2014年9月24日星期三

Regulation and dysregulation of MUTYH

The researchers used qualitative and quantitative methods to explore MUTYH. In the study, MUTYH is a human gene encoding a DNA glycosylase, MUTYH 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, a major oxidatively damaged DNA lesion. MUTYH is localized to the nucleus and mitochondria. Mutations result in heritable predisposition to colon and stomach cancer.


Mutations in the MUTYH cause an autosomal recessive form of familial adenomatous polyposis. Polyps caused by mutated MUTYH do not appear until adulthood and are less numerous than those found in patients with APC gene mutations.
Mutations in MUTYH affect the ability of cells to correct mistakes made during DNA replication. Both copies of the MYH are mutated in individuals who have autosomal recessive familial adenomatous polyposis. Most reported mutations in MUTYH( www.cusabio.com/cusabio-1086635/ ) cause production of a nonfunctional or low functioning glycosylase enzyme. When base excision repair in the cell is compromised, mutations in other genes build up, leading to cell overgrowth and possibly tumor formation. The two most common mutations in Caucasian Europeans are exchanges of amino acids in the enzyme.

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