Abstract:
:Inflammation and subsequent cyclooxygenase-2 (COX-2) activity has long been linked with the development of cancer, although little is known about any epigenetic effects of COX-2. A product of COX-2 activation, levuglandin (LG) quickly forms covalent bonds with nearby primary amines, such as those in lysine, which leads to LG-protein adducts. Here, we demonstrate that COX-2 activity causes LG-histone adducts in cultured cells and liver tissue, detectable through LC-MS, with the highest incidence in histone H4. Adduction is blocked by a γ-ketoaldehyde scavenger, which has no effect on COX-2 activity as measured by PGE2 production. Formation of the LG-histone adduct is associated with an increased histone solubility in NaCl, indicating destabilization of the nucleosome structure; this is also reversed with scavenger treatment. These data demonstrate that COX-2 activity can cause histone adduction and loosening of the nucleosome complex, which could lead to altered transcription and contribute to carcinogenesis.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Carrier EJ,Zagol-Ikapitte I,Amarnath V,Boutaud O,Oates JAdoi
10.1021/bi401673bsubject
Has Abstractpub_date
2014-04-22 00:00:00pages
2436-41issue
15eissn
0006-2960issn
1520-4995journal_volume
53pub_type
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