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Protein Arginine Deiminases and Associated Citrullination: Physiological Functions and Diseases Associated with Dysregulation

[ Vol. 16 , Issue. 7 ]

Author(s):

Erin E. Witalison, Paul R. Thompson and Lorne J. Hofseth   Pages 700 - 710 ( 11 )

Abstract:


Human proteins are subjected to more than 200 known post-translational modifications (PTMs) (e.g., phosphorylation, glycosylation, ubiquitination, S-nitrosylation, methylation, Nacetylation, and citrullination) and these PTMs can alter protein structure and function with consequent effects on the multitude of pathways necessary for maintaining the physiological homeostasis. When dysregulated, however, the enzymes that catalyze these PTMs can impact the genesis of countless diseases. In this review, we will focus on protein citrullination, a PTM catalyzed by the Protein Arginine Deiminase (PAD) family of enzymes. Specifically, we will describe the roles of the PADs in both normal human physiology and disease. The development of PAD inhibitors and their efficacy in a variety of autoimmune disorders and cancer will also be discussed.

Keywords:

Apoptosis, autoimmune disease, citrullination, gene regulation, inflammatory disease, protein arginine deiminases.

Affiliation:

Department of Drug Discovery and Biomedical Sciences, South Carolina College of Pharmacy, 770 Sumter St., Coker Life Sciences, Rm. 513C, University of South Carolina, Columbia, SC 29208, USA.

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