Abstract：
: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.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Sridharan D,Brown M,Lambert WC,McMahon LW,Lambert MWdoi
10.1242/jcs.00294keywords:
subject
Has Abstractpub_date
2003-03-01 00:00:00pages
823-35issue
Pt 5eissn
0021-9533issn
1477-9137journal_volume
116pub_type
杂志文章abstract：:Human erythrocytes suspended in buffered isotonic saline were frozen to the temperature of liquid nitrogen at various cooling rates of 3, 140, 700, 1800, 3500, 8000 and 11 500 deg. C/min. The membrane ultrastructure in the frozen state and the extent of haemolysis after thawing were examined at each cooling rate. As t...
journal_title：Journal of cell science
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更新日期：1981-06-01 00:00:00
abstract：:Prions are proteins that access self-templating amyloid forms, which confer phenotypic changes that can spread from individual to individual within or between species. These infectious phenotypes can be beneficial, as with yeast prions, or deleterious, as with mammalian prions that transmit spongiform encephalopathies...
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journal_title：Journal of cell science
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journal_title：Journal of cell science
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更新日期：1998-03-01 00:00:00
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journal_title：Journal of cell science
pub_type： 杂志文章
doi：
更新日期：1983-05-01 00:00:00
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journal_title：Journal of cell science
pub_type： 杂志文章
doi：
更新日期：1982-08-01 00:00:00
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pub_type： 杂志文章,评审
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更新日期：2005-12-01 00:00:00
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journal_title：Journal of cell science
pub_type： 杂志文章
doi：
更新日期：1980-04-01 00:00:00
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pub_type： 杂志文章
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更新日期：2015-02-15 00:00:00
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pub_type： 杂志文章
doi：10.1242/jcs.113019
更新日期：2012-12-15 00:00:00
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journal_title：Journal of cell science
pub_type： 杂志文章
doi：10.1242/jcs.173195
更新日期：2016-01-15 00:00:00
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doi：
更新日期：1991-07-01 00:00:00
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doi：
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