GlutaredoxinV1, Main, Exploration, bibRecord, 000330

Physical interaction between human ribonucleotide reductase large subunit and thioredoxin increases colorectal cancer malignancy.

Identifieur interne : 000330 ( Main/Exploration ); précédent : 000329; suivant : 000331

Physical interaction between human ribonucleotide reductase large subunit and thioredoxin increases colorectal cancer malignancy.

Source :

The Journal of biological chemistry [ 1083-351X ] ; 2017.

RBID : pubmed:28411237

Descripteurs français

English descriptors

KwdEn :
- Animals (MeSH), Cell Line, Tumor (MeSH), Colorectal Neoplasms (enzymology), Colorectal Neoplasms (genetics), Colorectal Neoplasms (pathology), Gene Expression Regulation, Enzymologic (MeSH), Gene Expression Regulation, Neoplastic (MeSH), Glutaredoxins (biosynthesis), Glutaredoxins (genetics), Humans (MeSH), Mice (MeSH), Mice, Inbred BALB C (MeSH), Mice, Nude (MeSH), Thioredoxins (biosynthesis), Thioredoxins (genetics), Tumor Suppressor Proteins (biosynthesis), Tumor Suppressor Proteins (genetics), Up-Regulation (MeSH).
MESH :
- chemical , biosynthesis : Glutaredoxins, Thioredoxins, Tumor Suppressor Proteins.
- enzymology : Colorectal Neoplasms.
- genetics : Colorectal Neoplasms, Glutaredoxins, Thioredoxins, Tumor Suppressor Proteins.
- pathology : Colorectal Neoplasms.
- Animals, Cell Line, Tumor, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Neoplastic, Humans, Mice, Mice, Inbred BALB C, Mice, Nude, Up-Regulation.

Abstract

Ribonucleotide reductase (RR) is the rate-limiting enzyme in DNA synthesis, catalyzing the reduction of ribonucleotides to deoxyribonucleotides. During each enzymatic turnover, reduction of the active site disulfide in the catalytic large subunit is performed by a pair of shuttle cysteine residues in its C-terminal tail. Thioredoxin (Trx) and glutaredoxin (Grx) are ubiquitous redox proteins, catalyzing thiol-disulfide exchange reactions. Here, immunohistochemical examination of clinical colorectal cancer (CRC) specimens revealed that human thioredoxin1 (hTrx1), but not human glutaredoxin1 (hGrx1), was up-regulated along with human RR large subunit (RRM1) in cancer tissues, and the expression levels of both proteins were correlated with cancer malignancy stage. Ectopically expressed hTrx1 significantly increased RR activity, DNA synthesis, and cell proliferation and migration. Importantly, inhibition of both hTrx1 and RRM1 produced a synergistic anticancer effect in CRC cells and xenograft mice. Furthermore, hTrx1 rather than hGrx1 was the efficient reductase for RRM1 regeneration. We also observed a direct protein-protein interaction between RRM1 and hTrx1 in CRC cells. Interestingly, besides the known two conserved cysteines, a third cysteine (Cys⁷⁷⁹) in the RRM1 C terminus was essential for RRM1 regeneration and binding to hTrx1, whereas both Cys³² and Cys³⁵ in hTrx1 played a counterpart role. Our findings suggest that the up-regulated RRM1 and hTrx1 in CRC directly interact with each other and promote RR activity, resulting in enhanced DNA synthesis and cancer malignancy. We propose that the RRM1-hTrx1 interaction might be a novel potential therapeutic target for cancer treatment.

DOI: 10.1074/jbc.M117.783365
PubMed: 28411237
PubMed Central: PMC5454097

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000351
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Le document en format XML

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<author><name sortKey="Lou, Meng" sort="Lou, Meng" uniqKey="Lou M" first="Meng" last="Lou">Meng Lou</name>
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<country xml:lang="fr">République populaire de Chine</country>
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<author><name sortKey="Liu, Xia" sort="Liu, Xia" uniqKey="Liu X" first="Xia" last="Liu">Xia Liu</name>
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<author><name sortKey="Zhu, Lijun" sort="Zhu, Lijun" uniqKey="Zhu L" first="Lijun" last="Zhu">Lijun Zhu</name>
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<author><name sortKey="Qi, Hongyan" sort="Qi, Hongyan" uniqKey="Qi H" first="Hongyan" last="Qi">Hongyan Qi</name>
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<country xml:lang="fr">République populaire de Chine</country>
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<author><name sortKey="Shen, Jing" sort="Shen, Jing" uniqKey="Shen J" first="Jing" last="Shen">Jing Shen</name>
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<country xml:lang="fr">République populaire de Chine</country>
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<author><name sortKey="Li, Haoran" sort="Li, Haoran" uniqKey="Li H" first="Haoran" last="Li">Haoran Li</name>
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<author><name sortKey="Shao, Jimin" sort="Shao, Jimin" uniqKey="Shao J" first="Jimin" last="Shao">Jimin Shao</name>
<affiliation wicri:level="1"><nlm:affiliation>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058, China, shaojimin@zju.edu.cn.</nlm:affiliation>
<country wicri:rule="url">République populaire de Chine</country>
<wicri:regionArea>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058, China</wicri:regionArea>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Physical interaction between human ribonucleotide reductase large subunit and thioredoxin increases colorectal cancer malignancy.</title>
<author><name sortKey="Lou, Meng" sort="Lou, Meng" uniqKey="Lou M" first="Meng" last="Lou">Meng Lou</name>
<affiliation wicri:level="1"><nlm:affiliation>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058, China.</nlm:affiliation>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058</wicri:regionArea>
<placeName><settlement type="city">Hangzhou</settlement>
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</placeName>
</affiliation>
</author>
<author><name sortKey="Liu, Qian" sort="Liu, Qian" uniqKey="Liu Q" first="Qian" last="Liu">Qian Liu</name>
<affiliation wicri:level="1"><nlm:affiliation>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058, China.</nlm:affiliation>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058</wicri:regionArea>
<placeName><settlement type="city">Hangzhou</settlement>
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<author><name sortKey="Ren, Guoping" sort="Ren, Guoping" uniqKey="Ren G" first="Guoping" last="Ren">Guoping Ren</name>
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<wicri:noCountry code="no comma">the Departments of Pathology and.</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Zeng, Jiling" sort="Zeng, Jiling" uniqKey="Zeng J" first="Jiling" last="Zeng">Jiling Zeng</name>
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<wicri:noCountry code="no comma">the Departments of Pathology and.</wicri:noCountry>
</affiliation>
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<author><name sortKey="Xiang, Xueping" sort="Xiang, Xueping" uniqKey="Xiang X" first="Xueping" last="Xiang">Xueping Xiang</name>
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<wicri:noCountry code="subField">and</wicri:noCountry>
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<author><name sortKey="Ding, Yongfeng" sort="Ding, Yongfeng" uniqKey="Ding Y" first="Yongfeng" last="Ding">Yongfeng Ding</name>
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<wicri:noCountry code="no comma">Surgical Oncology and.</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Lin, Qinghui" sort="Lin, Qinghui" uniqKey="Lin Q" first="Qinghui" last="Lin">Qinghui Lin</name>
<affiliation wicri:level="1"><nlm:affiliation>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058, China.</nlm:affiliation>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058</wicri:regionArea>
<placeName><settlement type="city">Hangzhou</settlement>
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<author><name sortKey="Zhong, Tingting" sort="Zhong, Tingting" uniqKey="Zhong T" first="Tingting" last="Zhong">Tingting Zhong</name>
<affiliation wicri:level="1"><nlm:affiliation>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058, China.</nlm:affiliation>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058</wicri:regionArea>
<placeName><settlement type="city">Hangzhou</settlement>
<region type="province">Zhejiang</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Liu, Xia" sort="Liu, Xia" uniqKey="Liu X" first="Xia" last="Liu">Xia Liu</name>
<affiliation wicri:level="1"><nlm:affiliation>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058, China.</nlm:affiliation>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058</wicri:regionArea>
<placeName><settlement type="city">Hangzhou</settlement>
<region type="province">Zhejiang</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Zhu, Lijun" sort="Zhu, Lijun" uniqKey="Zhu L" first="Lijun" last="Zhu">Lijun Zhu</name>
<affiliation wicri:level="1"><nlm:affiliation>Key Laboratory of Precision Diagnosis and Treatment for Hepatobiliary and Pancreatic Tumor of Zhejiang Province, First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310003, China.</nlm:affiliation>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>Key Laboratory of Precision Diagnosis and Treatment for Hepatobiliary and Pancreatic Tumor of Zhejiang Province, First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310003</wicri:regionArea>
<placeName><settlement type="city">Hangzhou</settlement>
<region type="province">Zhejiang</region>
</placeName>
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</author>
<author><name sortKey="Qi, Hongyan" sort="Qi, Hongyan" uniqKey="Qi H" first="Hongyan" last="Qi">Hongyan Qi</name>
<affiliation wicri:level="1"><nlm:affiliation>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058, China.</nlm:affiliation>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058</wicri:regionArea>
<placeName><settlement type="city">Hangzhou</settlement>
<region type="province">Zhejiang</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Shen, Jing" sort="Shen, Jing" uniqKey="Shen J" first="Jing" last="Shen">Jing Shen</name>
<affiliation wicri:level="1"><nlm:affiliation>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058, China.</nlm:affiliation>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058</wicri:regionArea>
<placeName><settlement type="city">Hangzhou</settlement>
<region type="province">Zhejiang</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Li, Haoran" sort="Li, Haoran" uniqKey="Li H" first="Haoran" last="Li">Haoran Li</name>
<affiliation wicri:level="2"><nlm:affiliation>Takeda Pharmaceuticals International Company, Cambridge, Massachusetts 02139.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Massachusetts</region>
</placeName>
<wicri:cityArea>Takeda Pharmaceuticals International Company, Cambridge</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Shao, Jimin" sort="Shao, Jimin" uniqKey="Shao J" first="Jimin" last="Shao">Jimin Shao</name>
<affiliation wicri:level="1"><nlm:affiliation>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058, China, shaojimin@zju.edu.cn.</nlm:affiliation>
<country wicri:rule="url">République populaire de Chine</country>
<wicri:regionArea>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058, China</wicri:regionArea>
<wicri:noRegion>China</wicri:noRegion>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term>
<term>Cell Line, Tumor (MeSH)</term>
<term>Colorectal Neoplasms (enzymology)</term>
<term>Colorectal Neoplasms (genetics)</term>
<term>Colorectal Neoplasms (pathology)</term>
<term>Gene Expression Regulation, Enzymologic (MeSH)</term>
<term>Gene Expression Regulation, Neoplastic (MeSH)</term>
<term>Glutaredoxins (biosynthesis)</term>
<term>Glutaredoxins (genetics)</term>
<term>Humans (MeSH)</term>
<term>Mice (MeSH)</term>
<term>Mice, Inbred BALB C (MeSH)</term>
<term>Mice, Nude (MeSH)</term>
<term>Thioredoxins (biosynthesis)</term>
<term>Thioredoxins (genetics)</term>
<term>Tumor Suppressor Proteins (biosynthesis)</term>
<term>Tumor Suppressor Proteins (genetics)</term>
<term>Up-Regulation (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term>
<term>Glutarédoxines (biosynthèse)</term>
<term>Glutarédoxines (génétique)</term>
<term>Humains (MeSH)</term>
<term>Lignée cellulaire tumorale (MeSH)</term>
<term>Protéines suppresseurs de tumeurs (biosynthèse)</term>
<term>Protéines suppresseurs de tumeurs (génétique)</term>
<term>Régulation de l'expression des gènes codant pour des enzymes (MeSH)</term>
<term>Régulation de l'expression des gènes tumoraux (MeSH)</term>
<term>Régulation positive (MeSH)</term>
<term>Souris (MeSH)</term>
<term>Souris de lignée BALB C (MeSH)</term>
<term>Souris nude (MeSH)</term>
<term>Thiorédoxines (biosynthèse)</term>
<term>Thiorédoxines (génétique)</term>
<term>Tumeurs colorectales (anatomopathologie)</term>
<term>Tumeurs colorectales (enzymologie)</term>
<term>Tumeurs colorectales (génétique)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Glutaredoxins</term>
<term>Thioredoxins</term>
<term>Tumor Suppressor Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Tumeurs colorectales</term>
</keywords>
<keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Glutarédoxines</term>
<term>Protéines suppresseurs de tumeurs</term>
<term>Thiorédoxines</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Tumeurs colorectales</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Colorectal Neoplasms</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Colorectal Neoplasms</term>
<term>Glutaredoxins</term>
<term>Thioredoxins</term>
<term>Tumor Suppressor Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutarédoxines</term>
<term>Protéines suppresseurs de tumeurs</term>
<term>Thiorédoxines</term>
<term>Tumeurs colorectales</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Colorectal Neoplasms</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Cell Line, Tumor</term>
<term>Gene Expression Regulation, Enzymologic</term>
<term>Gene Expression Regulation, Neoplastic</term>
<term>Humans</term>
<term>Mice</term>
<term>Mice, Inbred BALB C</term>
<term>Mice, Nude</term>
<term>Up-Regulation</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Humains</term>
<term>Lignée cellulaire tumorale</term>
<term>Régulation de l'expression des gènes codant pour des enzymes</term>
<term>Régulation de l'expression des gènes tumoraux</term>
<term>Régulation positive</term>
<term>Souris</term>
<term>Souris de lignée BALB C</term>
<term>Souris nude</term>
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<front><div type="abstract" xml:lang="en">Ribonucleotide reductase (RR) is the rate-limiting enzyme in DNA synthesis, catalyzing the reduction of ribonucleotides to deoxyribonucleotides. During each enzymatic turnover, reduction of the active site disulfide in the catalytic large subunit is performed by a pair of shuttle cysteine residues in its C-terminal tail. Thioredoxin (Trx) and glutaredoxin (Grx) are ubiquitous redox proteins, catalyzing thiol-disulfide exchange reactions. Here, immunohistochemical examination of clinical colorectal cancer (CRC) specimens revealed that human thioredoxin1 (hTrx1), but not human glutaredoxin1 (hGrx1), was up-regulated along with human RR large subunit (RRM1) in cancer tissues, and the expression levels of both proteins were correlated with cancer malignancy stage. Ectopically expressed hTrx1 significantly increased RR activity, DNA synthesis, and cell proliferation and migration. Importantly, inhibition of both hTrx1 and RRM1 produced a synergistic anticancer effect in CRC cells and xenograft mice. Furthermore, hTrx1 rather than hGrx1 was the efficient reductase for RRM1 regeneration. We also observed a direct protein-protein interaction between RRM1 and hTrx1 in CRC cells. Interestingly, besides the known two conserved cysteines, a third cysteine (Cys<sup>779</sup>
) in the RRM1 C terminus was essential for RRM1 regeneration and binding to hTrx1, whereas both Cys<sup>32</sup>
 and Cys<sup>35</sup>
 in hTrx1 played a counterpart role. Our findings suggest that the up-regulated RRM1 and hTrx1 in CRC directly interact with each other and promote RR activity, resulting in enhanced DNA synthesis and cancer malignancy. We propose that the RRM1-hTrx1 interaction might be a novel potential therapeutic target for cancer treatment.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28411237</PMID>
<DateCompleted><Year>2017</Year>
<Month>06</Month>
<Day>09</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>01</Month>
<Day>03</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>292</Volume>
<Issue>22</Issue>
<PubDate><Year>2017</Year>
<Month>06</Month>
<Day>02</Day>
</PubDate>
</JournalIssue>
<Title>The Journal of biological chemistry</Title>
<ISOAbbreviation>J Biol Chem</ISOAbbreviation>
</Journal>
<ArticleTitle>Physical interaction between human ribonucleotide reductase large subunit and thioredoxin increases colorectal cancer malignancy.</ArticleTitle>
<Pagination><MedlinePgn>9136-9149</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M117.783365</ELocationID>
<Abstract><AbstractText>Ribonucleotide reductase (RR) is the rate-limiting enzyme in DNA synthesis, catalyzing the reduction of ribonucleotides to deoxyribonucleotides. During each enzymatic turnover, reduction of the active site disulfide in the catalytic large subunit is performed by a pair of shuttle cysteine residues in its C-terminal tail. Thioredoxin (Trx) and glutaredoxin (Grx) are ubiquitous redox proteins, catalyzing thiol-disulfide exchange reactions. Here, immunohistochemical examination of clinical colorectal cancer (CRC) specimens revealed that human thioredoxin1 (hTrx1), but not human glutaredoxin1 (hGrx1), was up-regulated along with human RR large subunit (RRM1) in cancer tissues, and the expression levels of both proteins were correlated with cancer malignancy stage. Ectopically expressed hTrx1 significantly increased RR activity, DNA synthesis, and cell proliferation and migration. Importantly, inhibition of both hTrx1 and RRM1 produced a synergistic anticancer effect in CRC cells and xenograft mice. Furthermore, hTrx1 rather than hGrx1 was the efficient reductase for RRM1 regeneration. We also observed a direct protein-protein interaction between RRM1 and hTrx1 in CRC cells. Interestingly, besides the known two conserved cysteines, a third cysteine (Cys<sup>779</sup>
) in the RRM1 C terminus was essential for RRM1 regeneration and binding to hTrx1, whereas both Cys<sup>32</sup>
 and Cys<sup>35</sup>
 in hTrx1 played a counterpart role. Our findings suggest that the up-regulated RRM1 and hTrx1 in CRC directly interact with each other and promote RR activity, resulting in enhanced DNA synthesis and cancer malignancy. We propose that the RRM1-hTrx1 interaction might be a novel potential therapeutic target for cancer treatment.</AbstractText>
<CopyrightInformation>© 2017 by The American Society for Biochemistry and Molecular Biology, Inc.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lou</LastName>
<ForeName>Meng</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Liu</LastName>
<ForeName>Qian</ForeName>
<Initials>Q</Initials>
<AffiliationInfo><Affiliation>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ren</LastName>
<ForeName>Guoping</ForeName>
<Initials>G</Initials>
<AffiliationInfo><Affiliation>the Departments of Pathology and.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zeng</LastName>
<ForeName>Jiling</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>the Departments of Pathology and.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Xiang</LastName>
<ForeName>Xueping</ForeName>
<Initials>X</Initials>
<AffiliationInfo><Affiliation>the Department of Pathology, Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310003, China, and.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ding</LastName>
<ForeName>Yongfeng</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>Surgical Oncology and.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lin</LastName>
<ForeName>Qinghui</ForeName>
<Initials>Q</Initials>
<AffiliationInfo><Affiliation>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhong</LastName>
<ForeName>Tingting</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Liu</LastName>
<ForeName>Xia</ForeName>
<Initials>X</Initials>
<AffiliationInfo><Affiliation>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhu</LastName>
<ForeName>Lijun</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>Key Laboratory of Precision Diagnosis and Treatment for Hepatobiliary and Pancreatic Tumor of Zhejiang Province, First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310003, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Qi</LastName>
<ForeName>Hongyan</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Shen</LastName>
<ForeName>Jing</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Li</LastName>
<ForeName>Haoran</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>Takeda Pharmaceuticals International Company, Cambridge, Massachusetts 02139.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Shao</LastName>
<ForeName>Jimin</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>From the Department of Pathology and Pathophysiology, Key Laboratory of Disease Proteomics of Zhejiang Province, Research Center for Air Pollution and Health, Zhejiang University School of Medicine, Hangzhou 310058, China, shaojimin@zju.edu.cn.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2017</Year>
<Month>04</Month>
<Day>14</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>J Biol Chem</MedlineTA>
<NlmUniqueID>2985121R</NlmUniqueID>
<ISSNLinking>0021-9258</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C516005">GLRX protein, human</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D025521">Tumor Suppressor Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>52500-60-4</RegistryNumber>
<NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.17.4.1</RegistryNumber>
<NameOfSubstance UI="C475286">RRM1 protein, human</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D045744" MajorTopicYN="N">Cell Line, Tumor</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015179" MajorTopicYN="N">Colorectal Neoplasms</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015971" MajorTopicYN="Y">Gene Expression Regulation, Enzymologic</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015972" MajorTopicYN="Y">Gene Expression Regulation, Neoplastic</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName>
<QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008807" MajorTopicYN="N">Mice, Inbred BALB C</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008819" MajorTopicYN="N">Mice, Nude</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName>
<QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D025521" MajorTopicYN="N">Tumor Suppressor Proteins</DescriptorName>
<QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015854" MajorTopicYN="Y">Up-Regulation</DescriptorName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">colorectal cancer</Keyword>
<Keyword MajorTopicYN="Y">enzyme catalysis</Keyword>
<Keyword MajorTopicYN="Y">protein-protein interaction</Keyword>
<Keyword MajorTopicYN="Y">ribonucleotide reductase</Keyword>
<Keyword MajorTopicYN="Y">thioredoxin</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year>
<Month>02</Month>
<Day>25</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2017</Year>
<Month>04</Month>
<Day>11</Day>
</PubMedPubDate>
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<Month>4</Month>
<Day>16</Day>
<Hour>6</Hour>
<Minute>0</Minute>
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<PubMedPubDate PubStatus="medline"><Year>2017</Year>
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<Day>16</Day>
<Hour>6</Hour>
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<ArticleId IdType="doi">10.1074/jbc.M117.783365</ArticleId>
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<affiliations><list><country><li>République populaire de Chine</li>
<li>États-Unis</li>
</country>
<region><li>Massachusetts</li>
<li>Zhejiang</li>
</region>
<settlement><li>Hangzhou</li>
</settlement>
</list>
<tree><noCountry><name sortKey="Ding, Yongfeng" sort="Ding, Yongfeng" uniqKey="Ding Y" first="Yongfeng" last="Ding">Yongfeng Ding</name>
<name sortKey="Ren, Guoping" sort="Ren, Guoping" uniqKey="Ren G" first="Guoping" last="Ren">Guoping Ren</name>
<name sortKey="Xiang, Xueping" sort="Xiang, Xueping" uniqKey="Xiang X" first="Xueping" last="Xiang">Xueping Xiang</name>
<name sortKey="Zeng, Jiling" sort="Zeng, Jiling" uniqKey="Zeng J" first="Jiling" last="Zeng">Jiling Zeng</name>
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</region>
<name sortKey="Lin, Qinghui" sort="Lin, Qinghui" uniqKey="Lin Q" first="Qinghui" last="Lin">Qinghui Lin</name>
<name sortKey="Liu, Qian" sort="Liu, Qian" uniqKey="Liu Q" first="Qian" last="Liu">Qian Liu</name>
<name sortKey="Liu, Xia" sort="Liu, Xia" uniqKey="Liu X" first="Xia" last="Liu">Xia Liu</name>
<name sortKey="Qi, Hongyan" sort="Qi, Hongyan" uniqKey="Qi H" first="Hongyan" last="Qi">Hongyan Qi</name>
<name sortKey="Shao, Jimin" sort="Shao, Jimin" uniqKey="Shao J" first="Jimin" last="Shao">Jimin Shao</name>
<name sortKey="Shen, Jing" sort="Shen, Jing" uniqKey="Shen J" first="Jing" last="Shen">Jing Shen</name>
<name sortKey="Zhong, Tingting" sort="Zhong, Tingting" uniqKey="Zhong T" first="Tingting" last="Zhong">Tingting Zhong</name>
<name sortKey="Zhu, Lijun" sort="Zhu, Lijun" uniqKey="Zhu L" first="Lijun" last="Zhu">Lijun Zhu</name>
</country>
<country name="États-Unis"><region name="Massachusetts"><name sortKey="Li, Haoran" sort="Li, Haoran" uniqKey="Li H" first="Haoran" last="Li">Haoran Li</name>
</region>
</country>
</tree>
</affiliations>
</record>

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HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000330 | SxmlIndent | more

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{{Explor lien
   |wiki=    Bois
   |area=    GlutaredoxinV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:28411237
   |texte=   Physical interaction between human ribonucleotide reductase large subunit and thioredoxin increases colorectal cancer malignancy.
}}

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       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
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This area was generated with Dilib version V0.6.37.
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	Serveur d'exploration sur la glutarédoxine
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Serveur d'exploration sur la glutarédoxine

Physical interaction between human ribonucleotide reductase large subunit and thioredoxin increases colorectal cancer malignancy.

Physical interaction between human ribonucleotide reductase large subunit and thioredoxin increases colorectal cancer malignancy.

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