Open AccessNicotinamide N-Methyltransferase Suppression Participates in Nickel-Induced Histone H3 Lysine9 Dimethylation in BEAS-2B Cells
Author(s) -
Qian Li,
Mindi He,
Lin Mao,
Xue Wang,
Yulin Jiang,
Min Li,
Yonghui Lu,
Zhengping Yu,
Zhou Zhou
Publication year - 2017
Publication title -
cellular physiology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.486
H-Index - 87
eISSN - 1421-9778
pISSN - 1015-8987
DOI - 10.1159/000475432
Subject(s) - nad+ kinase , chemistry , nicotinamide , methyltransferase , methylation , histone h3 , histone , microbiology and biotechnology , acetylation , dna methylation , biochemistry , gene expression , enzyme , biology , dna , gene
Nickel compounds are well-established human carcinogens with weak mutagenic activity. Histone methylation has been proposed to play an important role in nickel-induced carcinogenesis. Nicotinamide N-methyltransferase (NNMT) decreases histone methylation in several cancer cells by altering the cellular ratio of S-adenosylmethionine (SAM) to S-adenosylhomocysteine (SAH). However, the role of NNMT in nickel-induced histone methylation remains unclear.