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

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.

journal_name

Curr Drug Targets

journal_title

Current drug targets

authors

Witalison EE,Thompson PR,Hofseth LJ

doi

10.2174/1389450116666150202160954

subject

Has Abstract

pub_date

2015-01-01 00:00:00

pages

700-10

issue

7

eissn

1389-4501

issn

1873-5592

pii

CDT-EPUB-64947

journal_volume

16

pub_type

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