Toxicoproteomic Profiling of hPXR Transgenic Mice Treated with Rifampicin and Isoniazid.
Identifieur interne : 000010 ( Main/Exploration ); précédent : 000009; suivant : 000011Toxicoproteomic Profiling of hPXR Transgenic Mice Treated with Rifampicin and Isoniazid.
Auteurs : Christopher Trent Brewer [États-Unis] ; Kiran Kodali [États-Unis] ; Jing Wu [États-Unis] ; Timothy I. Shaw [États-Unis] ; Junmin Peng [États-Unis] ; Taosheng Chen [États-Unis]Source :
- Cells [ 2073-4409 ] ; 2020.
Abstract
Tuberculosis is a global health threat that affects millions of people every year, and treatment-limiting toxicity remains a considerable source of treatment failure. Recent reports have characterized the nature of hPXR-mediated hepatotoxicity and the systemic toxicity of antitubercular drugs. The antitubercular drug isoniazid plays a role in such pathologic states as acute intermittent porphyria, anemia, hepatotoxicity, hypercoagulable states (deep vein thrombosis, pulmonary embolism, or ischemic stroke), pellagra (vitamin B3 deficiency), peripheral neuropathy, and vitamin B6 deficiency. However, the mechanisms by which isoniazid administration leads to these states are unclear. To elucidate the mechanism of rifampicin- and isoniazid-induced liver and systemic injury, we performed tandem mass tag mass spectrometry-based proteomic screening of mPxr-/- and hPXR mice treated with combinations of rifampicin and isoniazid. Proteomic profiling analysis suggested that the hPXR liver proteome is affected by antitubercular therapy to disrupt [Fe-S] cluster assembly machinery, [2Fe-2S] cluster-containing proteins, cytochrome P450 enzymes, heme biosynthesis, homocysteine catabolism, oxidative stress responses, vitamin B3 metabolism, and vitamin B6 metabolism. These novel findings provide insight into the etiology of some of these processes and potential targets for subsequent investigations. Data are available via ProteomeXchange with identifier PXD019505.
DOI: 10.3390/cells9071654
PubMed: 32660103
PubMed Central: PMC7407182
Affiliations:
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xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, TN 38105</wicri:regionArea><placeName><region type="state">Tennessee</region></placeName></affiliation><affiliation wicri:level="2"><nlm:affiliation>College of Medicine, University of Tennessee Health Science Center, Memphis, TN 38163, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>College of Medicine, University of Tennessee Health Science Center, Memphis, TN 38163</wicri:regionArea><placeName><region type="state">Tennessee</region></placeName></affiliation><affiliation wicri:level="2"><nlm:affiliation>Integrated Biomedical Sciences Program, College of Graduate Health Sciences, University of Tennessee Health Science Center, Memphis, TN 38163, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Integrated Biomedical Sciences Program, College of Graduate Health Sciences, University of Tennessee Health Science Center, Memphis, TN 38163</wicri:regionArea><placeName><region type="state">Tennessee</region></placeName></affiliation></author><author><name sortKey="Kodali, Kiran" sort="Kodali, Kiran" uniqKey="Kodali K" first="Kiran" last="Kodali">Kiran Kodali</name><affiliation wicri:level="2"><nlm:affiliation>Center for Proteomics and Metabolomics, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Center for Proteomics and Metabolomics, St. Jude Children's Research Hospital, Memphis, TN 38105</wicri:regionArea><placeName><region type="state">Tennessee</region></placeName></affiliation></author><author><name sortKey="Wu, Jing" sort="Wu, Jing" uniqKey="Wu J" first="Jing" last="Wu">Jing Wu</name><affiliation wicri:level="2"><nlm:affiliation>Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, TN 38105</wicri:regionArea><placeName><region type="state">Tennessee</region></placeName></affiliation></author><author><name sortKey="Shaw, Timothy I" sort="Shaw, Timothy I" uniqKey="Shaw T" first="Timothy I" last="Shaw">Timothy I. Shaw</name><affiliation wicri:level="2"><nlm:affiliation>Center for Proteomics and Metabolomics, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Center for Proteomics and Metabolomics, St. Jude Children's Research Hospital, Memphis, TN 38105</wicri:regionArea><placeName><region type="state">Tennessee</region></placeName></affiliation><affiliation wicri:level="2"><nlm:affiliation>Department of Computational Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Computational Biology, St. Jude Children's Research Hospital, Memphis, TN 38105</wicri:regionArea><placeName><region type="state">Tennessee</region></placeName></affiliation></author><author><name sortKey="Peng, Junmin" sort="Peng, Junmin" uniqKey="Peng J" first="Junmin" last="Peng">Junmin Peng</name><affiliation wicri:level="2"><nlm:affiliation>Center for Proteomics and Metabolomics, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Center for Proteomics and Metabolomics, St. Jude Children's Research Hospital, Memphis, TN 38105</wicri:regionArea><placeName><region type="state">Tennessee</region></placeName></affiliation><affiliation wicri:level="2"><nlm:affiliation>Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105</wicri:regionArea><placeName><region type="state">Tennessee</region></placeName></affiliation><affiliation wicri:level="2"><nlm:affiliation>Department of Developmental Neurobiology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Developmental Neurobiology, St. Jude Children's Research Hospital, Memphis, TN 38105</wicri:regionArea><placeName><region type="state">Tennessee</region></placeName></affiliation></author><author><name sortKey="Chen, Taosheng" sort="Chen, Taosheng" uniqKey="Chen T" first="Taosheng" last="Chen">Taosheng Chen</name><affiliation wicri:level="2"><nlm:affiliation>Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, TN 38105</wicri:regionArea><placeName><region type="state">Tennessee</region></placeName></affiliation></author></analytic><series><title level="j">Cells</title><idno type="eISSN">2073-4409</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Tuberculosis is a global health threat that affects millions of people every year, and treatment-limiting toxicity remains a considerable source of treatment failure. Recent reports have characterized the nature of <i>hPXR</i>-mediated hepatotoxicity and the systemic toxicity of antitubercular drugs. The antitubercular drug isoniazid plays a role in such pathologic states as acute intermittent porphyria, anemia, hepatotoxicity, hypercoagulable states (deep vein thrombosis, pulmonary embolism, or ischemic stroke), pellagra (vitamin B<sub>3</sub> deficiency), peripheral neuropathy, and vitamin B<sub>6</sub> deficiency. However, the mechanisms by which isoniazid administration leads to these states are unclear. To elucidate the mechanism of rifampicin- and isoniazid-induced liver and systemic injury, we performed tandem mass tag mass spectrometry-based proteomic screening of <i>mPxr</i><sup>-</sup><sup>/</sup><sup>-</sup> and <i>hPXR</i> mice treated with combinations of rifampicin and isoniazid. Proteomic profiling analysis suggested that the <i>hPXR</i> liver proteome is affected by antitubercular therapy to disrupt [Fe-S] cluster assembly machinery, [2Fe-2S] cluster-containing proteins, cytochrome P450 enzymes, heme biosynthesis, homocysteine catabolism, oxidative stress responses, vitamin B<sub>3</sub> metabolism, and vitamin B<sub>6</sub> metabolism. These novel findings provide insight into the etiology of some of these processes and potential targets for subsequent investigations. Data are available via ProteomeXchange with identifier PXD019505.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">32660103</PMID><DateRevised><Year>2020</Year><Month>11</Month><Day>20</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2073-4409</ISSN><JournalIssue CitedMedium="Internet"><Volume>9</Volume><Issue>7</Issue><PubDate><Year>2020</Year><Month>07</Month><Day>09</Day></PubDate></JournalIssue><Title>Cells</Title><ISOAbbreviation>Cells</ISOAbbreviation></Journal><ArticleTitle>Toxicoproteomic Profiling of <i>hPXR</i> Transgenic Mice Treated with Rifampicin and Isoniazid.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">E1654</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.3390/cells9071654</ELocationID><Abstract><AbstractText>Tuberculosis is a global health threat that affects millions of people every year, and treatment-limiting toxicity remains a considerable source of treatment failure. Recent reports have characterized the nature of <i>hPXR</i>-mediated hepatotoxicity and the systemic toxicity of antitubercular drugs. The antitubercular drug isoniazid plays a role in such pathologic states as acute intermittent porphyria, anemia, hepatotoxicity, hypercoagulable states (deep vein thrombosis, pulmonary embolism, or ischemic stroke), pellagra (vitamin B<sub>3</sub> deficiency), peripheral neuropathy, and vitamin B<sub>6</sub> deficiency. However, the mechanisms by which isoniazid administration leads to these states are unclear. To elucidate the mechanism of rifampicin- and isoniazid-induced liver and systemic injury, we performed tandem mass tag mass spectrometry-based proteomic screening of <i>mPxr</i><sup>-</sup><sup>/</sup><sup>-</sup> and <i>hPXR</i> mice treated with combinations of rifampicin and isoniazid. Proteomic profiling analysis suggested that the <i>hPXR</i> liver proteome is affected by antitubercular therapy to disrupt [Fe-S] cluster assembly machinery, [2Fe-2S] cluster-containing proteins, cytochrome P450 enzymes, heme biosynthesis, homocysteine catabolism, oxidative stress responses, vitamin B<sub>3</sub> metabolism, and vitamin B<sub>6</sub> metabolism. These novel findings provide insight into the etiology of some of these processes and potential targets for subsequent investigations. Data are available via ProteomeXchange with identifier PXD019505.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Brewer</LastName><ForeName>Christopher Trent</ForeName><Initials>CT</Initials><AffiliationInfo><Affiliation>Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>College of Medicine, University of Tennessee Health Science Center, Memphis, TN 38163, USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Integrated Biomedical Sciences Program, College of Graduate Health Sciences, University of Tennessee Health Science Center, Memphis, TN 38163, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kodali</LastName><ForeName>Kiran</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Center for Proteomics and Metabolomics, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>Jing</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shaw</LastName><ForeName>Timothy I</ForeName><Initials>TI</Initials><AffiliationInfo><Affiliation>Center for Proteomics and Metabolomics, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Computational Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Peng</LastName><ForeName>Junmin</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Center for Proteomics and Metabolomics, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Developmental Neurobiology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Taosheng</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R35 GM118041</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AG053987</GrantID><Acronym>AG</Acronym><Agency>NIA NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>F31 DK116523</GrantID><Acronym>DK</Acronym><Agency>NIDDK NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>07</Month><Day>09</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Cells</MedlineTA><NlmUniqueID>101600052</NlmUniqueID><ISSNLinking>2073-4409</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">anemia</Keyword><Keyword MajorTopicYN="Y">antitubercular therapy</Keyword><Keyword MajorTopicYN="Y">cytochrome P450</Keyword><Keyword MajorTopicYN="Y">drug-induced liver injury</Keyword><Keyword MajorTopicYN="Y">heme biosynthesis</Keyword><Keyword MajorTopicYN="Y">hypercoagulability</Keyword><Keyword MajorTopicYN="Y">iron–sulfur cluster</Keyword><Keyword MajorTopicYN="Y">pellagra</Keyword><Keyword MajorTopicYN="Y">vitamin B3</Keyword><Keyword MajorTopicYN="Y">vitamin B6</Keyword></KeywordList><CoiStatement>The authors declare no conflict of interest. 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Christopher Trent" uniqKey="Brewer C" first="Christopher Trent" last="Brewer">Christopher Trent Brewer</name><name sortKey="Chen, Taosheng" sort="Chen, Taosheng" uniqKey="Chen T" first="Taosheng" last="Chen">Taosheng Chen</name><name sortKey="Kodali, Kiran" sort="Kodali, Kiran" uniqKey="Kodali K" first="Kiran" last="Kodali">Kiran Kodali</name><name sortKey="Peng, Junmin" sort="Peng, Junmin" uniqKey="Peng J" first="Junmin" last="Peng">Junmin Peng</name><name sortKey="Peng, Junmin" sort="Peng, Junmin" uniqKey="Peng J" first="Junmin" last="Peng">Junmin Peng</name><name sortKey="Peng, Junmin" sort="Peng, Junmin" uniqKey="Peng J" first="Junmin" last="Peng">Junmin Peng</name><name sortKey="Shaw, Timothy I" sort="Shaw, Timothy I" uniqKey="Shaw T" first="Timothy I" last="Shaw">Timothy I. Shaw</name><name sortKey="Shaw, Timothy I" sort="Shaw, Timothy I" uniqKey="Shaw T" first="Timothy I" last="Shaw">Timothy I. Shaw</name><name sortKey="Wu, Jing" sort="Wu, Jing" uniqKey="Wu J" first="Jing" last="Wu">Jing Wu</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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