The Myeloablative Drug Busulfan Converts Cysteine to Dehydroalanine and Lanthionine in Redoxins.
Identifieur interne : 000408 ( Main/Exploration ); précédent : 000407; suivant : 000409The Myeloablative Drug Busulfan Converts Cysteine to Dehydroalanine and Lanthionine in Redoxins.
Auteurs : Michele Scian [États-Unis] ; Miklos Guttman [États-Unis] ; Samantha D. Bouldin [États-Unis] ; Caryn E. Outten [États-Unis] ; William M. Atkins [États-Unis]Source :
- Biochemistry [ 1520-4995 ] ; 2016.
Descripteurs français
- KwdFr :
- MESH :
- analogues et dérivés : Alanine.
- composition chimique : Agonistes myélo-ablatifs, Alanine, Busulfan, Cystéine, Sulfures.
- Humains, Spectrométrie de masse en tandem.
English descriptors
- KwdEn :
- MESH :
- chemical , analogs & derivatives : Alanine.
- chemical , chemistry : Alanine, Busulfan, Cysteine, Myeloablative Agonists, Sulfides.
- Humans, Tandem Mass Spectrometry.
Abstract
The myeloablative agent busulfan (1,4-butanediol dimethanesulfonate) is an old drug that is used routinely to eliminate cancerous bone marrow prior to hematopoietic stem cell transplant. The myeloablative activity and systemic toxicity of busulfan have been ascribed to its ability to cross-link DNA. In contrast, here we demonstrate that incubation of busulfan with the thiol redox proteins glutaredoxin or thioredoxin at pH 7.4 and 37 °C results in the formation of putative S-tetrahydrothiophenium adducts at their catalytic Cys residues, followed by β-elimination to yield dehydroalanine. Both proteins contain a second Cys, in their catalytic C-X-X-C motif, which reacts with the dehydroalanine, the initial Cys adduct with busulfan, or the S-tetrahydrothiophenium, to form novel intramolecular cross-links. The reactivity of the dehydroalanine (DHA) formed is further demonstrated by adduction with glutathione to yield a lanthionine and by a novel reaction with the reducing agent tris(2-carboxyethyl)phosphine (TCEP), which yields a phosphine adduct via Michael addition to the DHA. Formation of a second quaternary organophosphonium salt via nucleophilic substitution with TCEP on the initial busulfan-protein adduct or on the THT(+)-Redoxin species is also observed. These results reveal a rich potential for reactions of busulfan with proteins in vitro, and likely in vivo. It is striking that several of the chemically altered protein products retain none of the atoms of busulfan, in contrast to typical drug-protein adducts or traditional protein modification reagents. In particular, the ability of a clinically used drug to convert Cys to dehydrolanine in intact proteins, and its subsequent reaction with biological thiols, is unprecedented.
DOI: 10.1021/acs.biochem.6b00622
PubMed: 27490699
PubMed Central: PMC5466068
Affiliations:
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Bouldin</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry and Biochemistry, University of South Carolina , Columbia, South Carolina 29208, United States.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry and Biochemistry, University of South Carolina , Columbia, South Carolina 29208</wicri:regionArea><wicri:noRegion>South Carolina 29208</wicri:noRegion></affiliation></author><author><name sortKey="Outten, Caryn E" sort="Outten, Caryn E" uniqKey="Outten C" first="Caryn E" last="Outten">Caryn E. Outten</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry and Biochemistry, University of South Carolina , Columbia, South Carolina 29208, United States.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry and Biochemistry, University of South Carolina , Columbia, South Carolina 29208</wicri:regionArea><wicri:noRegion>South Carolina 29208</wicri:noRegion></affiliation></author><author><name sortKey="Atkins, William M" sort="Atkins, William M" uniqKey="Atkins W" first="William M" last="Atkins">William M. Atkins</name><affiliation wicri:level="1"><nlm:affiliation>Department of Medicinal Chemistry, University of Washington , Box 357610, Seattle, Washington 98195-7610, United States.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Medicinal Chemistry, University of Washington , Box 357610, Seattle, Washington 98195-7610</wicri:regionArea><wicri:noRegion>Washington 98195-7610</wicri:noRegion></affiliation></author></analytic><series><title level="j">Biochemistry</title><idno type="eISSN">1520-4995</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alanine (analogs & derivatives)</term><term>Alanine (chemistry)</term><term>Busulfan (chemistry)</term><term>Cysteine (chemistry)</term><term>Humans (MeSH)</term><term>Myeloablative Agonists (chemistry)</term><term>Sulfides (chemistry)</term><term>Tandem Mass Spectrometry (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Agonistes myélo-ablatifs (composition chimique)</term><term>Alanine (analogues et dérivés)</term><term>Alanine (composition chimique)</term><term>Busulfan (composition chimique)</term><term>Cystéine (composition chimique)</term><term>Humains (MeSH)</term><term>Spectrométrie de masse en tandem (MeSH)</term><term>Sulfures (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Alanine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Alanine</term><term>Busulfan</term><term>Cysteine</term><term>Myeloablative Agonists</term><term>Sulfides</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Alanine</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Agonistes myélo-ablatifs</term><term>Alanine</term><term>Busulfan</term><term>Cystéine</term><term>Sulfures</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Tandem Mass Spectrometry</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Spectrométrie de masse en tandem</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The myeloablative agent busulfan (1,4-butanediol dimethanesulfonate) is an old drug that is used routinely to eliminate cancerous bone marrow prior to hematopoietic stem cell transplant. The myeloablative activity and systemic toxicity of busulfan have been ascribed to its ability to cross-link DNA. In contrast, here we demonstrate that incubation of busulfan with the thiol redox proteins glutaredoxin or thioredoxin at pH 7.4 and 37 °C results in the formation of putative S-tetrahydrothiophenium adducts at their catalytic Cys residues, followed by β-elimination to yield dehydroalanine. Both proteins contain a second Cys, in their catalytic C-X-X-C motif, which reacts with the dehydroalanine, the initial Cys adduct with busulfan, or the S-tetrahydrothiophenium, to form novel intramolecular cross-links. The reactivity of the dehydroalanine (DHA) formed is further demonstrated by adduction with glutathione to yield a lanthionine and by a novel reaction with the reducing agent tris(2-carboxyethyl)phosphine (TCEP), which yields a phosphine adduct via Michael addition to the DHA. Formation of a second quaternary organophosphonium salt via nucleophilic substitution with TCEP on the initial busulfan-protein adduct or on the THT(+)-Redoxin species is also observed. These results reveal a rich potential for reactions of busulfan with proteins in vitro, and likely in vivo. It is striking that several of the chemically altered protein products retain none of the atoms of busulfan, in contrast to typical drug-protein adducts or traditional protein modification reagents. In particular, the ability of a clinically used drug to convert Cys to dehydrolanine in intact proteins, and its subsequent reaction with biological thiols, is unprecedented.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27490699</PMID><DateCompleted><Year>2017</Year><Month>05</Month><Day>01</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-4995</ISSN><JournalIssue CitedMedium="Internet"><Volume>55</Volume><Issue>33</Issue><PubDate><Year>2016</Year><Month>08</Month><Day>23</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>The Myeloablative Drug Busulfan Converts Cysteine to Dehydroalanine and Lanthionine in Redoxins.</ArticleTitle><Pagination><MedlinePgn>4720-30</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/acs.biochem.6b00622</ELocationID><Abstract><AbstractText>The myeloablative agent busulfan (1,4-butanediol dimethanesulfonate) is an old drug that is used routinely to eliminate cancerous bone marrow prior to hematopoietic stem cell transplant. The myeloablative activity and systemic toxicity of busulfan have been ascribed to its ability to cross-link DNA. In contrast, here we demonstrate that incubation of busulfan with the thiol redox proteins glutaredoxin or thioredoxin at pH 7.4 and 37 °C results in the formation of putative S-tetrahydrothiophenium adducts at their catalytic Cys residues, followed by β-elimination to yield dehydroalanine. Both proteins contain a second Cys, in their catalytic C-X-X-C motif, which reacts with the dehydroalanine, the initial Cys adduct with busulfan, or the S-tetrahydrothiophenium, to form novel intramolecular cross-links. The reactivity of the dehydroalanine (DHA) formed is further demonstrated by adduction with glutathione to yield a lanthionine and by a novel reaction with the reducing agent tris(2-carboxyethyl)phosphine (TCEP), which yields a phosphine adduct via Michael addition to the DHA. Formation of a second quaternary organophosphonium salt via nucleophilic substitution with TCEP on the initial busulfan-protein adduct or on the THT(+)-Redoxin species is also observed. These results reveal a rich potential for reactions of busulfan with proteins in vitro, and likely in vivo. It is striking that several of the chemically altered protein products retain none of the atoms of busulfan, in contrast to typical drug-protein adducts or traditional protein modification reagents. In particular, the ability of a clinically used drug to convert Cys to dehydrolanine in intact proteins, and its subsequent reaction with biological thiols, is unprecedented.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Scian</LastName><ForeName>Michele</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Medicinal Chemistry, University of Washington , Box 357610, Seattle, Washington 98195-7610, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Guttman</LastName><ForeName>Miklos</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Medicinal Chemistry, University of Washington , Box 357610, Seattle, Washington 98195-7610, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bouldin</LastName><ForeName>Samantha D</ForeName><Initials>SD</Initials><AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry, University of South Carolina , Columbia, South Carolina 29208, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Outten</LastName><ForeName>Caryn E</ForeName><Initials>CE</Initials><AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry, University of South Carolina , Columbia, South Carolina 29208, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Atkins</LastName><ForeName>William M</ForeName><Initials>WM</Initials><AffiliationInfo><Affiliation>Department of Medicinal Chemistry, University of Washington , Box 357610, Seattle, Washington 98195-7610, United States.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 CA182963</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 GM086619</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R35 GM118164</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>08</Month><Day>11</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019653">Myeloablative Agonists</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013440">Sulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>98RA387EKY</RegistryNumber><NameOfSubstance UI="C015102">dehydroalanine</NameOfSubstance></Chemical><Chemical><RegistryNumber>G1LN9045DK</RegistryNumber><NameOfSubstance UI="D002066">Busulfan</NameOfSubstance></Chemical><Chemical><RegistryNumber>JO78O46X3K</RegistryNumber><NameOfSubstance UI="C001520">lanthionine</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical><Chemical><RegistryNumber>OF5P57N2ZX</RegistryNumber><NameOfSubstance UI="D000409">Alanine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000409" MajorTopicYN="N">Alanine</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002066" MajorTopicYN="N">Busulfan</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019653" MajorTopicYN="N">Myeloablative Agonists</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013440" MajorTopicYN="N">Sulfides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053719" MajorTopicYN="N">Tandem Mass Spectrometry</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>8</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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Atkins</name><name sortKey="Bouldin, Samantha D" sort="Bouldin, Samantha D" uniqKey="Bouldin S" first="Samantha D" last="Bouldin">Samantha D. Bouldin</name><name sortKey="Guttman, Miklos" sort="Guttman, Miklos" uniqKey="Guttman M" first="Miklos" last="Guttman">Miklos Guttman</name><name sortKey="Outten, Caryn E" sort="Outten, Caryn E" uniqKey="Outten C" first="Caryn E" last="Outten">Caryn E. Outten</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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