakumar, Ponniah Smith-Windsor, Erin Bonham, Keith Sharma, Rajendra K. |
| description | A number of viral and eukaryotic proteins which undergo a lipophilic modification by the enzyme
N-myristoyltransferase (NMT: NMT1 and NMT2) are required for signal transduction and regulatory functions. To investigate whether NMT2 contributes to the pathogenesis of colorectal carcinoma, we observed a higher expression of NMT2 in most of the cases of cancerous tissues compared to normal tissues (84.6% of cases;
P
<
0.05) by Western blot analysis. Furthermore, protein–protein interaction of NMTs revealed that
m-calpain interacts with NMT1 while caspase-3 interacts with NMT2. Our findings provide the first evidence of higher expression of NMT2 in human colorectal adenocarcinomas and the interaction of both forms of NMT with various signaling molecules. |
| doi_str_mv | 10.1016/j.febslet.2006.02.076 |
| format | Article |
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N-myristoyltransferase (NMT: NMT1 and NMT2) are required for signal transduction and regulatory functions. To investigate whether NMT2 contributes to the pathogenesis of colorectal carcinoma, we observed a higher expression of NMT2 in most of the cases of cancerous tissues compared to normal tissues (84.6% of cases;
P
<
0.05) by Western blot analysis. Furthermore, protein–protein interaction of NMTs revealed that
m-calpain interacts with NMT1 while caspase-3 interacts with NMT2. Our findings provide the first evidence of higher expression of NMT2 in human colorectal adenocarcinomas and the interaction of both forms of NMT with various signaling molecules.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2006.02.076</identifier><identifier>PMID: 16530191</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Acyltransferases - metabolism ; Bcl2 ; Calpain - metabolism ; Caspase-3 ; Caspases - metabolism ; Colonic Neoplasms - enzymology ; Colonic Neoplasms - metabolism ; Gene Expression Regulation, Neoplastic ; HCCL ; human colon cancer cell lines ; Humans ; Lipid modification ; m-Calpain ; MetAP ; methionine aminopeptidase ; myristoyltransferase 1 ; myristoyltransferase 2 ; N-myristoyltransferase 2 ; NIP71 ; NMT inhibitor protein 71 ; NMT1 ; NMT2 ; p53 ; Peptide Hydrolases - metabolism ; PEST ; proline (P), glutamate (E), serine (S), and threonine (T) residues ; Protein Binding ; Proto-Oncogene Proteins c-bcl-2 - metabolism ; SDS–PAGE ; sodium dodecyl sulfate–polyacrylamide gel electrophoresis ; Tumor Cells, Cultured ; Tumor Suppressor Protein p53 - metabolism</subject><ispartof>FEBS letters, 2006-04, Vol.580 (8), p.2021-2026</ispartof><rights>2006 Federation of European Biochemical Societies</rights><rights>FEBS Letters 580 (2006) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4594-c856da504ea4ab747dbec655cce44bb0fbf962e83b4c1ee1e5a5b4e4e76bebbf3</citedby><cites>FETCH-LOGICAL-c4594-c856da504ea4ab747dbec655cce44bb0fbf962e83b4c1ee1e5a5b4e4e76bebbf3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2006.02.076$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.febslet.2006.02.076$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1417,1433,3550,27924,27925,45574,45575,45995,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16530191$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Selvakumar, Ponniah</creatorcontrib><creatorcontrib>Smith-Windsor, Erin</creatorcontrib><creatorcontrib>Bonham, Keith</creatorcontrib><creatorcontrib>Sharma, Rajendra K.</creatorcontrib><title>N-Myristoyltransferase 2 expression in human colon cancer: Cross-talk between the calpain and caspase system</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>A number of viral and eukaryotic proteins which undergo a lipophilic modification by the enzyme
N-myristoyltransferase (NMT: NMT1 and NMT2) are required for signal transduction and regulatory functions. To investigate whether NMT2 contributes to the pathogenesis of colorectal carcinoma, we observed a higher expression of NMT2 in most of the cases of cancerous tissues compared to normal tissues (84.6% of cases;
P
<
0.05) by Western blot analysis. Furthermore, protein–protein interaction of NMTs revealed that
m-calpain interacts with NMT1 while caspase-3 interacts with NMT2. Our findings provide the first evidence of higher expression of NMT2 in human colorectal adenocarcinomas and the interaction of both forms of NMT with various signaling molecules.</description><subject>Acyltransferases - metabolism</subject><subject>Bcl2</subject><subject>Calpain - metabolism</subject><subject>Caspase-3</subject><subject>Caspases - metabolism</subject><subject>Colonic Neoplasms - enzymology</subject><subject>Colonic Neoplasms - metabolism</subject><subject>Gene Expression Regulation, Neoplastic</subject><subject>HCCL</subject><subject>human colon cancer cell lines</subject><subject>Humans</subject><subject>Lipid modification</subject><subject>m-Calpain</subject><subject>MetAP</subject><subject>methionine aminopeptidase</subject><subject>myristoyltransferase 1</subject><subject>myristoyltransferase 2</subject><subject>N-myristoyltransferase 2</subject><subject>NIP71</subject><subject>NMT inhibitor protein 71</subject><subject>NMT1</subject><subject>NMT2</subject><subject>p53</subject><subject>Peptide Hydrolases - metabolism</subject><subject>PEST</subject><subject>proline (P), glutamate (E), serine (S), and threonine (T) residues</subject><subject>Protein Binding</subject><subject>Proto-Oncogene Proteins c-bcl-2 - metabolism</subject><subject>SDS–PAGE</subject><subject>sodium dodecyl sulfate–polyacrylamide gel electrophoresis</subject><subject>Tumor Cells, Cultured</subject><subject>Tumor Suppressor Protein p53 - metabolism</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU9v1DAQxS0EokvhI4By4pZgJ7YTc0GwailSgQNwtmxnonpx_uDxUvLtcbQrcSwne-T33njmR8hLRitGmXxzqAawGCBVNaWyonVFW_mI7FjXNmXDZfeY7ChlvBStai7IM8QDzXXH1FNywaRoKFNsR8KX8vMaPaZ5DSmaCQeIBqGoC_izRED081T4qbg7jmYq3Bxy6czkIL4t9nFGLJMJPwsL6R5gKtId5OewmGwxU5_vuGxxuGKC8Tl5MpiA8OJ8XpIf11ff9zfl7dePn_bvb0vHheKl64TsjaAcDDe25W1vwUkhnAPOraWDHZSsoWssdwyAgTDCcuDQSgvWDs0leX3KXeL86wiY9OjRQQhmgvmIWratUpyzB4VMdV1HZZOF4iR028wRBr1EP5q4akb1xkMf9JmH3nhoWuvMI_tenRsc7Qj9P9cZQBbcnAT3PsD6f6n6-upD_W2Du7GlktK6UzxHvTtFQV7tbw9Ro_OQUfU-gku6n_0Dv_0LmV22-g</recordid><startdate>20060403</startdate><enddate>20060403</enddate><creator>Selvakumar, Ponniah</creator><creator>Smith-Windsor, Erin</creator><creator>Bonham, Keith</creator><creator>Sharma, Rajendra K.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20060403</creationdate><title>N-Myristoyltransferase 2 expression in human colon cancer: Cross-talk between the calpain and caspase system</title><author>Selvakumar, Ponniah ; Smith-Windsor, Erin ; Bonham, Keith ; Sharma, Rajendra K.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4594-c856da504ea4ab747dbec655cce44bb0fbf962e83b4c1ee1e5a5b4e4e76bebbf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Acyltransferases - metabolism</topic><topic>Bcl2</topic><topic>Calpain - metabolism</topic><topic>Caspase-3</topic><topic>Caspases - metabolism</topic><topic>Colonic Neoplasms - enzymology</topic><topic>Colonic Neoplasms - metabolism</topic><topic>Gene Expression Regulation, Neoplastic</topic><topic>HCCL</topic><topic>human colon cancer cell lines</topic><topic>Humans</topic><topic>Lipid modification</topic><topic>m-Calpain</topic><topic>MetAP</topic><topic>methionine aminopeptidase</topic><topic>myristoyltransferase 1</topic><topic>myristoyltransferase 2</topic><topic>N-myristoyltransferase 2</topic><topic>NIP71</topic><topic>NMT inhibitor protein 71</topic><topic>NMT1</topic><topic>NMT2</topic><topic>p53</topic><topic>Peptide Hydrolases - metabolism</topic><topic>PEST</topic><topic>proline (P), glutamate (E), serine (S), and threonine (T) residues</topic><topic>Protein Binding</topic><topic>Proto-Oncogene Proteins c-bcl-2 - metabolism</topic><topic>SDS–PAGE</topic><topic>sodium dodecyl sulfate–polyacrylamide gel electrophoresis</topic><topic>Tumor Cells, Cultured</topic><topic>Tumor Suppressor Protein p53 - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Selvakumar, Ponniah</creatorcontrib><creatorcontrib>Smith-Windsor, Erin</creatorcontrib><creatorcontrib>Bonham, Keith</creatorcontrib><creatorcontrib>Sharma, Rajendra K.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Selvakumar, Ponniah</au><au>Smith-Windsor, Erin</au><au>Bonham, Keith</au><au>Sharma, Rajendra K.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>N-Myristoyltransferase 2 expression in human colon cancer: Cross-talk between the calpain and caspase system</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2006-04-03</date><risdate>2006</risdate><volume>580</volume><issue>8</issue><spage>2021</spage><epage>2026</epage><pages>2021-2026</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>A number of viral and eukaryotic proteins which undergo a lipophilic modification by the enzyme
N-myristoyltransferase (NMT: NMT1 and NMT2) are required for signal transduction and regulatory functions. To investigate whether NMT2 contributes to the pathogenesis of colorectal carcinoma, we observed a higher expression of NMT2 in most of the cases of cancerous tissues compared to normal tissues (84.6% of cases;
P
<
0.05) by Western blot analysis. Furthermore, protein–protein interaction of NMTs revealed that
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| source | Wiley-Blackwell Journals; Wiley-Blackwell Free Backfiles(OpenAccess); MEDLINE; Elsevier ScienceDirect Journals Complete; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Acyltransferases - metabolism Bcl2 Calpain - metabolism Caspase-3 Caspases - metabolism Colonic Neoplasms - enzymology Colonic Neoplasms - metabolism Gene Expression Regulation, Neoplastic HCCL human colon cancer cell lines Humans Lipid modification m-Calpain MetAP methionine aminopeptidase myristoyltransferase 1 myristoyltransferase 2 N-myristoyltransferase 2 NIP71 NMT inhibitor protein 71 NMT1 NMT2 p53 Peptide Hydrolases - metabolism PEST proline (P), glutamate (E), serine (S), and threonine (T) residues Protein Binding Proto-Oncogene Proteins c-bcl-2 - metabolism SDS–PAGE sodium dodecyl sulfate–polyacrylamide gel electrophoresis Tumor Cells, Cultured Tumor Suppressor Protein p53 - metabolism |
| title | N-Myristoyltransferase 2 expression in human colon cancer: Cross-talk between the calpain and caspase system |
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