Iron-mediated aggregation and a localized structural change characterize ferritin from a mutant light chain polypeptide that causes neurodegeneration.
Identifieur interne : 001F81 ( PubMed/Checkpoint ); précédent : 001F80; suivant : 001F82Iron-mediated aggregation and a localized structural change characterize ferritin from a mutant light chain polypeptide that causes neurodegeneration.
Auteurs : Martin A. Baraibar [États-Unis] ; Ana G. Barbeito ; Barry B. Muhoberac ; Ruben VidalSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2008.
Descripteurs français
- KwdFr :
- Animaux, Cellules cultivées, Dichroïsme circulaire, Dégénérescence nerveuse (anatomopathologie), Dégénérescence nerveuse (génétique), Dégénérescence nerveuse (métabolisme), Dénaturation des protéines, Fer (métabolisme), Ferritines (), Ferritines (génétique), Ferritines (métabolisme), Ferritines (ultrastructure), Humains, Liaison aux protéines, Microscopie électronique à transmission, Mutation (génétique), Peptides (), Peptides (génétique), Peptides (métabolisme), Souris, Température.
- MESH :
- anatomopathologie : Dégénérescence nerveuse.
- génétique : Dégénérescence nerveuse, Ferritines, Mutation, Peptides.
- métabolisme : Dégénérescence nerveuse, Fer, Ferritines, Peptides.
- ultrastructure : Ferritines.
- Animaux, Cellules cultivées, Dichroïsme circulaire, Dénaturation des protéines, Ferritines, Humains, Liaison aux protéines, Microscopie électronique à transmission, Peptides, Souris, Température.
English descriptors
- KwdEn :
- Animals, Cells, Cultured, Circular Dichroism, Ferritins (chemistry), Ferritins (genetics), Ferritins (metabolism), Ferritins (ultrastructure), Humans, Iron (metabolism), Mice, Microscopy, Electron, Transmission, Mutation (genetics), Nerve Degeneration (genetics), Nerve Degeneration (metabolism), Nerve Degeneration (pathology), Peptides (chemistry), Peptides (genetics), Peptides (metabolism), Protein Binding, Protein Denaturation, Temperature.
- MESH :
- chemical , chemistry : Ferritins, Peptides.
- chemical , genetics : Ferritins, Peptides.
- chemical , metabolism : Ferritins, Iron, Peptides.
- chemical , ultrastructure : Ferritins.
- genetics : Mutation, Nerve Degeneration.
- metabolism : Nerve Degeneration.
- pathology : Nerve Degeneration.
- Animals, Cells, Cultured, Circular Dichroism, Humans, Mice, Microscopy, Electron, Transmission, Protein Binding, Protein Denaturation, Temperature.
Abstract
Nucleotide insertions in the ferritin light chain (FTL) polypeptide gene cause hereditary ferritinopathy, a neurodegenerative disease characterized by abnormal accumulation of ferritin and iron in the central nervous system. Here we describe for the first time the protein structure and iron storage function of the FTL mutant p.Phe167SerfsX26 (MT-FTL), which has a C terminus altered in sequence and extended in length. MT-FTL polypeptides assembled spontaneously into soluble, spherical 24-mers that were ultrastructurally indistinguishable from those of the wild type. Far-UV CD showed a decrease in alpha-helical content, and 8-anilino-1-naphthalenesulfonate fluorescence revealed the appearance of hydrophobic binding sites. Near-UV CD and proteolysis studies suggested little or no structural alteration outside of the C-terminal region. In contrast to wild type, MT-FTL homopolymers precipitated at much lower iron loading, had a diminished capacity to incorporate iron, and were less thermostable. However, precipitation was significantly reversed by addition of iron chelators both in vitro and in vivo. Our results reveal substantial protein conformational changes localized at the 4-fold pore of MT-FTL homopolymers and imply that the C terminus of the MT-FTL polypeptide plays an important role in ferritin solubility, stability, and iron management. We propose that the protrusion of some portion of the C terminus above the spherical shell allows it to cross-link with other mutant polypeptides through iron bridging, leading to enhanced mutant precipitation by iron. Our data suggest that hereditary ferritinopathy pathogenesis is likely to result from a combination of reduction in iron storage function and enhanced toxicity associated with iron-induced ferritin aggregates.
DOI: 10.1074/jbc.M805532200
PubMed: 18755684
Affiliations:
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Muhoberac</name></author><author><name sortKey="Vidal, Ruben" sort="Vidal, Ruben" uniqKey="Vidal R" first="Ruben" last="Vidal">Ruben Vidal</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Cells, Cultured</term><term>Circular Dichroism</term><term>Ferritins (chemistry)</term><term>Ferritins (genetics)</term><term>Ferritins (metabolism)</term><term>Ferritins (ultrastructure)</term><term>Humans</term><term>Iron (metabolism)</term><term>Mice</term><term>Microscopy, Electron, Transmission</term><term>Mutation (genetics)</term><term>Nerve Degeneration (genetics)</term><term>Nerve Degeneration (metabolism)</term><term>Nerve Degeneration (pathology)</term><term>Peptides (chemistry)</term><term>Peptides (genetics)</term><term>Peptides (metabolism)</term><term>Protein Binding</term><term>Protein Denaturation</term><term>Temperature</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Cellules cultivées</term><term>Dichroïsme circulaire</term><term>Dégénérescence nerveuse (anatomopathologie)</term><term>Dégénérescence nerveuse (génétique)</term><term>Dégénérescence nerveuse (métabolisme)</term><term>Dénaturation des protéines</term><term>Fer (métabolisme)</term><term>Ferritines ()</term><term>Ferritines (génétique)</term><term>Ferritines (métabolisme)</term><term>Ferritines (ultrastructure)</term><term>Humains</term><term>Liaison aux protéines</term><term>Microscopie électronique à transmission</term><term>Mutation (génétique)</term><term>Peptides ()</term><term>Peptides (génétique)</term><term>Peptides (métabolisme)</term><term>Souris</term><term>Température</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Ferritins</term><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Ferritins</term><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Ferritins</term><term>Iron</term><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Ferritins</term></keywords><keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Dégénérescence nerveuse</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mutation</term><term>Nerve Degeneration</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Dégénérescence nerveuse</term><term>Ferritines</term><term>Mutation</term><term>Peptides</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Nerve Degeneration</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Dégénérescence nerveuse</term><term>Fer</term><term>Ferritines</term><term>Peptides</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Nerve Degeneration</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Ferritines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cells, Cultured</term><term>Circular Dichroism</term><term>Humans</term><term>Mice</term><term>Microscopy, Electron, Transmission</term><term>Protein Binding</term><term>Protein Denaturation</term><term>Temperature</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules cultivées</term><term>Dichroïsme circulaire</term><term>Dénaturation des protéines</term><term>Ferritines</term><term>Humains</term><term>Liaison aux protéines</term><term>Microscopie électronique à transmission</term><term>Peptides</term><term>Souris</term><term>Température</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Nucleotide insertions in the ferritin light chain (FTL) polypeptide gene cause hereditary ferritinopathy, a neurodegenerative disease characterized by abnormal accumulation of ferritin and iron in the central nervous system. Here we describe for the first time the protein structure and iron storage function of the FTL mutant p.Phe167SerfsX26 (MT-FTL), which has a C terminus altered in sequence and extended in length. MT-FTL polypeptides assembled spontaneously into soluble, spherical 24-mers that were ultrastructurally indistinguishable from those of the wild type. Far-UV CD showed a decrease in alpha-helical content, and 8-anilino-1-naphthalenesulfonate fluorescence revealed the appearance of hydrophobic binding sites. Near-UV CD and proteolysis studies suggested little or no structural alteration outside of the C-terminal region. In contrast to wild type, MT-FTL homopolymers precipitated at much lower iron loading, had a diminished capacity to incorporate iron, and were less thermostable. However, precipitation was significantly reversed by addition of iron chelators both in vitro and in vivo. Our results reveal substantial protein conformational changes localized at the 4-fold pore of MT-FTL homopolymers and imply that the C terminus of the MT-FTL polypeptide plays an important role in ferritin solubility, stability, and iron management. We propose that the protrusion of some portion of the C terminus above the spherical shell allows it to cross-link with other mutant polypeptides through iron bridging, leading to enhanced mutant precipitation by iron. Our data suggest that hereditary ferritinopathy pathogenesis is likely to result from a combination of reduction in iron storage function and enhanced toxicity associated with iron-induced ferritin aggregates.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18755684</PMID><DateCompleted><Year>2009</Year><Month>01</Month><Day>07</Day></DateCompleted><DateRevised><Year>2018</Year><Month>12</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>283</Volume><Issue>46</Issue><PubDate><Year>2008</Year><Month>Nov</Month><Day>14</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation></Journal><ArticleTitle>Iron-mediated aggregation and a localized structural change characterize ferritin from a mutant light chain polypeptide that causes neurodegeneration.</ArticleTitle><Pagination><MedlinePgn>31679-89</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M805532200</ELocationID><Abstract><AbstractText>Nucleotide insertions in the ferritin light chain (FTL) polypeptide gene cause hereditary ferritinopathy, a neurodegenerative disease characterized by abnormal accumulation of ferritin and iron in the central nervous system. Here we describe for the first time the protein structure and iron storage function of the FTL mutant p.Phe167SerfsX26 (MT-FTL), which has a C terminus altered in sequence and extended in length. MT-FTL polypeptides assembled spontaneously into soluble, spherical 24-mers that were ultrastructurally indistinguishable from those of the wild type. Far-UV CD showed a decrease in alpha-helical content, and 8-anilino-1-naphthalenesulfonate fluorescence revealed the appearance of hydrophobic binding sites. Near-UV CD and proteolysis studies suggested little or no structural alteration outside of the C-terminal region. In contrast to wild type, MT-FTL homopolymers precipitated at much lower iron loading, had a diminished capacity to incorporate iron, and were less thermostable. However, precipitation was significantly reversed by addition of iron chelators both in vitro and in vivo. Our results reveal substantial protein conformational changes localized at the 4-fold pore of MT-FTL homopolymers and imply that the C terminus of the MT-FTL polypeptide plays an important role in ferritin solubility, stability, and iron management. We propose that the protrusion of some portion of the C terminus above the spherical shell allows it to cross-link with other mutant polypeptides through iron bridging, leading to enhanced mutant precipitation by iron. Our data suggest that hereditary ferritinopathy pathogenesis is likely to result from a combination of reduction in iron storage function and enhanced toxicity associated with iron-induced ferritin aggregates.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Baraibar</LastName><ForeName>Martin A</ForeName><Initials>MA</Initials><AffiliationInfo><Affiliation>Department of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Barbeito</LastName><ForeName>Ana G</ForeName><Initials>AG</Initials></Author><Author ValidYN="Y"><LastName>Muhoberac</LastName><ForeName>Barry B</ForeName><Initials>BB</Initials></Author><Author ValidYN="Y"><LastName>Vidal</LastName><ForeName>Ruben</ForeName><Initials>R</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 NS050227</GrantID><Acronym>NS</Acronym><Agency>NINDS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>NS050227</GrantID><Acronym>NS</Acronym><Agency>NINDS 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>2008</Year><Month>08</Month><Day>28</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="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>9007-73-2</RegistryNumber><NameOfSubstance UI="D005293">Ferritins</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002478" MajorTopicYN="N">Cells, Cultured</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002942" MajorTopicYN="N">Circular Dichroism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005293" MajorTopicYN="N">Ferritins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046529" MajorTopicYN="N">Microscopy, Electron, Transmission</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009410" MajorTopicYN="N">Nerve Degeneration</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010455" 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IdType="pubmed">9753631</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Barbeito, Ana G" sort="Barbeito, Ana G" uniqKey="Barbeito A" first="Ana G" last="Barbeito">Ana G. Barbeito</name><name sortKey="Muhoberac, Barry B" sort="Muhoberac, Barry B" uniqKey="Muhoberac B" first="Barry B" last="Muhoberac">Barry B. Muhoberac</name><name sortKey="Vidal, Ruben" sort="Vidal, Ruben" uniqKey="Vidal R" first="Ruben" last="Vidal">Ruben Vidal</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Baraibar, Martin A" sort="Baraibar, Martin A" uniqKey="Baraibar M" first="Martin A" last="Baraibar">Martin A. Baraibar</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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