Skip to main content
SpringerLink
Log in

Peptidylarginine Deiminase Enzymes

  • Living reference work entry
  • First Online:
Encyclopedia of Cancer

  • 136 Accesses

Synonyms

PADIs; PADs; Protein arginine deiminases

Definition

The PADs are a family of posttranslational modification enzymes that convert positively charged protein-bound arginine and methylarginine residues to neutrally charged, non-ribosomally encoded citrulline residues. This process is referred to as citrullination or alternatively as deimination.

Characteristics

Introduction

Citrullination of arginine and methylarginine residues by PAD enzymes affects the tertiary structure of target substrates and alters protein-protein interactions, impacting various cellular processes (Fig. 1). Protein citrullination has recently gained increased attention due to its proven role in the pathogenesis of various inflammatory conditions such as rheumatoid arthritis, multiple sclerosis, psoriasis, and COPD and emerging roles in various carcinomas in humans and animals. In this essay, we will discuss the tissue specificity of the five PAD isoforms and the potential role of this enzyme family in...

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution

Institutional subscriptions

References

  • Slack JL, Causey CP, Thompson PR (2011) Protein arginine deiminase 4: a target for an epigenetic cancer therapy. Cell Mol Life Sci 68:709–720

    Article  CAS  PubMed  Google Scholar 

  • Tanikawa C, Espinosa M, Suzuki A, Masuda K, Yamamoto K, Tsuchiya E, Ueda K, Daigo Y, Nakamura Y, Matsuda K (2012) Regulation of histone modification and chromatin structure by the p53-PADI4 pathway. Nat Commun 3:676

    Article  PubMed  Google Scholar 

  • Vossenaar ER, Zendman AJW, Van Venrooij WJ, Pruijn GJM (2003) PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease. Bioessays 25:1106–1118

    Article  CAS  PubMed  Google Scholar 

  • Wang Y, Wysocka J, Sayegh J, Lee YH, Perlin JR, Leonelli L, Sonbuchner LS, McDonald CH, Cook RG, Dou Y (2004) Human PAD4 regulates histone arginine methylation levels via demethylimination. Sci STKE 306:279

    CAS  Google Scholar 

  • Zhang X, Gamble MJ, Stadler S, Cherrington BD, Causey CP, Thompson PR, Roberson MS, Kraus WL, Coonrod SA (2011) Genome-wide analysis reveals PADI4 cooperates with Elk-1 to activate c-Fos expression in breast cancer cells. PLoS Genet 7, e1002112

    Article  CAS  PubMed  PubMed Central  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Baker Institute for Animal Health, Department of Biomedical Sciences, School of Veterinary Medicine, Cornell University, Ithaca, NY, USA

    Sunish Mohanan & Scott Coonrod

Authors
  1. Sunish Mohanan
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Scott Coonrod
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Sunish Mohanan .

Editor information

Editors and Affiliations

  1. Abt. Tumorgenetik, Deutsches Krebsforschungszentrum, Heidelberg, Germany

    Manfred Schwab

Rights and permissions

Reprints and permissions

Copyright information

© 2014 Springer-Verlag Berlin Heidelberg

About this entry

Cite this entry

Mohanan, S., Coonrod, S. (2014). Peptidylarginine Deiminase Enzymes. In: Schwab, M. (eds) Encyclopedia of Cancer. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-27841-9_7106-5

Download citation

  • DOI: https://doi.org/10.1007/978-3-642-27841-9_7106-5

  • Received:

  • Accepted:

  • Published:

  • Publisher Name: Springer, Berlin, Heidelberg

  • Online ISBN: 978-3-642-27841-9

  • eBook Packages: Springer Reference Biomedicine and Life SciencesReference Module Biomedical and Life Sciences

Publish with us

Policies and ethics

Search

Navigation