Linked Life Data

12571280

Source:http://linkedlifedata.com/resource/pubmed/id/12571280

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 5
pubmed:dateCreated
2003-2-6
pubmed:abstractText
The events responsible for repair of DNA interstrand cross-links in mammalian cells, the proteins involved and their interactions with each other are poorly understood. The present study demonstrates that the structural protein nonerythroid alpha spectrin (alphaSpIISigma*), present in normal human cell nuclei, plays an important role in repair of DNA interstrand cross-links. These results show that alphaSpIISigma* relocalizes to nuclear foci after damage of normal human cells with the DNA interstrand cross-linking agent 8-methoxypsoralen plus ultraviolet A (UVA) light and that FANCA and the known DNA repair protein XPF localize to the same nuclear foci. That alphaSpIISigma* is essential for this re-localization is demonstrated by the finding that in cells from patients with Fanconi anemia complementation group A (FA-A), which have decreased ability to repair DNA interstrand cross-links and decreased levels of alphaSpIISigma*, there is a significant reduction in formation of damage-induced XPF as well as alphaSpIISigma* nuclear foci, even though levels of XPF are normal in these cells. In corrected FA-A cells, in which levels of alphaSpIISigma* are restored to normal, numbers of damage-induced nuclear foci are also returned to normal. Co-immunoprecipitation studies show that alphaSpIISigma*, FANCA and XPF co-immunoprecipitate with each other from normal human nuclear proteins. These results demonstrate that alphaSpIISigma*, FANCA and XPF interact with each other in the nucleus and indicate that there is a close functional relationship between these proteins. These studies suggest that an important role for alphaSpIISigma* in the nucleus is to act as a scaffold, aiding in recruitment and alignment of repair proteins at sites of damage.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
116
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
823-35
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:12571280-Blotting, Western, pubmed-meshheading:12571280-Cell Line, pubmed-meshheading:12571280-Cell Nucleus, pubmed-meshheading:12571280-Cross-Linking Reagents, pubmed-meshheading:12571280-DNA Adducts, pubmed-meshheading:12571280-DNA Damage, pubmed-meshheading:12571280-DNA Repair, pubmed-meshheading:12571280-DNA-Binding Proteins, pubmed-meshheading:12571280-Dose-Response Relationship, Radiation, pubmed-meshheading:12571280-Fanconi Anemia Complementation Group A Protein, pubmed-meshheading:12571280-Fluorescent Antibody Technique, Indirect, pubmed-meshheading:12571280-Humans, pubmed-meshheading:12571280-Methoxsalen, pubmed-meshheading:12571280-Nuclear Proteins, pubmed-meshheading:12571280-Precipitin Tests, pubmed-meshheading:12571280-Proteins, pubmed-meshheading:12571280-Spectrin, pubmed-meshheading:12571280-Time Factors, pubmed-meshheading:12571280-Ultraviolet Rays
pubmed:year
2003
pubmed:articleTitle
Nonerythroid alphaII spectrin is required for recruitment of FANCA and XPF to nuclear foci induced by DNA interstrand cross-links.
pubmed:affiliation
Department of Pathology and Laboratory Medicine, UMDNJ - New Jersey Medical School and the Graduate School of Biomedical Sciences, Newark, NJ 07103, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.