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Dff40 expression is upregulated in atherosclerotic plaque.
the low expression levels of DFF40/CAD and the absence of DNA laddering as common molecular traits in glioblastoma
Data suggest DFF40 expression in breast cancer cell line is involved in drug sensitivity/resistance to doxorubicin; apoptotic cell death due to doxorubicin (a topoisomerase II (show TOP2 Proteins) inhibitor) is enhanced by DFF40 overexpression in breast cancer cell line.
Data show that the caspase-activated DNase (CAD) is activated when caspases cleave its endogenous inhibitor ICAD (show DFFA Proteins), resulting in the characteristic DNA laddering of apoptosis.
Combinatorial use of some sulfonamides such as acetazolamide along with increased expression of DFF40 can potently kill tumor cells via apoptosis.
DFF40/CAD-independent mechanism driving conformational nuclear changes during caspase (show CASP3 Proteins)-dependent cell death
the highest order of chromatin compaction observed in the later steps of caspase (show CASP3 Proteins)-dependent apoptosis relies on DFF40/CAD-mediated DNA damage by generating 3'-OH ends in single-strand rather than double-strand DNA nicks/breaks
These results suggest a cooperative activity between CAD and DNAS1L3 (show DNASE1L3 Proteins) to accomplish internucleosomal DNA fragmentation .
Human papillomavirus type 16 E6 protein inhibits DNA fragmentation via interaction with DNA fragmentation factor (show DFFA Proteins) 40
During apoptotic rearrangement of interchromatin granule clusters, the nuclear matrix (NuMa rearrangement) and chromatin are closely associated. This process occurs in defined stages and depends on the activity of protein phosphatases, caspases and CAD.
Dff40 expression is upregulated in atherosclerotic plaque. Dff40 deficiency inhibited high-fat diet-induced atherosclerosis, as evidenced by decreased atherosclerotic plaques, inhibited inflammatory response, and macrophage apoptosis, as well as enhanced stability of plaques.
results show that caspase 3/CAD promotes cell differentiation by directly modifying the DNA/nuclear microenvironment, which enhances the expression of critical regulatory genes
Co-transfection of mouse DFF45 (show DFFA Proteins)(-/-) fibroblasts with plasmids encoding human DFF40 and DFF45 (show DFFA Proteins) reversed the apoptosis resistance normally observed in these cells
The thymus of DNase II(-/-)CAD(-/-) embryos contained many foci carrying undigested DNA and the cellularity was severely reduced due to a block in T cell development.
Interactions identified here between mouse liver histone H1 (show H1F0 Proteins) carboxyl-terminal domain and DFF40/CAD target and activate linker DNA cleavage during the terminal stages of apoptosis.
The results suggest that CAD protein may be preferentially degraded by the ubiquitin-proteasome system in the absence of its inhibitor (ICAD (show DFFA Proteins)) to maintain protein quality control.
A los of caspase-activated DNASE enhances tumorigenesis induced by a chemical carcinogen in a model of skin carcinogenesis in mice.
Apoptosis is a cell death process that removes toxic and/or useless cells during mammalian development. The apoptotic process is accompanied by shrinkage and fragmentation of the cells and nuclei and degradation of the chromosomal DNA into nucleosomal units. DNA fragmentation factor (DFF) is a heterodimeric protein of 40-kD (DFFB) and 45-kD (DFFA) subunits. DFFA is the substrate for caspase-3 and triggers DNA fragmentation during apoptosis. DFF becomes activated when DFFA is cleaved by caspase-3. The cleaved fragments of DFFA dissociate from DFFB, the active component of DFF. DFFB has been found to trigger both DNA fragmentation and chromatin condensation during apoptosis. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene but the biological validity of these variants has not been determined.
DNA fragmentation factor subunit beta
, DNA fragmentation factor, 40 kD, beta polypeptide
, DNA fragmentation factor, 40kDa, beta polypeptide (caspase-activated DNase)
, DNA fragmentation factor 40 kDa subunit
, caspase-activated DNase
, caspase-activated deoxyribonuclease
, caspase-activated nuclease
, DNA fragmentation factor 40 kD beta polypeptide (caspase-activated DNase)
, DNA fragmentation factor, 40 kD, beta polypeptide (caspase-activated DNase)
, DNA fragmentation factor, beta polypeptide (caspase-activated DNase)
, DNA fragmentation factor, beta subunit
, DNA fragmentation factor, 40 kD, beta subunit
, DNase inhibited by DNA fragmentation factor