Induction of peptidylarginine deiminase 2 and 3 by dibutyryl cAMP via cAMP-PKA signaling in human astrocytoma U-251MG cells

摘要: Peptidylarginine deiminases (PADs) are posttranslational modification enzymes that citrullinate (deiminate) protein arginine residues in a calcium-dependent manner, yielding citrulline residues. Enzymatic citrullination abolishes positive charges of native molecules, inevitably causing significant alterations their structure and function. Previously, we reported the abnormal accumulation citrullinated proteins an increase PAD2 content hippocampi patients with Alzheimer disease. In this study, investigated PAD expression by using dibutyryl cAMP (dbcAMP) human astrocytoma U-251MG cells. Under normal culture conditions, PAD3 mRNA is detectable quantitative PCR The addition dbcAMP dose-dependent manner significantly increased levels. Moreover, enzyme activity also dose-dependently. Furthermore, was inhibited cAMP-dependent PKA inhibitor KT5720, suggesting such dbcAMP-induced mediated cAMP-PKA signaling pathway This first report to document induced attribute induction these genes mediation © 2016 Wiley Periodicals, Inc.