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A mislocalization of the Wrn mutant protein in the liver endoplasmic reticulum fraction increased oxidative stress in that cellular compartment. Vitamin C reversed this oxidative stress.
The deleterious effects of the helicase-deficient Wrn protein are mediated by the dysfunction of several cellular organelles.
Data suggest that, in the context of Wrn deficiency-related telomere dysfunction, loss of p16Ink4a function could prevent cells from senescence.
The FEN1 E359K germline mutation disrupts the FEN1-WRN interaction and FEN1 GEN activity, causing aneuploidy-associated cancers.
Studies show that in the context of Myc-associated tumorigenesis, loss of Wrn amplifies the DNA damage response, both in preneoplastic and neoplastic tissue, engaging activation of tumor suppressor pathways.
embryonic fibroblasts lacking a functional Wrn helicase (show DNA2 ELISA Kits) inhibited the immortalization of Safb1 (show SAFB ELISA Kits)-null cells. These results indicate that an intact Wrn protein is required for immortalization and tumorigenesis in Safb1 (show SAFB ELISA Kits)-null mice.
BCR/ABL-mediated stimulation of WRN modulates the efficiency and fidelity of major DSB repair mechanisms to protect leukemia cells from apoptosis and to facilitate genomic instability.
WRN has a role in processing specific types of homologous recombination intermediates as well as an important function in nonhomologous recombination
results demonstrate that WRN loss confers a strong cellular phenotype in early passage human - though not mouse - primary fibroblasts.
Genetic cooperation between this protein and poly(ADP-ribose) polymerase-1 (show PARP1 ELISA Kits) prevent chromatid breaks, complex chromosomal rearrangements, and cancer in mice.
In meta-analyses including 59,190 individuals in 5 studies, the hazard ratio for ischemic stroke for C1367R TT homozygotes versus CC/CT was 1.14 . The study suggests that common genetic variation in WRN is associated with increased risk of ischemic stroke in the general population.
The findings suggest that the epidermis is among the tissue types that do not display symptoms of premature ageing caused by loss of function of wrn. This is in support that Werner's syndrome is a segmental progeroid syndrome.
Active control of repetitive structural transitions between replication forks and Holliday junctions by WRN has been reported.
Evaluation of localization of WRN signals demonstrated that WRN does not leave the nucleolus after irradiation. The WRN signal was not detected at the telomere sides, but H2AX was detected at the telomeric sides. Thus, the WRN protein is not involved in irradiation-induced DNA damage/repair, even at telomeric sides in human mesenchymal stem cells (hMSC) and hMSC-telomere 1.
In humans, mutations in WRN give rise to Werner syndrome characterized by premature development of features associated with aging.
Werner syndrome is a prototypical segmental progeroid syndrome characterized by multiple features consistent with accelerated aging. It is caused by null mutations of the WRN gene, which encodes a member of the RECQ family of DNA helicases.
Our results identify the human WRN RECQ protein as a G4 helicase that modulates gene expression in G4-dependent fashion at many chromosomal sites and provide several new and unexpected mechanistic insights into Werner syndrome (WS) disease pathogenesis
WRN or the Bloom syndrome helicase (BLM) stimulates DNA polymerase delta (show POLD1 ELISA Kits) progression across telomeric G-rich repeats, only WRN promotes sequential strand displacement synthesis and FEN1 (show FEN1 ELISA Kits) cleavage.
This study identified residues in the WRN RQC domain that are involved specifically in the interaction with G-quadruplex DNA.
findings indicate that WRN interacts with HDACs 1 and 2 to facilitate activity of stalled replication forks under conditions of replication stress.
This gene encodes a member of the RecQ subfamily and the DEAH (Asp-Glu-Ala-His) subfamily of DNA and RNA helicases. DNA helicases are involved in many aspects of DNA metabolism, including transcription, replication, recombination, and repair. This protein contains a nuclear localization signal in the C-terminus and shows a predominant nucleolar localization. It possesses an intrinsic 3' to 5' DNA helicase activity, and is also a 3' to 5' exonuclease. Based on interactions between this protein and Ku70/80 heterodimer in DNA end processing, this protein may be involved in the repair of double strand DNA breaks. Defects in this gene are the cause of Werner syndrome, an autosomal recessive disorder characterized by premature aging.
, Werner syndrome ATP-dependent helicase homolog
, exonuclease WRN
, DNA helicase, RecQ-like type 3
, Werner syndrome ATP-dependent helicase
, recQ protein-like 2