Differential redox potential between the human cytosolic and mitochondrial branched-chain aminotransferase
The human branched-chain isoenzymes are CXXC motif aminotransferase （hBCAT） redox sensitive homodimers central to glutamate metabolism in the central nervous system. These proteins respond differently to oxidation by H2O2, NO, and S-glutathionylation, suggesting that the redox potential is distinct...
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| Veröffentlicht in: | Acta biochimica et biophysica Sinica 2012-02, Vol.44 (2), p.172-176 |
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| creator | Coles, Steven J. Hancock, John T. Conway, Myra E. |
| description | The human branched-chain isoenzymes are CXXC motif aminotransferase （hBCAT） redox sensitive homodimers central to glutamate metabolism in the central nervous system. These proteins respond differently to oxidation by H2O2, NO, and S-glutathionylation, suggesting that the redox potential is distinct between isoenzymes. Using various reduced to oxidized glutathione ratios （GSH：GSSG） to alter the redox environment, we demon- strate that hBCATc （cytosolic） has an overall redox potential that is 30 mV lower than hBCATm （mitochondrial）. Furthermore, the CXXC motif of hBCATc was estimated to be 80 mV lower, suggesting that hBCATm is more oxidizing in nature. Western blot analysis revealed close correlations between hBCAT S-glutathionylation and the redox status of the assay environment, offering the hBCAT isoenzymes as novel biomarkers for cytosolic and mitochondrial oxidative stress. |
| doi_str_mv | 10.1093/abbs/gmr103 |
| format | Article |
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These proteins respond differently to oxidation by H2O2, NO, and S-glutathionylation, suggesting that the redox potential is distinct between isoenzymes. Using various reduced to oxidized glutathione ratios （GSH：GSSG） to alter the redox environment, we demon- strate that hBCATc （cytosolic） has an overall redox potential that is 30 mV lower than hBCATm （mitochondrial）. Furthermore, the CXXC motif of hBCATc was estimated to be 80 mV lower, suggesting that hBCATm is more oxidizing in nature. 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These proteins respond differently to oxidation by H2O2, NO, and S-glutathionylation, suggesting that the redox potential is distinct between isoenzymes. Using various reduced to oxidized glutathione ratios （GSH：GSSG） to alter the redox environment, we demon- strate that hBCATc （cytosolic） has an overall redox potential that is 30 mV lower than hBCATm （mitochondrial）. Furthermore, the CXXC motif of hBCATc was estimated to be 80 mV lower, suggesting that hBCATm is more oxidizing in nature. Western blot analysis revealed close correlations between hBCAT S-glutathionylation and the redox status of the assay environment, offering the hBCAT isoenzymes as novel biomarkers for cytosolic and mitochondrial oxidative stress.</description><subject>Amino Acid Motifs</subject><subject>Cytosol - enzymology</subject><subject>Glutathione - metabolism</subject><subject>Glutathione Disulfide - metabolism</subject><subject>Humans</subject><subject>In Vitro Techniques</subject><subject>Minor Histocompatibility Antigens</subject><subject>Mitochondria - enzymology</subject><subject>Oxidation-Reduction</subject><subject>Oxidative Stress</subject><subject>Pregnancy Proteins - chemistry</subject><subject>Pregnancy Proteins - genetics</subject><subject>Pregnancy Proteins - metabolism</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Transaminases - chemistry</subject><subject>Transaminases - genetics</subject><subject>Transaminases - metabolism</subject><subject>中枢神经系统</subject><subject>支链</subject><subject>氧化还原环境</subject><subject>氧化还原电位</subject><subject>电位差</subject><subject>线粒体</subject><subject>细胞内</subject><subject>转氨酶</subject><issn>1672-9145</issn><issn>1745-7270</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0UtLxDAUBeAgiu-Ve6kbFaSapGkeS_ENghtdlzS9nUbaZExS1H9vxxld6ioPPs6FexA6IPicYFVc6LqOF7MhEFysoW0iWJkLKvD6dOeC5oqwcgvtxPiKccE5wZtoi1KChZByG71e27aFAC5Z3WcBGv-RzX1avWtI7wAuSx1k3Thol5nP5KPvrcm0a7LBJm8675rwrYN2poMmN522LtODdT5Nf3EaoCPsoY1W9xH2V-cuerm9eb66zx-f7h6uLh9zUwiZck4bxWtaA22YplhJLiUrCWkZU1i2oFRNC2qENEYSJhpSlrzkICkQTECyYhedLHPnwb-NEFM12Gig77UDP8ZKESHLUnI1ydM_JZG0UIwztgg9W1ITfIwB2moe7KDDZ0VwtaihWtRQLWuY9OEqeKwHaH7tz94ncLwEfpz_k3S0mjutefZm3eyXM6y4VAIXX6dvnTQ</recordid><startdate>20120201</startdate><enddate>20120201</enddate><creator>Coles, Steven J.</creator><creator>Hancock, John T.</creator><creator>Conway, Myra E.</creator><general>Oxford University Press</general><scope>2RA</scope><scope>92L</scope><scope>CQIGP</scope><scope>W94</scope><scope>WU4</scope><scope>~WA</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>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20120201</creationdate><title>Differential redox potential between the human cytosolic and mitochondrial branched-chain aminotransferase</title><author>Coles, Steven J. ; Hancock, John T. ; Conway, Myra E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c378t-62d96b2be2d4a20986884511f44908fe99b232c78cc8147d155656e82e101e843</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Amino Acid Motifs</topic><topic>Cytosol - enzymology</topic><topic>Glutathione - metabolism</topic><topic>Glutathione Disulfide - metabolism</topic><topic>Humans</topic><topic>In Vitro Techniques</topic><topic>Minor Histocompatibility Antigens</topic><topic>Mitochondria - enzymology</topic><topic>Oxidation-Reduction</topic><topic>Oxidative Stress</topic><topic>Pregnancy Proteins - chemistry</topic><topic>Pregnancy Proteins - genetics</topic><topic>Pregnancy Proteins - metabolism</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Transaminases - chemistry</topic><topic>Transaminases - genetics</topic><topic>Transaminases - metabolism</topic><topic>中枢神经系统</topic><topic>支链</topic><topic>氧化还原环境</topic><topic>氧化还原电位</topic><topic>电位差</topic><topic>线粒体</topic><topic>细胞内</topic><topic>转氨酶</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Coles, Steven J.</creatorcontrib><creatorcontrib>Hancock, John T.</creatorcontrib><creatorcontrib>Conway, Myra E.</creatorcontrib><collection>中文科技期刊数据库</collection><collection>中文科技期刊数据库-CALIS站点</collection><collection>中文科技期刊数据库-7.0平台</collection><collection>中文科技期刊数据库-自然科学</collection><collection>中文科技期刊数据库-自然科学-生物科学</collection><collection>中文科技期刊数据库- 镜像站点</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Acta biochimica et biophysica Sinica</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Coles, Steven J.</au><au>Hancock, John T.</au><au>Conway, Myra E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Differential redox potential between the human cytosolic and mitochondrial branched-chain aminotransferase</atitle><jtitle>Acta biochimica et biophysica Sinica</jtitle><addtitle>Acta Biochimica et Biophysica Sinica</addtitle><date>2012-02-01</date><risdate>2012</risdate><volume>44</volume><issue>2</issue><spage>172</spage><epage>176</epage><pages>172-176</pages><issn>1672-9145</issn><eissn>1745-7270</eissn><abstract>The human branched-chain isoenzymes are CXXC motif aminotransferase （hBCAT） redox sensitive homodimers central to glutamate metabolism in the central nervous system. These proteins respond differently to oxidation by H2O2, NO, and S-glutathionylation, suggesting that the redox potential is distinct between isoenzymes. Using various reduced to oxidized glutathione ratios （GSH：GSSG） to alter the redox environment, we demon- strate that hBCATc （cytosolic） has an overall redox potential that is 30 mV lower than hBCATm （mitochondrial）. Furthermore, the CXXC motif of hBCATc was estimated to be 80 mV lower, suggesting that hBCATm is more oxidizing in nature. Western blot analysis revealed close correlations between hBCAT S-glutathionylation and the redox status of the assay environment, offering the hBCAT isoenzymes as novel biomarkers for cytosolic and mitochondrial oxidative stress.</abstract><cop>China</cop><pub>Oxford University Press</pub><pmid>22107788</pmid><doi>10.1093/abbs/gmr103</doi><tpages>5</tpages></addata></record> |
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| subjects | Amino Acid Motifs Cytosol - enzymology Glutathione - metabolism Glutathione Disulfide - metabolism Humans In Vitro Techniques Minor Histocompatibility Antigens Mitochondria - enzymology Oxidation-Reduction Oxidative Stress Pregnancy Proteins - chemistry Pregnancy Proteins - genetics Pregnancy Proteins - metabolism Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Transaminases - chemistry Transaminases - genetics Transaminases - metabolism 中枢神经系统 支链 氧化还原环境 氧化还原电位 电位差 线粒体 细胞内 转氨酶 |
| title | Differential redox potential between the human cytosolic and mitochondrial branched-chain aminotransferase |
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