University of Massachusetts Medical School Faculty Publications

Title

Peptidyl arginine deiminases: detection and functional analysis of protein citrullination

UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology; Thompson Lab

Publication Date

2019-03-01

Document Type

Article

Disciplines

Amino Acids, Peptides, and Proteins | Biochemical Phenomena, Metabolism, and Nutrition | Biochemistry | Enzymes and Coenzymes | Molecular Biology | Skin and Connective Tissue Diseases | Structural Biology

Abstract

Citrullination is a post-translational modification of arginine that is catalyzed by the protein arginine deiminases (PADs). Abnormal citrullination is observed in many autoimmune diseases and cancers. Anti-citrullinated protein antibodies (ACPA) are hallmarks of RA and used as diagnostic markers for disease diagnosis. Even though citrullination is associated with many different pathologies, its role remains unclear due to the challenges associated with the detection of citrullinated proteins since the mass change is only 0.984 Da. Moreover, the functional effects of protein citrullination remain mostly unknown. Herein, we discuss a brief overview of PAD structure and function, recent advances in the detection of citrullinated proteins in complex biological systems and the functional consequences of protein citrullination.

DOI of Published Version

10.1016/j.sbi.2019.01.024

Source

Curr Opin Struct Biol. 2019 Mar 1. pii: S0959-440X(19)30008-9. doi: 10.1016/j.sbi.2019.01.024. [Epub ahead of print] Link to article on publisher's site

Related Resources

Link to Article in PubMed

Journal/Book/Conference Title

Current opinion in structural biology

PubMed ID

30833201

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