Witalison Erin E, Thompson Paul R, Hofseth Lorne J
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.
Curr Drug Targets. 2015;16(7):700-10. doi: 10.2174/1389450116666150202160954.
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.
人类蛋白质会经历200多种已知的翻译后修饰(PTM)(例如磷酸化、糖基化、泛素化、S-亚硝基化、甲基化、N-乙酰化和瓜氨酸化),这些PTM可改变蛋白质结构和功能,进而影响维持生理稳态所需的众多途径。然而,当这些过程失调时,催化这些PTM的酶会影响无数疾病的发生。在本综述中,我们将聚焦于蛋白质瓜氨酸化,这是一种由蛋白质精氨酸脱亚氨酶(PAD)家族酶催化的PTM。具体而言,我们将描述PAD在正常人体生理和疾病中的作用。还将讨论PAD抑制剂的开发及其在多种自身免疫性疾病和癌症中的疗效。