The human counterpart of zebrafish shiraz shows sideroblastic-like microcytic anemia and iron overload.
Identifieur interne : 000C48 ( Main/Exploration ); précédent : 000C47; suivant : 000C49The human counterpart of zebrafish shiraz shows sideroblastic-like microcytic anemia and iron overload.
Auteurs : Clara Camaschella [Italie] ; Alessandro Campanella ; Luigia De Falco ; Loredana Boschetto ; Roberta Merlini ; Laura Silvestri ; Sonia Levi ; Achille IolasconSource :
- Blood [ 0006-4971 ] ; 2007.
Descripteurs français
- KwdFr :
- Aconitate hydratase (MeSH), Adulte d'âge moyen (MeSH), Anémie sidéroblastique (anatomopathologie), Anémie sidéroblastique (génétique), Cellules cultivées (MeSH), Glutarédoxines (MeSH), Humains (MeSH), Immunoprécipitation (MeSH), Mitochondries (enzymologie), Mutation (génétique), Mâle (MeSH), Oxidoreductases (génétique), Oxidoreductases (métabolisme), RT-PCR (MeSH), Surcharge en fer (MeSH), Technique de Western (MeSH), Test ELISA (MeSH).
- MESH :
- anatomopathologie : Anémie sidéroblastique.
- enzymologie : Mitochondries.
- génétique : Anémie sidéroblastique, Mutation, Oxidoreductases.
- métabolisme : Oxidoreductases.
- Aconitate hydratase, Adulte d'âge moyen, Cellules cultivées, Glutarédoxines, Humains, Immunoprécipitation, Mâle, RT-PCR, Surcharge en fer, Technique de Western, Test ELISA.
English descriptors
- KwdEn :
- Aconitate Hydratase (MeSH), Anemia, Sideroblastic (genetics), Anemia, Sideroblastic (pathology), Blotting, Western (MeSH), Cells, Cultured (MeSH), Enzyme-Linked Immunosorbent Assay (MeSH), Glutaredoxins (MeSH), Humans (MeSH), Immunoprecipitation (MeSH), Iron Overload (MeSH), Male (MeSH), Middle Aged (MeSH), Mitochondria (enzymology), Mutation (genetics), Oxidoreductases (genetics), Oxidoreductases (metabolism), Reverse Transcriptase Polymerase Chain Reaction (MeSH).
- MESH :
- chemical , genetics : Oxidoreductases.
- chemical , metabolism : Oxidoreductases.
- chemical : Aconitate Hydratase, Glutaredoxins.
- enzymology : Mitochondria.
- genetics : Anemia, Sideroblastic, Mutation.
- pathology : Anemia, Sideroblastic.
- Blotting, Western, Cells, Cultured, Enzyme-Linked Immunosorbent Assay, Humans, Immunoprecipitation, Iron Overload, Male, Middle Aged, Reverse Transcriptase Polymerase Chain Reaction.
Abstract
Inherited microcytic-hypochromic anemias in rodents and zebrafish suggest the existence of corresponding human disorders. The zebrafish mutant shiraz has severe anemia and is embryonically lethal because of glutaredoxin 5 (GRLX5) deletion, insufficient biogenesis of mitochondrial iron-sulfur (Fe/S) clusters, and deregulated iron-regulatory protein 1 (IRP1) activity. This leads to stabilization of transferrin receptor 1 (TfR) RNA, repression of ferritin, and ALA-synthase 2 (ALAS2) translation with impaired heme synthesis. We report the first case of GLRX5 deficiency in a middle-aged anemic male with iron overload and a low number of ringed sideroblasts. Anemia was worsened by blood transfusions but partially reversed by iron chelation. The patient had a homozygous (c.294A>G) mutation that interferes with intron 1 splicing and drastically reduces GLRX5 RNA. As in shiraz, aconitase and H-ferritin levels were low and TfR level was high in the patient's cells, compatible with increased IRP1 binding. Based on the biochemical and clinical phenotype, we hypothesize that IRP2, less degraded by low heme, contributes to the repression of the erythroblasts ferritin and ALAS2, increasing mitochondrial iron. Iron chelation, redistributing iron to the cytosol, might relieve IRP2 excess, improving heme synthesis and anemia. GLRX5 function is highly conserved, but at variance with zebrafish, its defect in humans leads to anemia and iron overload.
DOI: 10.1182/blood-2007-02-072520
PubMed: 17485548
Affiliations:
Links toward previous steps (curation, corpus...)
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Falco</name></author><author><name sortKey="Boschetto, Loredana" sort="Boschetto, Loredana" uniqKey="Boschetto L" first="Loredana" last="Boschetto">Loredana Boschetto</name></author><author><name sortKey="Merlini, Roberta" sort="Merlini, Roberta" uniqKey="Merlini R" first="Roberta" last="Merlini">Roberta Merlini</name></author><author><name sortKey="Silvestri, Laura" sort="Silvestri, Laura" uniqKey="Silvestri L" first="Laura" last="Silvestri">Laura Silvestri</name></author><author><name sortKey="Levi, Sonia" sort="Levi, Sonia" uniqKey="Levi S" first="Sonia" last="Levi">Sonia Levi</name></author><author><name sortKey="Iolascon, Achille" sort="Iolascon, Achille" uniqKey="Iolascon A" first="Achille" last="Iolascon">Achille Iolascon</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17485548</idno><idno type="pmid">17485548</idno><idno type="doi">10.1182/blood-2007-02-072520</idno><idno 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nuts="2">Lombardie</region></placeName></affiliation></author><author><name sortKey="Campanella, Alessandro" sort="Campanella, Alessandro" uniqKey="Campanella A" first="Alessandro" last="Campanella">Alessandro Campanella</name></author><author><name sortKey="De Falco, Luigia" sort="De Falco, Luigia" uniqKey="De Falco L" first="Luigia" last="De Falco">Luigia De Falco</name></author><author><name sortKey="Boschetto, Loredana" sort="Boschetto, Loredana" uniqKey="Boschetto L" first="Loredana" last="Boschetto">Loredana Boschetto</name></author><author><name sortKey="Merlini, Roberta" sort="Merlini, Roberta" uniqKey="Merlini R" first="Roberta" last="Merlini">Roberta Merlini</name></author><author><name sortKey="Silvestri, Laura" sort="Silvestri, Laura" uniqKey="Silvestri L" first="Laura" last="Silvestri">Laura Silvestri</name></author><author><name sortKey="Levi, Sonia" sort="Levi, Sonia" uniqKey="Levi S" first="Sonia" last="Levi">Sonia Levi</name></author><author><name sortKey="Iolascon, Achille" sort="Iolascon, Achille" uniqKey="Iolascon A" first="Achille" last="Iolascon">Achille Iolascon</name></author></analytic><series><title level="j">Blood</title><idno type="ISSN">0006-4971</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aconitate Hydratase (MeSH)</term><term>Anemia, Sideroblastic (genetics)</term><term>Anemia, Sideroblastic (pathology)</term><term>Blotting, Western (MeSH)</term><term>Cells, Cultured (MeSH)</term><term>Enzyme-Linked Immunosorbent Assay (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Humans (MeSH)</term><term>Immunoprecipitation (MeSH)</term><term>Iron Overload (MeSH)</term><term>Male (MeSH)</term><term>Middle Aged (MeSH)</term><term>Mitochondria (enzymology)</term><term>Mutation (genetics)</term><term>Oxidoreductases (genetics)</term><term>Oxidoreductases (metabolism)</term><term>Reverse Transcriptase Polymerase Chain Reaction (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Aconitate hydratase (MeSH)</term><term>Adulte d'âge moyen (MeSH)</term><term>Anémie sidéroblastique (anatomopathologie)</term><term>Anémie sidéroblastique (génétique)</term><term>Cellules cultivées (MeSH)</term><term>Glutarédoxines (MeSH)</term><term>Humains (MeSH)</term><term>Immunoprécipitation (MeSH)</term><term>Mitochondries (enzymologie)</term><term>Mutation (génétique)</term><term>Mâle (MeSH)</term><term>Oxidoreductases (génétique)</term><term>Oxidoreductases (métabolisme)</term><term>RT-PCR (MeSH)</term><term>Surcharge en fer (MeSH)</term><term>Technique de Western (MeSH)</term><term>Test ELISA (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Aconitate Hydratase</term><term>Glutaredoxins</term></keywords><keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Anémie sidéroblastique</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Mitochondries</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Mitochondria</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Anemia, Sideroblastic</term><term>Mutation</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Anémie sidéroblastique</term><term>Mutation</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Anemia, Sideroblastic</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Blotting, Western</term><term>Cells, Cultured</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Humans</term><term>Immunoprecipitation</term><term>Iron Overload</term><term>Male</term><term>Middle Aged</term><term>Reverse Transcriptase Polymerase Chain Reaction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Aconitate hydratase</term><term>Adulte d'âge moyen</term><term>Cellules cultivées</term><term>Glutarédoxines</term><term>Humains</term><term>Immunoprécipitation</term><term>Mâle</term><term>RT-PCR</term><term>Surcharge en fer</term><term>Technique de Western</term><term>Test ELISA</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Inherited microcytic-hypochromic anemias in rodents and zebrafish suggest the existence of corresponding human disorders. The zebrafish mutant shiraz has severe anemia and is embryonically lethal because of glutaredoxin 5 (GRLX5) deletion, insufficient biogenesis of mitochondrial iron-sulfur (Fe/S) clusters, and deregulated iron-regulatory protein 1 (IRP1) activity. This leads to stabilization of transferrin receptor 1 (TfR) RNA, repression of ferritin, and ALA-synthase 2 (ALAS2) translation with impaired heme synthesis. We report the first case of GLRX5 deficiency in a middle-aged anemic male with iron overload and a low number of ringed sideroblasts. Anemia was worsened by blood transfusions but partially reversed by iron chelation. The patient had a homozygous (c.294A>G) mutation that interferes with intron 1 splicing and drastically reduces GLRX5 RNA. As in shiraz, aconitase and H-ferritin levels were low and TfR level was high in the patient's cells, compatible with increased IRP1 binding. Based on the biochemical and clinical phenotype, we hypothesize that IRP2, less degraded by low heme, contributes to the repression of the erythroblasts ferritin and ALAS2, increasing mitochondrial iron. Iron chelation, redistributing iron to the cytosol, might relieve IRP2 excess, improving heme synthesis and anemia. GLRX5 function is highly conserved, but at variance with zebrafish, its defect in humans leads to anemia and iron overload.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17485548</PMID><DateCompleted><Year>2007</Year><Month>09</Month><Day>20</Day></DateCompleted><DateRevised><Year>2017</Year><Month>09</Month><Day>22</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-4971</ISSN><JournalIssue CitedMedium="Print"><Volume>110</Volume><Issue>4</Issue><PubDate><Year>2007</Year><Month>Aug</Month><Day>15</Day></PubDate></JournalIssue><Title>Blood</Title><ISOAbbreviation>Blood</ISOAbbreviation></Journal><ArticleTitle>The human counterpart of zebrafish shiraz shows sideroblastic-like microcytic anemia and iron overload.</ArticleTitle><Pagination><MedlinePgn>1353-8</MedlinePgn></Pagination><Abstract><AbstractText>Inherited microcytic-hypochromic anemias in rodents and zebrafish suggest the existence of corresponding human disorders. The zebrafish mutant shiraz has severe anemia and is embryonically lethal because of glutaredoxin 5 (GRLX5) deletion, insufficient biogenesis of mitochondrial iron-sulfur (Fe/S) clusters, and deregulated iron-regulatory protein 1 (IRP1) activity. This leads to stabilization of transferrin receptor 1 (TfR) RNA, repression of ferritin, and ALA-synthase 2 (ALAS2) translation with impaired heme synthesis. We report the first case of GLRX5 deficiency in a middle-aged anemic male with iron overload and a low number of ringed sideroblasts. Anemia was worsened by blood transfusions but partially reversed by iron chelation. The patient had a homozygous (c.294A>G) mutation that interferes with intron 1 splicing and drastically reduces GLRX5 RNA. As in shiraz, aconitase and H-ferritin levels were low and TfR level was high in the patient's cells, compatible with increased IRP1 binding. Based on the biochemical and clinical phenotype, we hypothesize that IRP2, less degraded by low heme, contributes to the repression of the erythroblasts ferritin and ALAS2, increasing mitochondrial iron. Iron chelation, redistributing iron to the cytosol, might relieve IRP2 excess, improving heme synthesis and anemia. GLRX5 function is highly conserved, but at variance with zebrafish, its defect in humans leads to anemia and iron overload.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Camaschella</LastName><ForeName>Clara</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Vita-Salute University, Milan, Italy. camaschella.clara@hsr.it</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Campanella</LastName><ForeName>Alessandro</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>De Falco</LastName><ForeName>Luigia</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Boschetto</LastName><ForeName>Loredana</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Merlini</LastName><ForeName>Roberta</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Silvestri</LastName><ForeName>Laura</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Levi</LastName><ForeName>Sonia</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Iolascon</LastName><ForeName>Achille</ForeName><Initials>A</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>GGP05024</GrantID><Agency>Telethon</Agency><Country>Italy</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D002363">Case Reports</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2007</Year><Month>05</Month><Day>07</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Blood</MedlineTA><NlmUniqueID>7603509</NlmUniqueID><ISSNLinking>0006-4971</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516011">GLRX5 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.2.1.3</RegistryNumber><NameOfSubstance UI="D000154">Aconitate Hydratase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>AIM</CitationSubset><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000154" MajorTopicYN="N">Aconitate Hydratase</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000756" MajorTopicYN="N">Anemia, Sideroblastic</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015153" MajorTopicYN="N">Blotting, Western</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002478" MajorTopicYN="N">Cells, Cultured</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004797" MajorTopicYN="N">Enzyme-Linked Immunosorbent Assay</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D047468" MajorTopicYN="N">Immunoprecipitation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019190" MajorTopicYN="Y">Iron Overload</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008297" MajorTopicYN="N">Male</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008875" MajorTopicYN="N">Middle Aged</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008928" MajorTopicYN="N">Mitochondria</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020133" MajorTopicYN="N">Reverse Transcriptase Polymerase Chain Reaction</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>5</Month><Day>9</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>9</Month><Day>21</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>5</Month><Day>9</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17485548</ArticleId><ArticleId IdType="pii">blood-2007-02-072520</ArticleId><ArticleId IdType="doi">10.1182/blood-2007-02-072520</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Italie</li></country><region><li>Lombardie</li></region><settlement><li>Milan</li></settlement></list><tree><noCountry><name sortKey="Boschetto, Loredana" sort="Boschetto, Loredana" uniqKey="Boschetto L" first="Loredana" last="Boschetto">Loredana Boschetto</name><name sortKey="Campanella, Alessandro" sort="Campanella, Alessandro" uniqKey="Campanella A" first="Alessandro" last="Campanella">Alessandro Campanella</name><name sortKey="De Falco, Luigia" sort="De Falco, Luigia" uniqKey="De Falco L" first="Luigia" last="De Falco">Luigia De Falco</name><name sortKey="Iolascon, Achille" sort="Iolascon, Achille" uniqKey="Iolascon A" first="Achille" last="Iolascon">Achille Iolascon</name><name sortKey="Levi, Sonia" sort="Levi, Sonia" uniqKey="Levi S" first="Sonia" last="Levi">Sonia Levi</name><name sortKey="Merlini, Roberta" sort="Merlini, Roberta" uniqKey="Merlini R" first="Roberta" last="Merlini">Roberta Merlini</name><name sortKey="Silvestri, Laura" sort="Silvestri, Laura" uniqKey="Silvestri L" first="Laura" last="Silvestri">Laura Silvestri</name></noCountry><country name="Italie"><region name="Lombardie"><name sortKey="Camaschella, Clara" sort="Camaschella, Clara" uniqKey="Camaschella C" first="Clara" last="Camaschella">Clara Camaschella</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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