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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2005-10-18
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pubmed:databankReference |
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pubmed:abstractText |
Autosomal recessive mandibuloacral dysplasia [mandibuloacral dysplasia type A (MADA); Online Mendelian Inheritance in Man (OMIM) no. 248370] is caused by a mutation in LMNA encoding lamin A/C. Here we show that this mutation causes accumulation of the lamin A precursor protein, a marked alteration of the nuclear architecture and, hence, chromatin disorganization. Heterochromatin domains are altered or completely lost in MADA nuclei, consistent with the finding that heterochromatin-associated protein HP1beta and histone H3 methylated at lysine 9 and their nuclear envelope partner protein lamin B receptor (LBR) are delocalized and solubilized. Both accumulation of lamin A precursor and chromatin defects become more severe in older patients. These results strongly suggest that altered chromatin remodeling is a key event in the cascade of epigenetic events causing MADA and could be related to the premature-aging phenotype.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/Heterochromatin,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Lamin Type A,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/heterochromatin-specific...,
http://linkedlifedata.com/resource/pubmed/chemical/lamin B receptor,
http://linkedlifedata.com/resource/pubmed/chemical/prelamin A
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1531-2267
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pubmed:author |
pubmed-author:BioccaSilviaS,
pubmed-author:CapanniCristinaC,
pubmed-author:ColumbaroMartaM,
pubmed-author:D'ApiceMaria RosariaMR,
pubmed-author:FilesiIlariaI,
pubmed-author:GullottaFrancescaF,
pubmed-author:LattanziGiovannaG,
pubmed-author:MaraldiNadir MNM,
pubmed-author:MattioliElisabettaE,
pubmed-author:NardoneAnna MariaAM,
pubmed-author:NovelliGiuseppeG,
pubmed-author:SabatelliPatriziaP,
pubmed-author:ScaranoGioacchinoG
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pubmed:issnType |
Electronic
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pubmed:day |
17
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pubmed:volume |
23
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
150-8
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pubmed:meshHeading |
pubmed-meshheading:16046620-Adolescent,
pubmed-meshheading:16046620-Adult,
pubmed-meshheading:16046620-Case-Control Studies,
pubmed-meshheading:16046620-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:16046620-Facial Bones,
pubmed-meshheading:16046620-Female,
pubmed-meshheading:16046620-Fibroblasts,
pubmed-meshheading:16046620-Heterochromatin,
pubmed-meshheading:16046620-Histones,
pubmed-meshheading:16046620-Humans,
pubmed-meshheading:16046620-Lamin Type A,
pubmed-meshheading:16046620-Male,
pubmed-meshheading:16046620-Middle Aged,
pubmed-meshheading:16046620-Nuclear Envelope,
pubmed-meshheading:16046620-Nuclear Proteins,
pubmed-meshheading:16046620-Protein Precursors,
pubmed-meshheading:16046620-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:16046620-Staining and Labeling
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pubmed:year |
2005
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pubmed:articleTitle |
Alterations of nuclear envelope and chromatin organization in mandibuloacral dysplasia, a rare form of laminopathy.
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pubmed:affiliation |
Laboratory of Clinical Biochemistry and Department of Neuroscience, University of Roma Tor Vergata, Rome, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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