Nitrosothiol Reactivity Profiling Identifies S-Nitrosylated Proteins with Unexpected Stability
Nitric oxide (NO) regulates protein function by S-nitrosylation of cysteine to form nitrosothiols. Nitrosothiols are highly susceptible to nonenzymatic degradation by cytosolic reducing agents. Here we show that although most protein nitrosothiols are rapidly degraded by cytosolic reductants, a smal...
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| Veröffentlicht in: | Chemistry & biology 2008-12, Vol.15 (12), p.1307-1316 |
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| creator | Paige, Jeremy S. Xu, Guoqiang Stancevic, Branka Jaffrey, Samie R. |
| description | Nitric oxide (NO) regulates protein function by
S-nitrosylation of cysteine to form nitrosothiols. Nitrosothiols are highly susceptible to nonenzymatic degradation by cytosolic reducing agents. Here we show that although most protein nitrosothiols are rapidly degraded by cytosolic reductants, a small subset form unusually stable
S-nitrosylated proteins. Our findings suggest that stable
S-nitrosylation reflects a protein conformation change that shields the nitrosothiol. To identify stable protein nitrosothiols, we developed a proteomic method for profiling
S-nitrosylation. We examined the stability of over 100
S-nitrosylated proteins, and identified 10 stable nitrosothiols. These proteins remained
S-nitrosylated in cells after NO synthesis was inhibited, unlike most
S-nitrosylated proteins. Taken together, our data identify a class of NO targets that form stable nitrosothiols in the cell and are likely to mediate the persistent cellular effects of NO. |
| doi_str_mv | 10.1016/j.chembiol.2008.10.013 |
| format | Article |
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S-nitrosylation of cysteine to form nitrosothiols. Nitrosothiols are highly susceptible to nonenzymatic degradation by cytosolic reducing agents. Here we show that although most protein nitrosothiols are rapidly degraded by cytosolic reductants, a small subset form unusually stable
S-nitrosylated proteins. Our findings suggest that stable
S-nitrosylation reflects a protein conformation change that shields the nitrosothiol. To identify stable protein nitrosothiols, we developed a proteomic method for profiling
S-nitrosylation. We examined the stability of over 100
S-nitrosylated proteins, and identified 10 stable nitrosothiols. These proteins remained
S-nitrosylated in cells after NO synthesis was inhibited, unlike most
S-nitrosylated proteins. Taken together, our data identify a class of NO targets that form stable nitrosothiols in the cell and are likely to mediate the persistent cellular effects of NO.</description><identifier>ISSN: 1074-5521</identifier><identifier>EISSN: 1879-1301</identifier><identifier>DOI: 10.1016/j.chembiol.2008.10.013</identifier><identifier>PMID: 19101475</identifier><language>eng</language><publisher>United States: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Brain - cytology ; CHEMBIO ; Chromatography, Liquid ; Crystallization ; Drug Stability ; Gas Chromatography-Mass Spectrometry ; Glutathione - chemistry ; Glutathione - metabolism ; Humans ; Mice ; Molecular Sequence Data ; Molecular Structure ; Nitric Oxide - chemistry ; Nitric Oxide - metabolism ; Oxidation-Reduction ; Peptides - analysis ; Peptides - chemistry ; Protein Array Analysis ; Proteomics ; Rats ; S-Nitrosothiols - analysis ; S-Nitrosothiols - chemistry ; S-Nitrosothiols - metabolism ; Signal Transduction ; SIGNALING</subject><ispartof>Chemistry & biology, 2008-12, Vol.15 (12), p.1307-1316</ispartof><rights>2008 Elsevier Ltd</rights><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c469t-59f3e5e9edf43b8d53f4609fc27904df22f1023725d3c1c959ff1878abbc5f433</citedby><cites>FETCH-LOGICAL-c469t-59f3e5e9edf43b8d53f4609fc27904df22f1023725d3c1c959ff1878abbc5f433</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.chembiol.2008.10.013$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19101475$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Paige, Jeremy S.</creatorcontrib><creatorcontrib>Xu, Guoqiang</creatorcontrib><creatorcontrib>Stancevic, Branka</creatorcontrib><creatorcontrib>Jaffrey, Samie R.</creatorcontrib><title>Nitrosothiol Reactivity Profiling Identifies S-Nitrosylated Proteins with Unexpected Stability</title><title>Chemistry & biology</title><addtitle>Chem Biol</addtitle><description>Nitric oxide (NO) regulates protein function by
S-nitrosylation of cysteine to form nitrosothiols. Nitrosothiols are highly susceptible to nonenzymatic degradation by cytosolic reducing agents. Here we show that although most protein nitrosothiols are rapidly degraded by cytosolic reductants, a small subset form unusually stable
S-nitrosylated proteins. Our findings suggest that stable
S-nitrosylation reflects a protein conformation change that shields the nitrosothiol. To identify stable protein nitrosothiols, we developed a proteomic method for profiling
S-nitrosylation. We examined the stability of over 100
S-nitrosylated proteins, and identified 10 stable nitrosothiols. These proteins remained
S-nitrosylated in cells after NO synthesis was inhibited, unlike most
S-nitrosylated proteins. Taken together, our data identify a class of NO targets that form stable nitrosothiols in the cell and are likely to mediate the persistent cellular effects of NO.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Brain - cytology</subject><subject>CHEMBIO</subject><subject>Chromatography, Liquid</subject><subject>Crystallization</subject><subject>Drug Stability</subject><subject>Gas Chromatography-Mass Spectrometry</subject><subject>Glutathione - chemistry</subject><subject>Glutathione - metabolism</subject><subject>Humans</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Molecular Structure</subject><subject>Nitric Oxide - chemistry</subject><subject>Nitric Oxide - metabolism</subject><subject>Oxidation-Reduction</subject><subject>Peptides - analysis</subject><subject>Peptides - chemistry</subject><subject>Protein Array Analysis</subject><subject>Proteomics</subject><subject>Rats</subject><subject>S-Nitrosothiols - analysis</subject><subject>S-Nitrosothiols - chemistry</subject><subject>S-Nitrosothiols - metabolism</subject><subject>Signal Transduction</subject><subject>SIGNALING</subject><issn>1074-5521</issn><issn>1879-1301</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkVtv1DAQhS1ERUvhL1R54i2LL4kTvyBQxaVSRRGlr1iOPe7OKhsvtnfb_fc42uX2xJMtz3fOjOcQcsHoglEmX68WdgnrAcO44JT25XFBmXhCzljfqZoJyp6WO-2aum05OyXPU1pRSlmv5DNyylQxabr2jHz_jDmGFPKyWFVfwdiMO8z76ksMHkec7qsrB1NGj5Cq2_qA70eTwc1MBpxS9YB5Wd1N8LgBOxdusxmKOO9fkBNvxgQvj-c5ufvw_tvlp_r65uPV5bvr2jZS5bpVXkALCpxvxNC7VvhGUuUt7xRtnOfcM8pFx1snLLOq8L58tDfDYNsiEefkzcF3sx3W4GyZOJpRbyKuTdzrYFD_W5lwqe_DTnPJeylkMXh1NIjhxxZS1mtMFsbRTBC2SUulaC-bpoDyANqyhxTB_27CqJ6j0Sv9Kxo9RzO_l2iK8OLvEf_IjlkU4O0BgLKoHULUySJMFhzGslbtAv6vx0-_NKbM</recordid><startdate>20081222</startdate><enddate>20081222</enddate><creator>Paige, Jeremy S.</creator><creator>Xu, Guoqiang</creator><creator>Stancevic, Branka</creator><creator>Jaffrey, Samie R.</creator><general>Elsevier Ltd</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20081222</creationdate><title>Nitrosothiol Reactivity Profiling Identifies S-Nitrosylated Proteins with Unexpected Stability</title><author>Paige, Jeremy S. ; Xu, Guoqiang ; Stancevic, Branka ; Jaffrey, Samie R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c469t-59f3e5e9edf43b8d53f4609fc27904df22f1023725d3c1c959ff1878abbc5f433</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Brain - cytology</topic><topic>CHEMBIO</topic><topic>Chromatography, Liquid</topic><topic>Crystallization</topic><topic>Drug Stability</topic><topic>Gas Chromatography-Mass Spectrometry</topic><topic>Glutathione - chemistry</topic><topic>Glutathione - metabolism</topic><topic>Humans</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Molecular Structure</topic><topic>Nitric Oxide - chemistry</topic><topic>Nitric Oxide - metabolism</topic><topic>Oxidation-Reduction</topic><topic>Peptides - analysis</topic><topic>Peptides - chemistry</topic><topic>Protein Array Analysis</topic><topic>Proteomics</topic><topic>Rats</topic><topic>S-Nitrosothiols - analysis</topic><topic>S-Nitrosothiols - chemistry</topic><topic>S-Nitrosothiols - metabolism</topic><topic>Signal Transduction</topic><topic>SIGNALING</topic><toplevel>online_resources</toplevel><creatorcontrib>Paige, Jeremy S.</creatorcontrib><creatorcontrib>Xu, Guoqiang</creatorcontrib><creatorcontrib>Stancevic, Branka</creatorcontrib><creatorcontrib>Jaffrey, Samie R.</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>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Chemistry & biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Paige, Jeremy S.</au><au>Xu, Guoqiang</au><au>Stancevic, Branka</au><au>Jaffrey, Samie R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nitrosothiol Reactivity Profiling Identifies S-Nitrosylated Proteins with Unexpected Stability</atitle><jtitle>Chemistry & biology</jtitle><addtitle>Chem Biol</addtitle><date>2008-12-22</date><risdate>2008</risdate><volume>15</volume><issue>12</issue><spage>1307</spage><epage>1316</epage><pages>1307-1316</pages><issn>1074-5521</issn><eissn>1879-1301</eissn><abstract>Nitric oxide (NO) regulates protein function by
S-nitrosylation of cysteine to form nitrosothiols. Nitrosothiols are highly susceptible to nonenzymatic degradation by cytosolic reducing agents. Here we show that although most protein nitrosothiols are rapidly degraded by cytosolic reductants, a small subset form unusually stable
S-nitrosylated proteins. Our findings suggest that stable
S-nitrosylation reflects a protein conformation change that shields the nitrosothiol. To identify stable protein nitrosothiols, we developed a proteomic method for profiling
S-nitrosylation. We examined the stability of over 100
S-nitrosylated proteins, and identified 10 stable nitrosothiols. These proteins remained
S-nitrosylated in cells after NO synthesis was inhibited, unlike most
S-nitrosylated proteins. Taken together, our data identify a class of NO targets that form stable nitrosothiols in the cell and are likely to mediate the persistent cellular effects of NO.</abstract><cop>United States</cop><pub>Elsevier Ltd</pub><pmid>19101475</pmid><doi>10.1016/j.chembiol.2008.10.013</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Cell Press Free Archives; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Animals Brain - cytology CHEMBIO Chromatography, Liquid Crystallization Drug Stability Gas Chromatography-Mass Spectrometry Glutathione - chemistry Glutathione - metabolism Humans Mice Molecular Sequence Data Molecular Structure Nitric Oxide - chemistry Nitric Oxide - metabolism Oxidation-Reduction Peptides - analysis Peptides - chemistry Protein Array Analysis Proteomics Rats S-Nitrosothiols - analysis S-Nitrosothiols - chemistry S-Nitrosothiols - metabolism Signal Transduction SIGNALING |
| title | Nitrosothiol Reactivity Profiling Identifies S-Nitrosylated Proteins with Unexpected Stability |
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