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This study demonstrated that the Cerebellar Abiotrophy associated single nucleotide polymorphism introduces a new binding site for a novel transcription factor (Myelin Transcription Factor-1 Like protein, MYT1L). and Cerebellar Abiotrophy-affected horses show differential expression of a specific isoform of MUTYH as well as different localization in the Purkinje and granular neurons of the cerebellum.
qPCR analysis of cDNA from the cerebella of affected and unaffected horses suggested that MUTYH expression is down-regulated in affected horses.
The MUTYH gene presents downregulation in the more advanced stages of colorectal cancer
MUTYH variants among Japanese colorectal polyposis patients.
Our results suggest that p.(Gly396Asp) in MUTYH, and potentially other mutations in additional members of the same DNA excision-repair pathway (such as the OGG1 gene) might be involved in driving the tumorigenesis leading to familial and sporadic small intestinal neuroendocrine tumors .
Knockdown of MYH in pancreatic cancer cells reduces tumor growth and sensitizes cells to antineoplastic agents.
Rheumatoid arthritis is associated with increased serum level of the MUTYH protein.
Inactivating MUTYH germline mutations are associated with high-grade midline gliomas.
this review focuses on multifaceted roles of MUTYH in the cell, both in the prevention of mutagenesis and tumorigenesis
Acetohexamide exerted this protective function by antagonizing expression of the DNA glycosylase, MUTYH. Together, our data reveal the existence of an NER-independent mechanism to remove UV-induced DNA damage and prevent cell death.
Data indicate that DNA glycosylases MYH, UNG2, MPG, NTH1, NEIL1, 2 and 3 on nascent DNA.
No biallelic mutation carriers for the MUTYH variants c.536A.G p.Tyr179Cys (Y179C) in exon 7 and c.1187G.A p.Gly396Asp (G396D) in exon 13 was found, after screening with a novel high resolution melt curve (HRM) analysis assay.
MUTYH p.Y179C mutation was associated with an increased risk of colorectal cancer among Egyptian patients rather than MUTYH p.G396D mutation.
The majority (18/23) of patients with Familial Adenomatous Polyposis and all of the patients with Attenuated Familial Adenomatous Polyposis with an Adrenal Lesion had a genetically proven syndrome.All of the patients with MUTYH-Associated Polyposis had a biallelic germline MUTYH mutation.
These results suggested that reduced MUTYH expression is associated with somatic mutation loads via a reduction in DNA repair capacity in prostate adenocarcinoma.
MTH1 together with MYH plays an important role in protection against mutations induced by modified dNTPs during chronic oxidative stress.
Reduced MUTYH, MTH1, and OGG1 expression and TP53 mutations occur in diffuse-type adenocarcinoma of gastric cardia.
Authors identified 266 probands (91% Caucasians) with a MUTYH mutation (41 biallelic and 225 monoallelic) from the Colon Cancer Family Registry. Mutation status, sex, age and histories of cancer from their 1,903 first- and 3,255 second-degree relatives were analyzed using modified segregation analysis conditioned on the ascertainment criteria.
A high heterogeneity of MUTYH variants and a high rate of variants of unknown significance were identified in a cohort of Italian patients with suspected MUTYH-associated polyposis. Genotype-phenotype analysis suggests that the p.Glu480del variant is associated with a severe phenotype.
Mutational signature analysis identifies MUTYH deficiency in colorectal cancers and adrenocortical carcinomas.
report of the results of functional evaluation of nine missense-type MUTYH variant proteins in the Japanese population; findingssuggest that p.N238S and p.R247G are likely to be pathogenic alleles for MUTYH-associated polyposis
Case Report: MUTYH-associated polyposis with cutaneous sebaceous lesions.
results suggested that MYH, which interacts with TRADD, inhibits TNF-alpha necroptotic signaling. Therefore, MYH inactivation is essential for necroptosis via the downregulation of caspase-8.
Ogg1 and Mutyh regulate hippocampal gene expression related to cognition and behavior, suggesting a role for the glycosylases in regulating adaptive behavior.
MUTYH loss is associated with an increase in inflammation associated colorectal cancer risk, which involves immunosuppression and altered inflammatory response.
Results show that MYH is a vital DNA repair enzyme that protects cells from oxidative DNA damage and is critical for a proper cellular response to DNA damage.
a 5-methylcytosine glycosylase activity for the murine DNA base excision repair enzyme Myh is described and shown that it is critically involved in remodeling the IL-2 Promoter for transcription.
Data indicate that maternal folate depletion during pregnancy and high-fat feeding from weaning altered gene expression of Ogg1, Neil1, Mutyh and Xrcc1 in the brain of adult offspring.
The action of MUTYH, which initiates excision repair of adenine opposite 8-oxoG, triggers neurodegeneration in mice.
OGG1 and MYH appear to be dispensable for antimutator function in mitochondria.
Mutyh plays a major role in maintaining intestinal integrity by affecting the inflammatory response.
Aim of this study was to characterize the biological effects, in a mammalian cell background, of human MUTYH mutations identified in MUTYH-associated polyposis patients
Replication-associated repair of adenine:8-oxoguanine mispairs by MYH
a specific germ-line mutation (G382D) is identified in mutyH which may be responsible for the mutator phenotype
MUTYHalpha and MUTYHbeta were detected in wild-type embryonic stem (ES) cells or thymocytes prepared from wild-type mice
The C-terminal domain of MUTYH is necessary for its ability to prevent OGG1 or APEX1 from inappropriately processing its substrate.
Because there is an increased incidence of lung and small intestine cancer in Myh(-/-)/Ogg1(-/-) mice, these findings support a causal role for unrepaired oxidized DNA bases in cancer development.
MUTYH has a DNA glycosylase activity excising not only adenine opposite 8-oxoguanine (8-oxoG) but also 2-hydroxyadenine (2-OH-A) opposite guanine.
MUTYH suppresses spontaneous tumorigenesis in mice, thus providing experimental evidence for the association between biallelic germ-line MUTYH mutations and a recessive form of human hereditary colorectal adenoma and carcinoma
Required for normal cell-cycle progression and nuclear division, suggesting multiple roles of Myh in the maintenance of genome stability and tumor prevention.
A large fraction of the cancer-prone phenotype of Msh2 deficient mice depends on Mutyh activity.
This gene encodes a DNA glycosylase involved in oxidative DNA damage repair. The enzyme excises adenine bases from the DNA backbone at sites where adenine is inappropriately paired with guanine, cytosine, or 8-oxo-7,8-dihydroguanine, a major oxidatively damaged DNA lesion. The protein is localized to the nucleus and mitochondria. Mutations in this gene result in heritable predisposition to colon and stomach cancer. Multiple transcript variants encoding different isoforms have been found for this gene.
mutY homolog (E. coli)
, A/G-specific adenine DNA glycosylase
, A/G-specific adenine DNA glycosylase-like
, mutY homolog
, adenine-DNA glycosylase
, mutY homolog alpha
, the full-length form type A, 5' region