| Literature DB >> 29987187 |
Stanley B DeVore1, Coleman H Young1, Guangyuan Li1, Anitha Sundararajan2, Thiruvarangan Ramaraj2, Joann Mudge2, Faye Schilkey2, Aaron Muth3, Paul R Thompson3, Brian D Cherrington4.
Abstract
Peptidylarginine deiminase (PAD) enzymes convert histone arginine residues into citrulline to modulate chromatin organization and gene expression. Although PADs are expressed in anterior pituitary gland cells, their functional role and expression in pituitary adenomas are unknown. To begin to address these issues, we first examined normal human pituitaries and pituitary adenomas and found that PAD2, PAD4, and citrullinated histones are highest in prolactinomas and somatoprolactinomas. In the somatoprolactinoma-derived GH3 cell line, PADs citrullinate histone H3, which is attenuated by a pan-PAD inhibitor. RNA sequencing and chromatin immunoprecipitation (ChIP) studies show that the expression of microRNAs (miRNAs) let-7c-2, 23b, and 29c is suppressed by histone citrullination. Our studies demonstrate that these miRNAs directly target the mRNA of the oncogenes encoding HMGA, insulin-like growth factor 1 (IGF-1), and N-MYC, which are highly implicated in human prolactinoma/somatoprolactinoma pathogenesis. Our results are the first to define a direct role for PAD-catalyzed histone citrullination in miRNA expression, which may underlie the etiology of prolactinoma and somatoprolactinoma tumors through regulation of oncogene expression.Entities:
Keywords: citrullination; epigenetics; miRNA; oncogenes; prolactinoma
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Year: 2018 PMID: 29987187 PMCID: PMC6146832 DOI: 10.1128/MCB.00084-18
Source DB: PubMed Journal: Mol Cell Biol ISSN: 0270-7306 Impact factor: 4.272