SulfurTransferaseV1, Main, Exploration, bibRecord, 000071

The human allicin-proteome: S-thioallylation of proteins by the garlic defence substance allicin and its biological effects.

Identifieur interne : 000071 ( Main/Exploration ); précédent : 000070; suivant : 000072

The human allicin-proteome: S-thioallylation of proteins by the garlic defence substance allicin and its biological effects.

Auteurs : Martin C H. Gruhlke [Allemagne] ; Haike Antelmann [Allemagne] ; Jörg Bernhardt [Allemagne] ; Veronika Kloubert [Allemagne] ; Lothar Rink [Allemagne] ; Alan J. Slusarenko [Allemagne]

Source :

Free radical biology & medicine [ 1873-4596 ] ; 2019.

RBID : pubmed:30500420

Descripteurs français

English descriptors

KwdEn :
- Actin Depolymerizing Factors (genetics), Actin Depolymerizing Factors (metabolism), Actins (genetics), Actins (metabolism), Animals (MeSH), Cell Line (MeSH), Eukaryotic Initiation Factor-2 (genetics), Eukaryotic Initiation Factor-2 (metabolism), Fibroblasts (cytology), Fibroblasts (drug effects), Fibroblasts (metabolism), Filamins (genetics), Filamins (metabolism), Fructose-Bisphosphate Aldolase (genetics), Fructose-Bisphosphate Aldolase (metabolism), Garlic (chemistry), Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) (genetics), Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) (metabolism), HSP110 Heat-Shock Proteins (genetics), HSP110 Heat-Shock Proteins (metabolism), HSP90 Heat-Shock Proteins (genetics), HSP90 Heat-Shock Proteins (metabolism), Humans (MeSH), Jurkat Cells (MeSH), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Mice (MeSH), Microfilament Proteins (genetics), Microfilament Proteins (metabolism), Protein Processing, Post-Translational (MeSH), Proteome (genetics), Proteome (metabolism), Pyruvate Kinase (genetics), Pyruvate Kinase (metabolism), Sulfhydryl Compounds (metabolism), Sulfinic Acids (isolation & purification), Sulfinic Acids (pharmacology), Tubulin (genetics), Tubulin (metabolism), Zinc (metabolism).
MESH :
- chemical , genetics : Actin Depolymerizing Factors, Actins, Eukaryotic Initiation Factor-2, Filamins, Fructose-Bisphosphate Aldolase, Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating), HSP110 Heat-Shock Proteins, HSP90 Heat-Shock Proteins, Membrane Glycoproteins, Microfilament Proteins, Proteome, Pyruvate Kinase, Tubulin.
- chemical , isolation & purification : Sulfinic Acids.
- chemical , metabolism : Actin Depolymerizing Factors, Actins, Eukaryotic Initiation Factor-2, Filamins, Fructose-Bisphosphate Aldolase, Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating), HSP110 Heat-Shock Proteins, HSP90 Heat-Shock Proteins, Membrane Glycoproteins, Microfilament Proteins, Proteome, Pyruvate Kinase, Sulfhydryl Compounds, Tubulin, Zinc.
- chemistry : Garlic.
- cytology : Fibroblasts.
- drug effects : Fibroblasts.
- metabolism : Fibroblasts.
- chemical , pharmacology : Sulfinic Acids.
- Animals, Cell Line, Humans, Jurkat Cells, Mice, Protein Processing, Post-Translational.

Abstract

A single clove of edible garlic (Allium sativum L.) of about 10 g produces up to 5 mg of allicin (diallylthiosulfinate), a thiol-reactive sulfur-containing defence substance that gives injured garlic tissue its characteristic smell. Allicin induces apoptosis or necrosis in a dose-dependent manner but biocompatible doses influence cellular metabolism and signalling cascades. Oxidation of protein thiols and depletion of the glutathione pool are thought to be responsible for allicin's physiological effects. Here, we studied the effect of allicin on post-translational thiol-modification in human Jurkat T-cells using shotgun LC-MS/MS analyses. We identified 332 proteins that were modified by S-thioallylation in the Jurkat cell proteome which causes a mass shift of 72 Da on cysteines. Many S-thioallylated proteins are highly abundant proteins, including cytoskeletal proteins tubulin, actin, cofilin, filamin and plastin-2, the heat shock chaperones HSP90 and HSPA4, the glycolytic enzymes GAPDH, ALDOA, PKM as well the protein translation factor EEF2. Allicin disrupted the actin cytoskeleton in murine L929 fibroblasts. Allicin stimulated the immune response by causing Zn²⁺ release from proteins and increasing the Zn²⁺-dependent IL-1-triggered production of IL-2 in murine EL-4 T-cells. Furthermore, allicin caused inhibition of enolase activity, an enzyme considered a cancer therapy target. In conclusion, our study revealed the widespread extent of S-thioallylation in the human Jurkat cell proteome and showed effects of allicin exposure on essential cellular functions of selected targets, many of which are targets for cancer therapy.

DOI: 10.1016/j.freeradbiomed.2018.11.022
PubMed: 30500420
PubMed Central: PMC6342545

Affiliations:

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Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Actin Depolymerizing Factors (genetics)</term>
<term>Actin Depolymerizing Factors (metabolism)</term>
<term>Actins (genetics)</term>
<term>Actins (metabolism)</term>
<term>Animals (MeSH)</term>
<term>Cell Line (MeSH)</term>
<term>Eukaryotic Initiation Factor-2 (genetics)</term>
<term>Eukaryotic Initiation Factor-2 (metabolism)</term>
<term>Fibroblasts (cytology)</term>
<term>Fibroblasts (drug effects)</term>
<term>Fibroblasts (metabolism)</term>
<term>Filamins (genetics)</term>
<term>Filamins (metabolism)</term>
<term>Fructose-Bisphosphate Aldolase (genetics)</term>
<term>Fructose-Bisphosphate Aldolase (metabolism)</term>
<term>Garlic (chemistry)</term>
<term>Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) (genetics)</term>
<term>Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) (metabolism)</term>
<term>HSP110 Heat-Shock Proteins (genetics)</term>
<term>HSP110 Heat-Shock Proteins (metabolism)</term>
<term>HSP90 Heat-Shock Proteins (genetics)</term>
<term>HSP90 Heat-Shock Proteins (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Jurkat Cells (MeSH)</term>
<term>Membrane Glycoproteins (genetics)</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Mice (MeSH)</term>
<term>Microfilament Proteins (genetics)</term>
<term>Microfilament Proteins (metabolism)</term>
<term>Protein Processing, Post-Translational (MeSH)</term>
<term>Proteome (genetics)</term>
<term>Proteome (metabolism)</term>
<term>Pyruvate Kinase (genetics)</term>
<term>Pyruvate Kinase (metabolism)</term>
<term>Sulfhydryl Compounds (metabolism)</term>
<term>Sulfinic Acids (isolation & purification)</term>
<term>Sulfinic Acids (pharmacology)</term>
<term>Tubulin (genetics)</term>
<term>Tubulin (metabolism)</term>
<term>Zinc (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Acides sulfiniques (isolement et purification)</term>
<term>Acides sulfiniques (pharmacologie)</term>
<term>Actines (génétique)</term>
<term>Actines (métabolisme)</term>
<term>Ail (composition chimique)</term>
<term>Animaux (MeSH)</term>
<term>Cellules Jurkat (MeSH)</term>
<term>Facteur-2 d'initiation eucaryote (génétique)</term>
<term>Facteur-2 d'initiation eucaryote (métabolisme)</term>
<term>Facteurs de dépolymérisation de l'actine (génétique)</term>
<term>Facteurs de dépolymérisation de l'actine (métabolisme)</term>
<term>Fibroblastes (cytologie)</term>
<term>Fibroblastes (effets des médicaments et des substances chimiques)</term>
<term>Fibroblastes (métabolisme)</term>
<term>Filamines (génétique)</term>
<term>Filamines (métabolisme)</term>
<term>Fructose bisphosphate aldolase (génétique)</term>
<term>Fructose bisphosphate aldolase (métabolisme)</term>
<term>Glyceraldehyde 3-phosphate dehydrogenase (phosphorylating) (génétique)</term>
<term>Glyceraldehyde 3-phosphate dehydrogenase (phosphorylating) (métabolisme)</term>
<term>Glycoprotéines membranaires (génétique)</term>
<term>Glycoprotéines membranaires (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Lignée cellulaire (MeSH)</term>
<term>Maturation post-traductionnelle des protéines (MeSH)</term>
<term>Protéines des microfilaments (génétique)</term>
<term>Protéines des microfilaments (métabolisme)</term>
<term>Protéines du choc thermique HSP110 (génétique)</term>
<term>Protéines du choc thermique HSP110 (métabolisme)</term>
<term>Protéines du choc thermique HSP90 (génétique)</term>
<term>Protéines du choc thermique HSP90 (métabolisme)</term>
<term>Protéome (génétique)</term>
<term>Protéome (métabolisme)</term>
<term>Pyruvate kinase (génétique)</term>
<term>Pyruvate kinase (métabolisme)</term>
<term>Souris (MeSH)</term>
<term>Thiols (métabolisme)</term>
<term>Tubuline (génétique)</term>
<term>Tubuline (métabolisme)</term>
<term>Zinc (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Actin Depolymerizing Factors</term>
<term>Actins</term>
<term>Eukaryotic Initiation Factor-2</term>
<term>Filamins</term>
<term>Fructose-Bisphosphate Aldolase</term>
<term>Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)</term>
<term>HSP110 Heat-Shock Proteins</term>
<term>HSP90 Heat-Shock Proteins</term>
<term>Membrane Glycoproteins</term>
<term>Microfilament Proteins</term>
<term>Proteome</term>
<term>Pyruvate Kinase</term>
<term>Tubulin</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Sulfinic Acids</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Actin Depolymerizing Factors</term>
<term>Actins</term>
<term>Eukaryotic Initiation Factor-2</term>
<term>Filamins</term>
<term>Fructose-Bisphosphate Aldolase</term>
<term>Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)</term>
<term>HSP110 Heat-Shock Proteins</term>
<term>HSP90 Heat-Shock Proteins</term>
<term>Membrane Glycoproteins</term>
<term>Microfilament Proteins</term>
<term>Proteome</term>
<term>Pyruvate Kinase</term>
<term>Sulfhydryl Compounds</term>
<term>Tubulin</term>
<term>Zinc</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Garlic</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Ail</term>
</keywords>
<keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Fibroblastes</term>
</keywords>
<keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Fibroblasts</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Fibroblasts</term>
</keywords>
<keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Fibroblastes</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Actines</term>
<term>Facteur-2 d'initiation eucaryote</term>
<term>Facteurs de dépolymérisation de l'actine</term>
<term>Filamines</term>
<term>Fructose bisphosphate aldolase</term>
<term>Glyceraldehyde 3-phosphate dehydrogenase (phosphorylating)</term>
<term>Glycoprotéines membranaires</term>
<term>Protéines des microfilaments</term>
<term>Protéines du choc thermique HSP110</term>
<term>Protéines du choc thermique HSP90</term>
<term>Protéome</term>
<term>Pyruvate kinase</term>
<term>Tubuline</term>
</keywords>
<keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Acides sulfiniques</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Fibroblasts</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Actines</term>
<term>Facteur-2 d'initiation eucaryote</term>
<term>Facteurs de dépolymérisation de l'actine</term>
<term>Fibroblastes</term>
<term>Filamines</term>
<term>Fructose bisphosphate aldolase</term>
<term>Glyceraldehyde 3-phosphate dehydrogenase (phosphorylating)</term>
<term>Glycoprotéines membranaires</term>
<term>Protéines des microfilaments</term>
<term>Protéines du choc thermique HSP110</term>
<term>Protéines du choc thermique HSP90</term>
<term>Protéome</term>
<term>Pyruvate kinase</term>
<term>Thiols</term>
<term>Tubuline</term>
<term>Zinc</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Acides sulfiniques</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Sulfinic Acids</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Cell Line</term>
<term>Humans</term>
<term>Jurkat Cells</term>
<term>Mice</term>
<term>Protein Processing, Post-Translational</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Cellules Jurkat</term>
<term>Humains</term>
<term>Lignée cellulaire</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Souris</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">A single clove of edible garlic (Allium sativum L.) of about 10 g produces up to 5 mg of allicin (diallylthiosulfinate), a thiol-reactive sulfur-containing defence substance that gives injured garlic tissue its characteristic smell. Allicin induces apoptosis or necrosis in a dose-dependent manner but biocompatible doses influence cellular metabolism and signalling cascades. Oxidation of protein thiols and depletion of the glutathione pool are thought to be responsible for allicin's physiological effects. Here, we studied the effect of allicin on post-translational thiol-modification in human Jurkat T-cells using shotgun LC-MS/MS analyses. We identified 332 proteins that were modified by S-thioallylation in the Jurkat cell proteome which causes a mass shift of 72 Da on cysteines. Many S-thioallylated proteins are highly abundant proteins, including cytoskeletal proteins tubulin, actin, cofilin, filamin and plastin-2, the heat shock chaperones HSP90 and HSPA4, the glycolytic enzymes GAPDH, ALDOA, PKM as well the protein translation factor EEF2. Allicin disrupted the actin cytoskeleton in murine L929 fibroblasts. Allicin stimulated the immune response by causing Zn<sup>2+</sup>
 release from proteins and increasing the Zn<sup>2+</sup>
-dependent IL-1-triggered production of IL-2 in murine EL-4 T-cells. Furthermore, allicin caused inhibition of enolase activity, an enzyme considered a cancer therapy target. In conclusion, our study revealed the widespread extent of S-thioallylation in the human Jurkat cell proteome and showed effects of allicin exposure on essential cellular functions of selected targets, many of which are targets for cancer therapy.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30500420</PMID>
<DateCompleted><Year>2020</Year>
<Month>01</Month>
<Day>21</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>03</Month>
<Day>09</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-4596</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>131</Volume>
<PubDate><Year>2019</Year>
<Month>02</Month>
<Day>01</Day>
</PubDate>
</JournalIssue>
<Title>Free radical biology & medicine</Title>
<ISOAbbreviation>Free Radic Biol Med</ISOAbbreviation>
</Journal>
<ArticleTitle>The human allicin-proteome: S-thioallylation of proteins by the garlic defence substance allicin and its biological effects.</ArticleTitle>
<Pagination><MedlinePgn>144-153</MedlinePgn>
</Pagination>
<ELocationID EIdType="pii" ValidYN="Y">S0891-5849(18)31537-5</ELocationID>
<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.freeradbiomed.2018.11.022</ELocationID>
<Abstract><AbstractText>A single clove of edible garlic (Allium sativum L.) of about 10 g produces up to 5 mg of allicin (diallylthiosulfinate), a thiol-reactive sulfur-containing defence substance that gives injured garlic tissue its characteristic smell. Allicin induces apoptosis or necrosis in a dose-dependent manner but biocompatible doses influence cellular metabolism and signalling cascades. Oxidation of protein thiols and depletion of the glutathione pool are thought to be responsible for allicin's physiological effects. Here, we studied the effect of allicin on post-translational thiol-modification in human Jurkat T-cells using shotgun LC-MS/MS analyses. We identified 332 proteins that were modified by S-thioallylation in the Jurkat cell proteome which causes a mass shift of 72 Da on cysteines. Many S-thioallylated proteins are highly abundant proteins, including cytoskeletal proteins tubulin, actin, cofilin, filamin and plastin-2, the heat shock chaperones HSP90 and HSPA4, the glycolytic enzymes GAPDH, ALDOA, PKM as well the protein translation factor EEF2. Allicin disrupted the actin cytoskeleton in murine L929 fibroblasts. Allicin stimulated the immune response by causing Zn<sup>2+</sup>
 release from proteins and increasing the Zn<sup>2+</sup>
-dependent IL-1-triggered production of IL-2 in murine EL-4 T-cells. Furthermore, allicin caused inhibition of enolase activity, an enzyme considered a cancer therapy target. In conclusion, our study revealed the widespread extent of S-thioallylation in the human Jurkat cell proteome and showed effects of allicin exposure on essential cellular functions of selected targets, many of which are targets for cancer therapy.</AbstractText>
<CopyrightInformation>Copyright © 2018 The Authors. Published by Elsevier Inc. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gruhlke</LastName>
<ForeName>Martin C H</ForeName>
<Initials>MCH</Initials>
<AffiliationInfo><Affiliation>Department of Plant Physiology, RWTH Aachen University, Worringer Weg 1, D-52056 Aachen, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Antelmann</LastName>
<ForeName>Haike</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>Freie Universität Berlin, Institute of Biology-Microbiology, Königin-Luise-Str. 12-16, D-14195 Berlin, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Bernhardt</LastName>
<ForeName>Jörg</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Institute of Microbiology, University of Greifswald, Felix-Hausdorff-Straße 8, D-17489 Greifswald, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kloubert</LastName>
<ForeName>Veronika</ForeName>
<Initials>V</Initials>
<AffiliationInfo><Affiliation>Institute of Immunology, RWTH Aachen University Hospital, Pauwelsstraße 30, D-52074 Aachen, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Rink</LastName>
<ForeName>Lothar</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>Institute of Immunology, RWTH Aachen University Hospital, Pauwelsstraße 30, D-52074 Aachen, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Slusarenko</LastName>
<ForeName>Alan J</ForeName>
<Initials>AJ</Initials>
<AffiliationInfo><Affiliation>Department of Plant Physiology, RWTH Aachen University, Worringer Weg 1, D-52056 Aachen, Germany.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2018</Year>
<Month>11</Month>
<Day>27</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Free Radic Biol Med</MedlineTA>
<NlmUniqueID>8709159</NlmUniqueID>
<ISSNLinking>0891-5849</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D051339">Actin Depolymerizing Factors</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000199">Actins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D015852">Eukaryotic Initiation Factor-2</NameOfSubstance>
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<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D064448">Filamins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D050957">HSP110 Heat-Shock Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D018841">HSP90 Heat-Shock Proteins</NameOfSubstance>
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<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C121993">HSPA4 protein, human</NameOfSubstance>
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<NameOfSubstance UI="D008562">Membrane Glycoproteins</NameOfSubstance>
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<Chemical><RegistryNumber>0</RegistryNumber>
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<NameOfSubstance UI="D011770">Pyruvate Kinase</NameOfSubstance>
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<Chemical><RegistryNumber>EC 4.1.2.13</RegistryNumber>
<NameOfSubstance UI="D005634">Fructose-Bisphosphate Aldolase</NameOfSubstance>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D051339" MajorTopicYN="N">Actin Depolymerizing Factors</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000199" MajorTopicYN="N">Actins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015852" MajorTopicYN="N">Eukaryotic Initiation Factor-2</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005347" MajorTopicYN="N">Fibroblasts</DescriptorName>
<QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D064448" MajorTopicYN="N">Filamins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005634" MajorTopicYN="N">Fructose-Bisphosphate Aldolase</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005737" MajorTopicYN="N">Garlic</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D024581" MajorTopicYN="N">Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D050957" MajorTopicYN="N">HSP110 Heat-Shock Proteins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018841" MajorTopicYN="N">HSP90 Heat-Shock Proteins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D019169" MajorTopicYN="N">Jurkat Cells</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008840" MajorTopicYN="N">Microfilament Proteins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011499" MajorTopicYN="Y">Protein Processing, Post-Translational</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020543" MajorTopicYN="N">Proteome</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011770" MajorTopicYN="N">Pyruvate Kinase</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013441" MajorTopicYN="N">Sulfinic Acids</DescriptorName>
<QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName>
<QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014404" MajorTopicYN="N">Tubulin</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015032" MajorTopicYN="N">Zinc</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Actin</Keyword>
<Keyword MajorTopicYN="Y">Allicin</Keyword>
<Keyword MajorTopicYN="Y">Cysteine</Keyword>
<Keyword MajorTopicYN="Y">Cytoskeleton</Keyword>
<Keyword MajorTopicYN="Y">Enolase</Keyword>
<Keyword MajorTopicYN="Y">Fibroblasts</Keyword>
<Keyword MajorTopicYN="Y">Glycolysis</Keyword>
<Keyword MajorTopicYN="Y">IL-2</Keyword>
<Keyword MajorTopicYN="Y">Interleukin IL-1</Keyword>
<Keyword MajorTopicYN="Y">Jurkat</Keyword>
<Keyword MajorTopicYN="Y">Protein modification</Keyword>
<Keyword MajorTopicYN="Y">S-thioallylation</Keyword>
<Keyword MajorTopicYN="Y">T-cells</Keyword>
<Keyword MajorTopicYN="Y">Warburg effect</Keyword>
<Keyword MajorTopicYN="Y">Zinc</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year>
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The human allicin-proteome: S-thioallylation of proteins by the garlic defence substance allicin and its biological effects.

The human allicin-proteome: S-thioallylation of proteins by the garlic defence substance allicin and its biological effects.

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