Beta-actin deficiency with oxidative posttranslational modifications in Rett syndrome erythrocytes: insights into an altered cytoskeletal organization
Beta-actin, a critical player in cellular functions ranging from cell motility and the maintenance of cell shape to transcription regulation, was evaluated in the erythrocyte membranes from patients with typical Rett syndrome (RTT) and methyl CpG binding protein 2 (MECP2) gene mutations. RTT, affect...
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| Veröffentlicht in: | PloS one 2014-03, Vol.9 (3), p.e93181-e93181 |
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| creator | Cortelazzo, Alessio De Felice, Claudio Pecorelli, Alessandra Belmonte, Giuseppe Signorini, Cinzia Leoncini, Silvia Zollo, Gloria Capone, Antonietta Giovampaola, Cinzia Della Sticozzi, Claudia Valacchi, Giuseppe Ciccoli, Lucia Guerranti, Roberto Hayek, Joussef |
| description | Beta-actin, a critical player in cellular functions ranging from cell motility and the maintenance of cell shape to transcription regulation, was evaluated in the erythrocyte membranes from patients with typical Rett syndrome (RTT) and methyl CpG binding protein 2 (MECP2) gene mutations. RTT, affecting almost exclusively females with an average frequency of 1∶10,000 female live births, is considered the second commonest cause of severe cognitive impairment in the female gender. Evaluation of beta-actin was carried out in a comparative cohort study on red blood cells (RBCs), drawn from healthy control subjects and RTT patients using mass spectrometry-based quantitative analysis. We observed a decreased expression of the beta-actin isoforms (relative fold changes for spots 1, 2 and 3: -1.82±0.15, -2.15±0.06, and -2.59±0.48, respectively) in pathological RBCs. The results were validated by western blotting and immunofluorescence microscopy. In addition, beta-actin from RTT patients also showed a dramatic increase in oxidative posttranslational modifications (PTMs) as the result of its binding with the lipid peroxidation product 4-hydroxy-2-nonenal (4-HNE). Our findings demonstrate, for the first time, a beta-actin down-regulation and oxidative PTMs for RBCs of RTT patients, thus indicating an altered cytoskeletal organization. |
| doi_str_mv | 10.1371/journal.pone.0093181 |
| format | Article |
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RTT, affecting almost exclusively females with an average frequency of 1∶10,000 female live births, is considered the second commonest cause of severe cognitive impairment in the female gender. Evaluation of beta-actin was carried out in a comparative cohort study on red blood cells (RBCs), drawn from healthy control subjects and RTT patients using mass spectrometry-based quantitative analysis. We observed a decreased expression of the beta-actin isoforms (relative fold changes for spots 1, 2 and 3: -1.82±0.15, -2.15±0.06, and -2.59±0.48, respectively) in pathological RBCs. The results were validated by western blotting and immunofluorescence microscopy. In addition, beta-actin from RTT patients also showed a dramatic increase in oxidative posttranslational modifications (PTMs) as the result of its binding with the lipid peroxidation product 4-hydroxy-2-nonenal (4-HNE). Our findings demonstrate, for the first time, a beta-actin down-regulation and oxidative PTMs for RBCs of RTT patients, thus indicating an altered cytoskeletal organization.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0093181</identifier><identifier>PMID: 24671107</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Actin ; Actin Cytoskeleton - metabolism ; Actins - deficiency ; Aldehydes - metabolism ; Biology and Life Sciences ; Blood & organ donations ; Blood cells ; Case-Control Studies ; Cell Membrane - metabolism ; Cell size ; Child ; Child, Preschool ; Cognitive ability ; Comparative analysis ; CpG islands ; Cytoskeleton ; Erythrocytes ; Erythrocytes - metabolism ; Female ; Females ; Gene mutation ; Gene regulation ; Genetic aspects ; Hospitals ; Humans ; Immunofluorescence ; Intellectual disabilities ; Isoforms ; Life sciences ; Lipid Peroxidation ; Mass spectrometry ; Mass spectroscopy ; MeCP2 protein ; Medicine ; Medicine and Health Sciences ; Membranes ; Methyl-CpG binding protein ; Methyl-CpG-Binding Protein 2 - genetics ; Microscopy ; Motility ; Mutation ; Oxidation-Reduction ; Oxidative stress ; Patients ; Peroxidation ; Protein binding ; Protein Isoforms - metabolism ; Protein Processing, Post-Translational ; Proteins ; Quantitative analysis ; Red blood cells ; Rett syndrome ; Rett Syndrome - metabolism ; Rett Syndrome - pathology ; Rodents ; Spots ; Transcription ; Tutoring ; Western blotting</subject><ispartof>PloS one, 2014-03, Vol.9 (3), p.e93181-e93181</ispartof><rights>COPYRIGHT 2014 Public Library of Science</rights><rights>2014 Cortelazzo et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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Academic</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Nursing & Allied Health Premium</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Materials Science Collection</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cortelazzo, Alessio</au><au>De Felice, Claudio</au><au>Pecorelli, Alessandra</au><au>Belmonte, Giuseppe</au><au>Signorini, Cinzia</au><au>Leoncini, Silvia</au><au>Zollo, Gloria</au><au>Capone, Antonietta</au><au>Giovampaola, Cinzia Della</au><au>Sticozzi, Claudia</au><au>Valacchi, Giuseppe</au><au>Ciccoli, Lucia</au><au>Guerranti, Roberto</au><au>Hayek, Joussef</au><au>D’Esposito, Maurizio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Beta-actin deficiency with oxidative posttranslational modifications in Rett syndrome erythrocytes: insights into an altered cytoskeletal organization</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2014-03-26</date><risdate>2014</risdate><volume>9</volume><issue>3</issue><spage>e93181</spage><epage>e93181</epage><pages>e93181-e93181</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Beta-actin, a critical player in cellular functions ranging from cell motility and the maintenance of cell shape to transcription regulation, was evaluated in the erythrocyte membranes from patients with typical Rett syndrome (RTT) and methyl CpG binding protein 2 (MECP2) gene mutations. RTT, affecting almost exclusively females with an average frequency of 1∶10,000 female live births, is considered the second commonest cause of severe cognitive impairment in the female gender. Evaluation of beta-actin was carried out in a comparative cohort study on red blood cells (RBCs), drawn from healthy control subjects and RTT patients using mass spectrometry-based quantitative analysis. We observed a decreased expression of the beta-actin isoforms (relative fold changes for spots 1, 2 and 3: -1.82±0.15, -2.15±0.06, and -2.59±0.48, respectively) in pathological RBCs. The results were validated by western blotting and immunofluorescence microscopy. In addition, beta-actin from RTT patients also showed a dramatic increase in oxidative posttranslational modifications (PTMs) as the result of its binding with the lipid peroxidation product 4-hydroxy-2-nonenal (4-HNE). Our findings demonstrate, for the first time, a beta-actin down-regulation and oxidative PTMs for RBCs of RTT patients, thus indicating an altered cytoskeletal organization.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24671107</pmid><doi>10.1371/journal.pone.0093181</doi><tpages>e93181</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2014-03, Vol.9 (3), p.e93181-e93181 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1510500431 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Public Library of Science (PLoS); PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Actin Actin Cytoskeleton - metabolism Actins - deficiency Aldehydes - metabolism Biology and Life Sciences Blood & organ donations Blood cells Case-Control Studies Cell Membrane - metabolism Cell size Child Child, Preschool Cognitive ability Comparative analysis CpG islands Cytoskeleton Erythrocytes Erythrocytes - metabolism Female Females Gene mutation Gene regulation Genetic aspects Hospitals Humans Immunofluorescence Intellectual disabilities Isoforms Life sciences Lipid Peroxidation Mass spectrometry Mass spectroscopy MeCP2 protein Medicine Medicine and Health Sciences Membranes Methyl-CpG binding protein Methyl-CpG-Binding Protein 2 - genetics Microscopy Motility Mutation Oxidation-Reduction Oxidative stress Patients Peroxidation Protein binding Protein Isoforms - metabolism Protein Processing, Post-Translational Proteins Quantitative analysis Red blood cells Rett syndrome Rett Syndrome - metabolism Rett Syndrome - pathology Rodents Spots Transcription Tutoring Western blotting |
| title | Beta-actin deficiency with oxidative posttranslational modifications in Rett syndrome erythrocytes: insights into an altered cytoskeletal organization |
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