Bacterial and human peptidylarginine deiminases: targets for inhibiting the autoimmune response in rheumatoid arthritis?
Open accessAbstract
Peptidylarginine deiminases (PADs) convert arginine within a peptide (peptidylarginine) into peptidylcitrulline. Citrullination by human PADs is important in normal physiology and inflammation. Porphyromonas gingivalis, a major pathogen in periodontitis, is the only prokaryote described to possess PAD. P. gingivalis infection may generate citrullinated peptides, which trigger anti-citrullinated peptide antibodies. In susceptible individuals, host protein citrullination by human PADs in the joint probably perpetuates antibody formation, paving the way for the development of chronic arthritis. Blockades of bacterial and human PADs may act as powerful novel therapies by inhibiting the generation of the antigens that trigger and sustain autoimmunity in rheumatoid arthritis.
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Cites
Socransky, S. S., & Haffajee, A. D. (2005) · Periodontology 2000 · doi:10.1111/j.1600-0757.2005.00107.x · Cited by 1,691 · see citing works
McGraw, W. T., Potempa, J., Farley, D., & Travis, J. (1999) · Infection and Immunity · doi:10.1128/iai.67.7.3248-3256.1999 · Cited by 378 · cited 10× · see citing works
“Th e localization and functions of each of the human PAD enzymes are summarized in Table 1. Homologous amino acid sequences for some or all of these PADs exist in other eukaryotic species, such as the mouse, chicken, frog, and bony fi sh. Among prokaryotic species, PAD activity has, to date, been described in Porphyro…”
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Bingham, C. O., & Moni, M. (2013) · Current Opinion in Rheumatology · doi:10.1097/bor.0b013e32835fb8ec · Cited by 174 · see citing works
Atanasova, K. R., & Yilmaz, Ö. (2014) · Molecular Oral Microbiology · doi:10.1111/omi.12047 · Cited by 129 · see citing works
Kriebel, K., Hieke, C., Müller-Hilke, B., Nakata, M., & Kreikemeyer, B. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.00053 · Cited by 118 · see citing works
- Authors
- Mangat, P., Wegner, N., Venables, P. J., & Potempa, J.
- Affiliations
- Kennedy Institute of Rheumatology (GB)
- Jagiellonian University (PL)
- Corresponding author
- Venables, Patrick J
- ORCID
- Potempa, Jan
- Venue
- Arthritis Research & Therapy
- Published
- 2010
- Volume
- 12
- Issue
- 3
- Pages
- 209
- ISSN
- 1478-6354 (ISSN-L)
- PMC
- PMC2911857
- OpenAlex
- W2124631347
- Cited by
- 111
- References
- 2
- Citations by year
- 2025: 8 · 2024: 3 · 2023: 5 · 2022: 4 · 2021: 9 · 2020: 8 · 2019: 11 · 2018: 13 · 2017: 7 · 2016: 5 · 2015: 2 · 2014: 10 · 2013: 11 · 2012: 10
- FWCI
- 1.09
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Arthritis Research & Therapy (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Commission (POIG.02.01.00-12-064/08)
- Versus Arthritis
- National Institutes of Health
- U.S. Public Health Service (1642/B/P01/2008/35)
- National Institute of Dental and Craniofacial Research (R01DE009761, DE09761)
- Topics
- Health Sciences › Medicine › Rheumatology › Rheumatoid Arthritis Research and Therapies
- Health Sciences › Medicine › Complementary and alternative medicine › Natural Compounds in Disease Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Keywords
- peptidylarginine deiminase, citrullination, rheumatoid arthritis, Porphyromonas gingivalis, anti-citrullinated protein antibodies, autoimmunity, periodontitis, PAD inhibitors, citrullinated peptides
- MeSH terms
- Protein-Arginine Deiminases, Amino Acid Sequence, Animals, Arthritis, Rheumatoid, Humans, Hydrolases, Molecular Sequence Data, Periodontitis, Risk Factors, Autoimmunity, Porphyromonas gingivalis
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