scholarly journals Characterization of a DNA-damage-recognition protein from F9 teratocarcinoma cells, which is inducible by retinoic acid and cyclic AMP

1993 ◽  
Vol 293 (3) ◽  
pp. 879-879
Keyword(s):  
Dna Damage ◽  
Retinoic Acid ◽  
Cyclic Amp ◽  
Damage Recognition ◽  
Teratocarcinoma Cells ◽  
Recognition Protein ◽  
F9 Teratocarcinoma ◽  
Dna Damage Recognition

scholarly journals Characterization of a DNA-damage-recognition protein from F9 teratocarcinoma cells, which is inducible by retinoic acid and cyclic AMP

1993 ◽  
Vol 290 (1) ◽  
pp. 129-134 ◽  
Author(s):  
C C K Chao ◽  
N K Sun ◽  
S Lin-Chao
Keyword(s):  
Dna Damage ◽  
Retinoic Acid ◽  
Cyclic Amp ◽  
Mammalian Cells ◽  
Nuclear Protein ◽  
Binding Activity ◽  
Damage Recognition ◽  
Nuclear Extracts ◽  
Recognition Protein ◽  
Damaged Dna

A nuclear protein that recognizes u.v.-damaged DNA was detected in extracts from murine F9 embryonic stem cells using a DNA-binding assay. The nuclear-protein-binding activity was increased in cells after treatment with retinoic acid/dibutyryl cyclic AMP (dbcAMP), with optimum induction at 6 days. In vitro treatment of nuclear extracts with agents that affect protein conformation (such as urea, Nonidet P40 and Ca2+) slightly modulated the damage-recognition activity. Furthermore, treatment of nuclear extracts with phosphatase dramatically inhibited the binding activity. In addition, damaged-DNA recognition of the nuclear extracts was effectively inhibited by damaged double- and single-stranded DNA. The expression of the nuclear protein with similar characteristics was abundant in HeLa cells and was increased in drug- or u.v.-resistant cells. The findings suggest that the recognition of a u.v.-DNA adduct is modulated, at least in part, by an activity that is induced during retinoic acid/dbcAMP-induced differentiation. These results also imply that the identified damage-recognition protein may be important for the sensitivity or resistance of mammalian cells to DNA damage.

Characterization of a DNA damage-recognition protein from mammalian cells that binds specifically to intrastrand d(GpG) and d(ApG) DNA adducts of the anticancer drug cisplatin

Biochemistry ◽  
1990 ◽  
Vol 29 (24) ◽  
pp. 5872-5880 ◽  
Author(s):  
Brian A. Donahue ◽  
Marianne Augot ◽  
Steven F. Bellon ◽  
Daniel K. Treiber ◽  
Jeffrey H. Toney ◽  
...  
Keyword(s):  
Dna Damage ◽  
Anticancer Drug ◽  
Dna Adducts ◽  
Mammalian Cells ◽  
Damage Recognition ◽  
Recognition Protein ◽  
Dna Damage Recognition

scholarly journals Damage-recognition proteins as a potential indicator of DNA-damage-mediated sensitivity or resistance of human cells to ultraviolet radiation

1992 ◽  
Vol 282 (1) ◽  
pp. 203-207 ◽  
Author(s):  
C C K Chao
Keyword(s):  
Dna Damage ◽  
Dna Repair ◽  
Hela Cells ◽  
Xeroderma Pigmentosum ◽  
Cross Linking ◽  
Damage Recognition ◽  
Modified Dna ◽  
Potential Indicator ◽  
Recognition Protein ◽  
Dna Damage Recognition

We have previously identified damage-recognition proteins that bind to cisplatin[cis-diamminedichloroplatinum(II), a DNA cross-linking agent]- or u.v.-modified DNA in HeLa cells [Chao, Huang, Huang & Lin-Chao (1991) Mol. Cell. Biol. 11, 2075-2080; Chao, Huang, Lee & Lin-Chao (1991) Biochem. J. 277, 875-878]. In the present study we compared damage-recognition proteins in cells expressing different sensitivities to DNA damage. An increase in damage-recognition proteins and an enhancement of plasmid re-activation were detected in HeLa cells resistant to cisplatin and u.v. However, repair-defective cells derived from xeroderma-pigmentosum (a rare skin disease) patients did not express less cisplatin damage-recognition proteins than repair-competent cells, suggesting that damage-recognition-protein expression may not be related to DNA repair. By contrast, cells resistant to DNA damage consistently expressed high levels of u.v.-modified-DNA damage-recognition proteins. The results support the notion that u.v. damage-recognition proteins are different from those that bind to cisplatin. These findings also suggest that the damage-recognition proteins identified could be used as potential indicators of the sensitivity or resistance of cells to u.v.

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