Structure, function and disease relevance of Omega-class glutathione transferases
The Omega-class cytosolic glutathione transferases (GSTs) have distinct structural and functional attributes that allow them to perform novel roles unrelated to the functions of other GSTs. Mammalian GSTO1-1 has been found to play a previously unappreciated role in the glutathionylation cycle that i...
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| Veröffentlicht in: | Archives of toxicology 2016-05, Vol.90 (5), p.1049-1067 |
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| creator | Board, Philip G. Menon, Deepthi |
| description | The Omega-class cytosolic glutathione transferases (GSTs) have distinct structural and functional attributes that allow them to perform novel roles unrelated to the functions of other GSTs. Mammalian GSTO1-1 has been found to play a previously unappreciated role in the glutathionylation cycle that is emerging as significant mechanism regulating protein function. GSTO1-1-catalyzed glutathionylation or deglutathionylation of a key signaling protein may explain the requirement for catalytically active GSTO1-1 in LPS-stimulated pro-inflammatory signaling through the TLR4 receptor. The observation that ML175 a specific GSTO1-1 inhibitor can block LPS-stimulated inflammatory signaling has opened a new avenue for the development of novel anti-inflammatory drugs that could be useful in the treatment of toxic shock and other inflammatory disorders. The role of GSTO2-2 remains unclear. As a dehydroascorbate reductase, it could contribute to the maintenance of cellular redox balance and it is interesting to note that the
GSTO2 N142D
polymorphism has been associated with multiple diseases including Alzheimer’s disease, Parkinson’s disease, familial amyotrophic lateral sclerosis, chronic obstructive pulmonary disease, age-related cataract and breast cancer. |
| doi_str_mv | 10.1007/s00204-016-1691-1 |
| format | Article |
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GSTO2 N142D
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GSTO2 N142D
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Menon, Deepthi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c471t-e8384e9a1db55236c3de4cd11be84d534b33cc74683ca328a4122324e13db63e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Animals</topic><topic>Anti-Inflammatory Agents - pharmacology</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Environmental Health</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>Genetic Predisposition to Disease</topic><topic>Genetic recombination</topic><topic>Glutathione - metabolism</topic><topic>Glutathione Transferase - antagonists & inhibitors</topic><topic>Glutathione Transferase - chemistry</topic><topic>Glutathione Transferase - genetics</topic><topic>Glutathione Transferase - metabolism</topic><topic>Humans</topic><topic>Inactivation, Metabolic</topic><topic>Inflammation</topic><topic>Occupational Medicine/Industrial Medicine</topic><topic>Oxidation-Reduction</topic><topic>Pharmacology/Toxicology</topic><topic>Polymorphism, Genetic</topic><topic>Protein Conformation</topic><topic>Protein Processing, Post-Translational</topic><topic>Proteins</topic><topic>Review Article</topic><topic>Structure-Activity Relationship</topic><topic>Substrate Specificity</topic><topic>Toxicology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Board, Philip G.</creatorcontrib><creatorcontrib>Menon, Deepthi</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health and Safety Science Abstracts (Full archive)</collection><collection>Neurosciences Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Science Database</collection><collection>Research Library (Corporate)</collection><collection>Environmental Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Environmental Science Collection</collection><collection>ProQuest Central Basic</collection><collection>Safety Science and Risk</collection><jtitle>Archives of toxicology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Board, Philip G.</au><au>Menon, Deepthi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure, function and disease relevance of Omega-class glutathione transferases</atitle><jtitle>Archives of toxicology</jtitle><stitle>Arch Toxicol</stitle><addtitle>Arch Toxicol</addtitle><date>2016-05-01</date><risdate>2016</risdate><volume>90</volume><issue>5</issue><spage>1049</spage><epage>1067</epage><pages>1049-1067</pages><issn>0340-5761</issn><eissn>1432-0738</eissn><abstract>The Omega-class cytosolic glutathione transferases (GSTs) have distinct structural and functional attributes that allow them to perform novel roles unrelated to the functions of other GSTs. Mammalian GSTO1-1 has been found to play a previously unappreciated role in the glutathionylation cycle that is emerging as significant mechanism regulating protein function. GSTO1-1-catalyzed glutathionylation or deglutathionylation of a key signaling protein may explain the requirement for catalytically active GSTO1-1 in LPS-stimulated pro-inflammatory signaling through the TLR4 receptor. The observation that ML175 a specific GSTO1-1 inhibitor can block LPS-stimulated inflammatory signaling has opened a new avenue for the development of novel anti-inflammatory drugs that could be useful in the treatment of toxic shock and other inflammatory disorders. The role of GSTO2-2 remains unclear. As a dehydroascorbate reductase, it could contribute to the maintenance of cellular redox balance and it is interesting to note that the
GSTO2 N142D
polymorphism has been associated with multiple diseases including Alzheimer’s disease, Parkinson’s disease, familial amyotrophic lateral sclerosis, chronic obstructive pulmonary disease, age-related cataract and breast cancer.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>26993125</pmid><doi>10.1007/s00204-016-1691-1</doi><tpages>19</tpages></addata></record> |
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| ispartof | Archives of toxicology, 2016-05, Vol.90 (5), p.1049-1067 |
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| subjects | Animals Anti-Inflammatory Agents - pharmacology Biomedical and Life Sciences Biomedicine Environmental Health Enzyme Inhibitors - pharmacology Gene Expression Regulation, Enzymologic Genetic Predisposition to Disease Genetic recombination Glutathione - metabolism Glutathione Transferase - antagonists & inhibitors Glutathione Transferase - chemistry Glutathione Transferase - genetics Glutathione Transferase - metabolism Humans Inactivation, Metabolic Inflammation Occupational Medicine/Industrial Medicine Oxidation-Reduction Pharmacology/Toxicology Polymorphism, Genetic Protein Conformation Protein Processing, Post-Translational Proteins Review Article Structure-Activity Relationship Substrate Specificity Toxicology |
| title | Structure, function and disease relevance of Omega-class glutathione transferases |
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