The Solution Structure and Dynamics of Full-length Human Cerebral Dopamine Neurotrophic Factor and Its Neuroprotective Role against α-Synuclein Oligomers.
Identifieur interne : 000311 ( PubMed/Corpus ); précédent : 000310; suivant : 000312The Solution Structure and Dynamics of Full-length Human Cerebral Dopamine Neurotrophic Factor and Its Neuroprotective Role against α-Synuclein Oligomers.
Auteurs : Cristiane Latge ; Katia M S. Cabral ; Guilherme A P. De Oliveira ; Diana P. Raymundo ; Julia A. Freitas ; Laizes Johanson ; Luciana F. Romão ; Fernando L. Palhano ; Torsten Herrmann ; Marcius S. Almeida ; Debora FoguelSource :
- The Journal of biological chemistry [ 1083-351X ] ; 2015.
English descriptors
- KwdEn :
- Animals, Biopolymers (metabolism), Cell Line, Crystallography, X-Ray, Humans, Mice, Nerve Growth Factors (chemistry), Nerve Growth Factors (physiology), Neuroprotective Agents, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, Structure-Activity Relationship, alpha-Synuclein (metabolism).
- MESH :
- chemical , chemistry : Nerve Growth Factors.
- chemical , metabolism : Biopolymers, alpha-Synuclein.
- chemical , physiology : Nerve Growth Factors.
- Animals, Cell Line, Crystallography, X-Ray, Humans, Mice, Neuroprotective Agents, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, Structure-Activity Relationship.
Abstract
Cerebral dopamine neurotrophic factor (CDNF) is a promising therapeutic agent for Parkinson disease. As such, there has been great interest in studying its mode of action, which remains unknown. The three-dimensional crystal structure of the N terminus (residues 9-107) of CDNF has been determined, but there have been no published structural studies on the full-length protein due to proteolysis of its C-terminal domain, which is considered intrinsically disordered. An improved purification protocol enabled us to obtain active full-length CDNF and to determine its three-dimensional structure in solution. CDNF contains two well folded domains (residues 10-100 and 111-157) that are linked by a loop of intermediate flexibility. We identified two surface patches on the N-terminal domain that were characterized by increased conformational dynamics that should allow them to embrace active sites. One of these patches is formed by residues Ser-33, Leu-34, Ala-66, Lys-68, Ile-69, Leu-70, Ser-71, and Glu-72. The other includes a flexibly disordered N-terminal tail (residues 1-9), followed by the N-terminal portion of α-helix 1 (residues Cys-11, Glu-12, Val-13, Lys-15, and Glu-16) and residue Glu-88. The surface of the C-terminal domain contains two conserved active sites, which have previously been identified in mesencephalic astrocyte-derived neurotrophic factor, a CDNF paralog, which corresponds to its intracellular mode of action. We also showed that CDNF was able to protect dopaminergic neurons against injury caused by α-synuclein oligomers. This advises its use against physiological damages caused by α-synuclein oligomers, as observed in Parkinson disease and several other neurodegenerative diseases.
DOI: 10.1074/jbc.M115.662254
PubMed: 26149686
Links to Exploration step
pubmed:26149686Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The Solution Structure and Dynamics of Full-length Human Cerebral Dopamine Neurotrophic Factor and Its Neuroprotective Role against α-Synuclein Oligomers.</title><author><name sortKey="Latge, Cristiane" sort="Latge, Cristiane" uniqKey="Latge C" first="Cristiane" last="Latge">Cristiane Latge</name><affiliation><nlm:affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Cabral, Katia M S" sort="Cabral, Katia M S" uniqKey="Cabral K" first="Katia M S" last="Cabral">Katia M S. Cabral</name><affiliation><nlm:affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="De Oliveira, Guilherme A P" sort="De Oliveira, Guilherme A P" uniqKey="De Oliveira G" first="Guilherme A P" last="De Oliveira">Guilherme A P. De Oliveira</name><affiliation><nlm:affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Raymundo, Diana P" sort="Raymundo, Diana P" uniqKey="Raymundo D" first="Diana P" last="Raymundo">Diana P. 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Palhano</name><affiliation><nlm:affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Herrmann, Torsten" sort="Herrmann, Torsten" uniqKey="Herrmann T" first="Torsten" last="Herrmann">Torsten Herrmann</name><affiliation><nlm:affiliation>the Institut des Sciences Analytiques, UMR 5280 CNRS, 5 rue de la Doua, 69100 Villeurbanne, France, and.</nlm:affiliation></affiliation></author><author><name sortKey="Almeida, Marcius S" sort="Almeida, Marcius S" uniqKey="Almeida M" first="Marcius S" last="Almeida">Marcius S. Almeida</name><affiliation><nlm:affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil, the Centro Nacional de Biologia Estrutural e Bioimagem (CENABIO), Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Foguel, Debora" sort="Foguel, Debora" uniqKey="Foguel D" first="Debora" last="Foguel">Debora Foguel</name><affiliation><nlm:affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil, foguel@bioqmed.ufrj.br.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:26149686</idno><idno type="pmid">26149686</idno><idno type="doi">10.1074/jbc.M115.662254</idno><idno type="wicri:Area/PubMed/Corpus">000311</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000311</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The Solution Structure and Dynamics of Full-length Human Cerebral Dopamine Neurotrophic Factor and Its Neuroprotective Role against α-Synuclein Oligomers.</title><author><name sortKey="Latge, Cristiane" sort="Latge, Cristiane" uniqKey="Latge C" first="Cristiane" last="Latge">Cristiane Latge</name><affiliation><nlm:affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Cabral, Katia M S" sort="Cabral, Katia M S" uniqKey="Cabral K" first="Katia M S" last="Cabral">Katia M S. Cabral</name><affiliation><nlm:affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="De Oliveira, Guilherme A P" sort="De Oliveira, Guilherme A P" uniqKey="De Oliveira G" first="Guilherme A P" last="De Oliveira">Guilherme A P. De Oliveira</name><affiliation><nlm:affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Raymundo, Diana P" sort="Raymundo, Diana P" uniqKey="Raymundo D" first="Diana P" last="Raymundo">Diana P. Raymundo</name><affiliation><nlm:affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Freitas, Julia A" sort="Freitas, Julia A" uniqKey="Freitas J" first="Julia A" last="Freitas">Julia A. Freitas</name><affiliation><nlm:affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Johanson, Laizes" sort="Johanson, Laizes" uniqKey="Johanson L" first="Laizes" last="Johanson">Laizes Johanson</name><affiliation><nlm:affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Romao, Luciana F" sort="Romao, Luciana F" uniqKey="Romao L" first="Luciana F" last="Romão">Luciana F. Romão</name><affiliation><nlm:affiliation>the UFRJ/Pólo Xerém, Universidade Federal do Rio de Janeiro 25245-390, Rio de Janeiro, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Palhano, Fernando L" sort="Palhano, Fernando L" uniqKey="Palhano F" first="Fernando L" last="Palhano">Fernando L. Palhano</name><affiliation><nlm:affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Herrmann, Torsten" sort="Herrmann, Torsten" uniqKey="Herrmann T" first="Torsten" last="Herrmann">Torsten Herrmann</name><affiliation><nlm:affiliation>the Institut des Sciences Analytiques, UMR 5280 CNRS, 5 rue de la Doua, 69100 Villeurbanne, France, and.</nlm:affiliation></affiliation></author><author><name sortKey="Almeida, Marcius S" sort="Almeida, Marcius S" uniqKey="Almeida M" first="Marcius S" last="Almeida">Marcius S. Almeida</name><affiliation><nlm:affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil, the Centro Nacional de Biologia Estrutural e Bioimagem (CENABIO), Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Foguel, Debora" sort="Foguel, Debora" uniqKey="Foguel D" first="Debora" last="Foguel">Debora Foguel</name><affiliation><nlm:affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil, foguel@bioqmed.ufrj.br.</nlm:affiliation></affiliation></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="eISSN">1083-351X</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Biopolymers (metabolism)</term><term>Cell Line</term><term>Crystallography, X-Ray</term><term>Humans</term><term>Mice</term><term>Nerve Growth Factors (chemistry)</term><term>Nerve Growth Factors (physiology)</term><term>Neuroprotective Agents</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Protein Conformation</term><term>Structure-Activity Relationship</term><term>alpha-Synuclein (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nerve Growth Factors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Biopolymers</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Nerve Growth Factors</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Crystallography, X-Ray</term><term>Humans</term><term>Mice</term><term>Neuroprotective Agents</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Protein Conformation</term><term>Structure-Activity Relationship</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Cerebral dopamine neurotrophic factor (CDNF) is a promising therapeutic agent for Parkinson disease. As such, there has been great interest in studying its mode of action, which remains unknown. The three-dimensional crystal structure of the N terminus (residues 9-107) of CDNF has been determined, but there have been no published structural studies on the full-length protein due to proteolysis of its C-terminal domain, which is considered intrinsically disordered. An improved purification protocol enabled us to obtain active full-length CDNF and to determine its three-dimensional structure in solution. CDNF contains two well folded domains (residues 10-100 and 111-157) that are linked by a loop of intermediate flexibility. We identified two surface patches on the N-terminal domain that were characterized by increased conformational dynamics that should allow them to embrace active sites. One of these patches is formed by residues Ser-33, Leu-34, Ala-66, Lys-68, Ile-69, Leu-70, Ser-71, and Glu-72. The other includes a flexibly disordered N-terminal tail (residues 1-9), followed by the N-terminal portion of α-helix 1 (residues Cys-11, Glu-12, Val-13, Lys-15, and Glu-16) and residue Glu-88. The surface of the C-terminal domain contains two conserved active sites, which have previously been identified in mesencephalic astrocyte-derived neurotrophic factor, a CDNF paralog, which corresponds to its intracellular mode of action. We also showed that CDNF was able to protect dopaminergic neurons against injury caused by α-synuclein oligomers. This advises its use against physiological damages caused by α-synuclein oligomers, as observed in Parkinson disease and several other neurodegenerative diseases.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26149686</PMID><DateCreated><Year>2015</Year><Month>08</Month><Day>15</Day></DateCreated><DateCompleted><Year>2015</Year><Month>12</Month><Day>08</Day></DateCompleted><DateRevised><Year>2016</Year><Month>08</Month><Day>14</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>290</Volume><Issue>33</Issue><PubDate><Year>2015</Year><Month>Aug</Month><Day>14</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation></Journal><ArticleTitle>The Solution Structure and Dynamics of Full-length Human Cerebral Dopamine Neurotrophic Factor and Its Neuroprotective Role against α-Synuclein Oligomers.</ArticleTitle><Pagination><MedlinePgn>20527-40</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M115.662254</ELocationID><Abstract><AbstractText>Cerebral dopamine neurotrophic factor (CDNF) is a promising therapeutic agent for Parkinson disease. As such, there has been great interest in studying its mode of action, which remains unknown. The three-dimensional crystal structure of the N terminus (residues 9-107) of CDNF has been determined, but there have been no published structural studies on the full-length protein due to proteolysis of its C-terminal domain, which is considered intrinsically disordered. An improved purification protocol enabled us to obtain active full-length CDNF and to determine its three-dimensional structure in solution. CDNF contains two well folded domains (residues 10-100 and 111-157) that are linked by a loop of intermediate flexibility. We identified two surface patches on the N-terminal domain that were characterized by increased conformational dynamics that should allow them to embrace active sites. One of these patches is formed by residues Ser-33, Leu-34, Ala-66, Lys-68, Ile-69, Leu-70, Ser-71, and Glu-72. The other includes a flexibly disordered N-terminal tail (residues 1-9), followed by the N-terminal portion of α-helix 1 (residues Cys-11, Glu-12, Val-13, Lys-15, and Glu-16) and residue Glu-88. The surface of the C-terminal domain contains two conserved active sites, which have previously been identified in mesencephalic astrocyte-derived neurotrophic factor, a CDNF paralog, which corresponds to its intracellular mode of action. We also showed that CDNF was able to protect dopaminergic neurons against injury caused by α-synuclein oligomers. This advises its use against physiological damages caused by α-synuclein oligomers, as observed in Parkinson disease and several other neurodegenerative diseases.</AbstractText><CopyrightInformation>© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Latge</LastName><ForeName>Cristiane</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cabral</LastName><ForeName>Katia M S</ForeName><Initials>KM</Initials><AffiliationInfo><Affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>de Oliveira</LastName><ForeName>Guilherme A P</ForeName><Initials>GA</Initials><AffiliationInfo><Affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Raymundo</LastName><ForeName>Diana P</ForeName><Initials>DP</Initials><AffiliationInfo><Affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Freitas</LastName><ForeName>Julia A</ForeName><Initials>JA</Initials><AffiliationInfo><Affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Johanson</LastName><ForeName>Laizes</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Romão</LastName><ForeName>Luciana F</ForeName><Initials>LF</Initials><AffiliationInfo><Affiliation>the UFRJ/Pólo Xerém, Universidade Federal do Rio de Janeiro 25245-390, Rio de Janeiro, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Palhano</LastName><ForeName>Fernando L</ForeName><Initials>FL</Initials><AffiliationInfo><Affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Herrmann</LastName><ForeName>Torsten</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>the Institut des Sciences Analytiques, UMR 5280 CNRS, 5 rue de la Doua, 69100 Villeurbanne, France, and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Almeida</LastName><ForeName>Marcius S</ForeName><Initials>MS</Initials><AffiliationInfo><Affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil, the Centro Nacional de Biologia Estrutural e Bioimagem (CENABIO), Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Foguel</LastName><ForeName>Debora</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>From the Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil, foguel@bioqmed.ufrj.br.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><DataBankList 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protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009414">Nerve Growth Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018696">Neuroprotective Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051844">alpha-Synuclein</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Protein Sci. 1993 Mar;2(3):404-10</RefSource><PMID Version="1">8453378</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2003 Jul 4;278(27):25009-13</RefSource><PMID Version="1">12719433</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Methods Enzymol. 1994;239:563-96</RefSource><PMID Version="1">7830599</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Cell Sci. 1995 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disease</Keyword><Keyword MajorTopicYN="N">neurodegeneration</Keyword><Keyword MajorTopicYN="N">neurotrophic factor</Keyword><Keyword MajorTopicYN="N">protein dynamic</Keyword><Keyword MajorTopicYN="N">protein structure</Keyword><Keyword MajorTopicYN="N">α-synuclein (a-synuclein)</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>05</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>7</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>7</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>12</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26149686</ArticleId><ArticleId 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