RapamycinFungusV1, Main, Exploration, bibRecord, 000668

Acetaminophen reduces the protein levels of high affinity amino acid permeases and causes tryptophan depletion.

Identifieur interne : 000668 ( Main/Exploration ); précédent : 000667; suivant : 000669

Acetaminophen reduces the protein levels of high affinity amino acid permeases and causes tryptophan depletion.

Auteurs : Angelina Huseinovic [Pays-Bas] ; Stefan J. Dekker [Pays-Bas] ; Bob Boogaard [Pays-Bas] ; Nico P E. Vermeulen [Pays-Bas] ; Jan M. Kooter [Pays-Bas] ; J Chris Vos [Pays-Bas]

Source :

Amino acids [ 1438-2199 ] ; 2018.

RBID : pubmed:29978260

Descripteurs français

KwdFr :
- Acides aminés (métabolisme), Acétaminophène (toxicité), Antienzymes (toxicité), Cellules HepG2 (MeSH), Humains (MeSH), Protéines de Saccharomyces cerevisiae (antagonistes et inhibiteurs), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Systèmes de transport d'acides aminés (antagonistes et inhibiteurs), Systèmes de transport d'acides aminés (génétique), Systèmes de transport d'acides aminés (métabolisme), Tryptophane (métabolisme), Ubiquitine (métabolisme).
MESH :
- antagonistes et inhibiteurs : Protéines de Saccharomyces cerevisiae, Systèmes de transport d'acides aminés.
- effets des médicaments et des substances chimiques : Saccharomyces cerevisiae.
- enzymologie : Saccharomyces cerevisiae.
- génétique : Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae, Systèmes de transport d'acides aminés.
- métabolisme : Acides aminés, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae, Systèmes de transport d'acides aminés, Tryptophane, Ubiquitine.
- toxicité : Acétaminophène, Antienzymes.
- Cellules HepG2, Humains.

English descriptors

KwdEn :
- Acetaminophen (toxicity), Amino Acid Transport Systems (antagonists & inhibitors), Amino Acid Transport Systems (genetics), Amino Acid Transport Systems (metabolism), Amino Acids (metabolism), Enzyme Inhibitors (toxicity), Hep G2 Cells (MeSH), Humans (MeSH), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (antagonists & inhibitors), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Tryptophan (metabolism), Ubiquitin (metabolism).
MESH :
- chemical , antagonists & inhibitors : Amino Acid Transport Systems, Saccharomyces cerevisiae Proteins.
- chemical , genetics : Amino Acid Transport Systems, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Amino Acid Transport Systems, Amino Acids, Saccharomyces cerevisiae Proteins, Tryptophan, Ubiquitin.
- chemical , toxicity : Acetaminophen, Enzyme Inhibitors.
- drug effects : Saccharomyces cerevisiae.
- enzymology : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Hep G2 Cells, Humans.

Abstract

In yeast, toxicity of acetaminophen (APAP), a frequently used analgesic and antipyretic drug, depends on ubiquitin-controlled processes. Previously, we showed a remarkable overlap in toxicity profiles between APAP and tyrosine, and a similarity with drugs like rapamycin and quinine, which induce degradation of the amino acid permease Tat2. Therefore, we investigated in yeast whether APAP reduced the expression levels of amino acid permeases. The protein levels of Tat2, Tat1, Mup1 and Hip1 were reduced, while the expression of the general permease Gap1 was increased, consistent with a nutrient starvation response. Overexpression of Tat1 and Tat2, but not Mup1, Hip1 and Gap1 conferred resistance to APAP. A tryptophan auxotrophic strain trp1Δ was more sensitive to APAP than wild-type and addition of tryptophan completely restored the growth restriction of trp1∆ upon APAP exposure, while tyrosine had an additive effect on APAP toxicity. Furthermore, intracellular aromatic amino acid concentrations were reduced upon APAP exposure. This effect was less prominent in ubiquitin-deficient yeast strains that were APAP resistant and showed a reduced degradation of high affinity amino acid permeases. APAP-induced changes in intracellular amino acid concentrations were also detected in hepatoma HepG2 cells indicating significance for humans.

DOI: 10.1007/s00726-018-2613-8
PubMed: 29978260
PubMed Central: PMC6153950

Affiliations:

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

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Le document en format XML

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<series><title level="j">Amino acids</title>
<idno type="eISSN">1438-2199</idno>
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<term>Amino Acid Transport Systems (antagonists & inhibitors)</term>
<term>Amino Acid Transport Systems (genetics)</term>
<term>Amino Acid Transport Systems (metabolism)</term>
<term>Amino Acids (metabolism)</term>
<term>Enzyme Inhibitors (toxicity)</term>
<term>Hep G2 Cells (MeSH)</term>
<term>Humans (MeSH)</term>
<term>Saccharomyces cerevisiae (drug effects)</term>
<term>Saccharomyces cerevisiae (enzymology)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (antagonists & inhibitors)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Tryptophan (metabolism)</term>
<term>Ubiquitin (metabolism)</term>
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<term>Acétaminophène (toxicité)</term>
<term>Antienzymes (toxicité)</term>
<term>Cellules HepG2 (MeSH)</term>
<term>Humains (MeSH)</term>
<term>Protéines de Saccharomyces cerevisiae (antagonistes et inhibiteurs)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Saccharomyces cerevisiae (effets des médicaments et des substances chimiques)</term>
<term>Saccharomyces cerevisiae (enzymologie)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
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<term>Systèmes de transport d'acides aminés (génétique)</term>
<term>Systèmes de transport d'acides aminés (métabolisme)</term>
<term>Tryptophane (métabolisme)</term>
<term>Ubiquitine (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Amino Acid Transport Systems</term>
<term>Saccharomyces cerevisiae Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Amino Acid Transport Systems</term>
<term>Saccharomyces cerevisiae Proteins</term>
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<term>Amino Acids</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Tryptophan</term>
<term>Ubiquitin</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Acetaminophen</term>
<term>Enzyme Inhibitors</term>
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<term>Systèmes de transport d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">In yeast, toxicity of acetaminophen (APAP), a frequently used analgesic and antipyretic drug, depends on ubiquitin-controlled processes. Previously, we showed a remarkable overlap in toxicity profiles between APAP and tyrosine, and a similarity with drugs like rapamycin and quinine, which induce degradation of the amino acid permease Tat2. Therefore, we investigated in yeast whether APAP reduced the expression levels of amino acid permeases. The protein levels of Tat2, Tat1, Mup1 and Hip1 were reduced, while the expression of the general permease Gap1 was increased, consistent with a nutrient starvation response. Overexpression of Tat1 and Tat2, but not Mup1, Hip1 and Gap1 conferred resistance to APAP. A tryptophan auxotrophic strain trp1Δ was more sensitive to APAP than wild-type and addition of tryptophan completely restored the growth restriction of trp1∆ upon APAP exposure, while tyrosine had an additive effect on APAP toxicity. Furthermore, intracellular aromatic amino acid concentrations were reduced upon APAP exposure. This effect was less prominent in ubiquitin-deficient yeast strains that were APAP resistant and showed a reduced degradation of high affinity amino acid permeases. APAP-induced changes in intracellular amino acid concentrations were also detected in hepatoma HepG2 cells indicating significance for humans.</div>
</front>
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<ArticleTitle>Acetaminophen reduces the protein levels of high affinity amino acid permeases and causes tryptophan depletion.</ArticleTitle>
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<Abstract><AbstractText>In yeast, toxicity of acetaminophen (APAP), a frequently used analgesic and antipyretic drug, depends on ubiquitin-controlled processes. Previously, we showed a remarkable overlap in toxicity profiles between APAP and tyrosine, and a similarity with drugs like rapamycin and quinine, which induce degradation of the amino acid permease Tat2. Therefore, we investigated in yeast whether APAP reduced the expression levels of amino acid permeases. The protein levels of Tat2, Tat1, Mup1 and Hip1 were reduced, while the expression of the general permease Gap1 was increased, consistent with a nutrient starvation response. Overexpression of Tat1 and Tat2, but not Mup1, Hip1 and Gap1 conferred resistance to APAP. A tryptophan auxotrophic strain trp1Δ was more sensitive to APAP than wild-type and addition of tryptophan completely restored the growth restriction of trp1∆ upon APAP exposure, while tyrosine had an additive effect on APAP toxicity. Furthermore, intracellular aromatic amino acid concentrations were reduced upon APAP exposure. This effect was less prominent in ubiquitin-deficient yeast strains that were APAP resistant and showed a reduced degradation of high affinity amino acid permeases. APAP-induced changes in intracellular amino acid concentrations were also detected in hepatoma HepG2 cells indicating significance for humans.</AbstractText>
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<Initials>A</Initials>
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<AffiliationInfo><Affiliation>AIMMS, Division of Molecular Toxicology, Department of Chemistry and Pharmaceutical Sciences, VU University Amsterdam, De Boelelaan 1083, 1081 HZ, Amsterdam, The Netherlands.</Affiliation>
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<Initials>NPE</Initials>
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</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Kooter</LastName>
<ForeName>Jan M</ForeName>
<Initials>JM</Initials>
<AffiliationInfo><Affiliation>AIMMS, Department of Molecular Cell Biology, Section Genetics, VU University Amsterdam, De Boelelaan 1083, 1081 HZ, Amsterdam, The Netherlands.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Vos</LastName>
<ForeName>J Chris</ForeName>
<Initials>JC</Initials>
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<AffiliationInfo><Affiliation>AIMMS, Division of Molecular Toxicology, Department of Chemistry and Pharmaceutical Sciences, VU University Amsterdam, De Boelelaan 1083, 1081 HZ, Amsterdam, The Netherlands. j.c.vos@vu.nl.</Affiliation>
</AffiliationInfo>
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<ReferenceList><Reference><Citation>J Biol Chem. 2003 Jul 18;278(29):26976-82</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12709439</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Physiol. 2012 Dec 15;590(24):6413-24</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23045339</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Genet. 1999 Dec;36(6):317-28</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10654085</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cancer Epidemiol Biomarkers Prev. 2011 Dec;20(12):2637-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21994402</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Paediatr Respir Rev. 2013 Mar;14(1):9-15; quiz 16</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23347656</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Genetics. 2012 Oct;192(2):319-60</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23028185</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 2003 Nov;23(21):7566-84</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14560004</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2009 Jul 3;284(27):17968-74</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19416971</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Genetics. 2012 Mar;190(3):885-929</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22419079</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Drug Metab Dispos. 2003 Dec;31(12):1499-506</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14625346</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>JAMA Pediatr. 2014 Apr;168(4):313-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24566677</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 1993 Aug;13(8):5010-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7687745</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>PLoS One. 2010 Aug 17;5(8):e11935</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20808905</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Arch Toxicol. 2017 Mar;91(3):1385-1400</Citation>
<ArticleIdList><ArticleId IdType="pubmed">27344343</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEMS Microbiol Lett. 2004 Oct 1;239(1):171-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15451116</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Pharm. 2014 Dec 1;11(12):4395-404</Citation>
<ArticleIdList><ArticleId IdType="pubmed">25313982</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Soc Trans. 2009 Feb;37(Pt 1):242-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19143640</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Chromatogr. 1992 Feb 7;591(1-2):181-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1613051</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Hepatology. 2005 Dec;42(6):1364-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16317692</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Yeast. 2015 Jan;32(1):29-45</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24733517</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Gene. 1983 Nov;25(2-3):333-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6363214</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Chem Biol Interact. 2016 Aug 5;255:12-22</Citation>
<ArticleIdList><ArticleId IdType="pubmed">26718876</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Toxicol In Vitro. 2018 Mar;47:259-268</Citation>
<ArticleIdList><ArticleId IdType="pubmed">29258884</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Amino Acids. 2016;2016:8952520</Citation>
<ArticleIdList><ArticleId IdType="pubmed">26881063</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Clin Oncol. 2011 Jun 10;29(17):2424-31</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21555699</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Traffic. 2009 Dec;10(12):1856-67</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19912579</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Liver Int. 2014 Aug;34(7):e171-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24575957</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 1999 Sep 20;146(6):1227-38</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10491387</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Pharmacol Toxicol. 1996 Apr;78(4):224-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8861779</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Biotechnol. 2014 Apr;32(4):373-80</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24658645</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Crit Rev Toxicol. 2001 Jan;31(1):55-138</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11215692</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Microbiology. 2005 Jan;151(Pt 1):99-111</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15632430</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Lancet. 2010 Jul 17;376(9736):190-201</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20638564</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>PLoS One. 2014 Apr 09;9(4):e93597</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24718614</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>PLoS One. 2017 Mar 14;12(3):e0173573</Citation>
<ArticleIdList><ArticleId IdType="pubmed">28291796</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Pak Med Assoc. 2012 May;62(5):524-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22755330</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell Biol Toxicol. 2012 Apr;28(2):69-87</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22258563</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Asia Pac Allergy. 2014 Jan;4(1):68-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24527413</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biotechnol Bioeng. 1992 Sep;40(6):643-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18601163</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Intern Med. 2003 Feb;253(2):240-3</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12542566</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 1994 Oct;14(10):6597-606</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7523855</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Sci. 2009 Jun 15;122(Pt 12):2089-99</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19494127</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>PLoS Genet. 2014 Dec 18;10(12):e1004860</Citation>
<ArticleIdList><ArticleId IdType="pubmed">25521617</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Anesthesiology. 1997 Jun;86(6):1359-66; discussion 8A</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9197306</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Eukaryot Cell. 2013 Jul;12(7):990-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23666621</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Genetics. 2002 Jun;161(2):563-74</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12072454</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
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Acetaminophen reduces the protein levels of high affinity amino acid permeases and causes tryptophan depletion.

Acetaminophen reduces the protein levels of high affinity amino acid permeases and causes tryptophan depletion.

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