抗ETS1 associated protein II [FITC]抗体 | Anti- ETS1 associated protein II [FITC] antibody

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Background

Tyrosyl DNA phosphodiesterase-2 (TDP2) activity involves TRAF and TNF receptor-associated protein (TTRAP), which are 5'-tyrosyl DNA phosphodiesterase (5'-TDP) that can cleave 5'-phosphotyrosyl bonds, which can be denoted as previously mentioned TDP2.(1) Topoisomerase II (Top2) activity involves these intermediaries which the topoisomerase is covalently bound to a DNA double-strand via 5'posphotyrsyl bond. These intermediates are normally transient; they can be stabilized by anti-tumor agents that act as Top2 poisons resulting in the induction of cytotoxic double-strand breaks. And they are implicated in the formation of site-specific translocations that are commonly associated with cancer patterns. Topoisomerases regulate DNA topology and play a key role to many aspects of chromosome metabolism. Their actions include transient cleavage of DNA, which if it occurs around sites of endogenous DNA damage or in the presence of topoisermase poisons, can resulting in abortive topoisomerase-induced DNA strand breaks (2). These breaks possess covalent linkage of the enzyme to the DNA termini by a 3' or 5'- phosphotyrosyl bond and are implicated in hereditary human disease, chromosomal instability and cancer. (2). It has been shown that TDP2-delete DT40 cells are highly sensitive to anticancer Top2 poison, etoposide, but are not hypersensitive to the Top 1 poison camptothecin, or the DNA-alkyating agent, methyl methanesulfonate. These results support an important mechanism for resistance to Top2-induced chromosome breakage and raise the likelihood that TDP2 is a significant factor in cancer development and treatment (1). The significance of liberating DNA termini from trapped topisomerase is shown by the progressive neurodegenerative disease observed in individuals possessing the mutation in tyrosyl-DNA phosodiesterase 1 (TDP1). A complementary human enzyme that cleaves 5'-phosphotyrosyl bonds has not been reported. An enzyme TTRAP a member of the Mg(2+)/Mn(2+)dependent family of phospdiesterases, whose cellular results in increased sensitivity toward topoisomerase-ii-induced DNA double strand breaks. TTRAP therefore is the first human 5'-tyrosyl DNA phophodiesterase to be identified, and it is suggested that this enzyme is denoted tyrosyl DNA phosphopdiesterease-2 (2).

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