PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease
- PMID: 14579251
- DOI: 10.1002/bies.10357
PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease
Abstract
Peptidylarginine deiminase (PAD, EC 3.5.3.15) enzymes catalyze the conversion of protein-bound arginine to citrulline. This post-translational modification may have a big impact on the structure and function of the target protein. In this review, we will discuss the effects of citrullination and its involvement in several human diseases, including rheumatoid arthritis and multiple sclerosis. So far, four isotypes of PAD have been described in mammals. We describe the existence of PAD in non-mammalian vertebrates and the existence of a fifth mammalian PAD. In addition, tissue-specific expression, genomic organization and evolutionary conservation of the different PAD isotypes will be discussed in detail. This article contains supplementary material which may be viewed at the BioEssays website at http://www.interscience.wiley.com/jpages/0265-9247/suppmat/2003/25/v25.1106.html.
Copyright 2003 Wiley Periodicals, Inc.
Similar articles
-
Transcriptional regulation of peptidylarginine deiminase expression in human keratinocytes.J Dermatol Sci. 2009 Jan;53(1):2-9. doi: 10.1016/j.jdermsci.2008.09.009. Epub 2008 Nov 11. J Dermatol Sci. 2009. PMID: 19004619 Review.
-
Peptidyl arginine deiminase type 2 (PAD-2) and PAD-4 but not PAD-1, PAD-3, and PAD-6 are expressed in rheumatoid arthritis synovium in close association with tissue inflammation.Arthritis Rheum. 2007 Nov;56(11):3541-53. doi: 10.1002/art.22983. Arthritis Rheum. 2007. PMID: 17968929
-
Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6.Gene. 2004 Apr 14;330:19-27. doi: 10.1016/j.gene.2003.12.038. Gene. 2004. PMID: 15087120
-
Peptidylarginine deiminase 4 and citrullination in health and disease.Autoimmun Rev. 2010 Jan;9(3):158-60. doi: 10.1016/j.autrev.2009.06.002. Epub 2009 Jun 18. Autoimmun Rev. 2010. PMID: 19540364 Review.
-
Kinetics of human peptidylarginine deiminase 2 (hPAD2)--reduction of Ca2+ dependence by phospholipids and assessment of proposed inhibition by paclitaxel side chains.Biochem Cell Biol. 2008 Oct;86(5):437-47. doi: 10.1139/o08-124. Biochem Cell Biol. 2008. PMID: 18923545
Cited by
-
Peptidylarginine deiminase enzymes and citrullinated proteins in female reproductive physiology and associated diseases†.Biol Reprod. 2022 Dec 10;107(6):1395-1410. doi: 10.1093/biolre/ioac173. Biol Reprod. 2022. PMID: 36087287 Free PMC article. Review.
-
Reduced glutathione as a physiological co-activator in the activation of peptidylarginine deiminase.Arthritis Res Ther. 2016 May 5;18(1):102. doi: 10.1186/s13075-016-1000-7. Arthritis Res Ther. 2016. PMID: 27149996 Free PMC article.
-
PAD4-dependent citrullination of nuclear translocation of GSK3β promotes colorectal cancer progression via the degradation of nuclear CDKN1A.Neoplasia. 2022 Nov;33:100835. doi: 10.1016/j.neo.2022.100835. Epub 2022 Sep 13. Neoplasia. 2022. PMID: 36113195 Free PMC article.
-
Histone citrullination: a new target for tumors.Mol Cancer. 2021 Jun 11;20(1):90. doi: 10.1186/s12943-021-01373-z. Mol Cancer. 2021. PMID: 34116679 Free PMC article. Review.
-
Deimination restores inner retinal visual function in murine demyelinating disease.J Clin Invest. 2013 Feb;123(2):646-56. doi: 10.1172/JCI64811. Epub 2013 Jan 2. J Clin Invest. 2013. PMID: 23281397 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Research Materials
