Citrullination under physiological and pathological conditions

Joint Bone Spine

Volumn 79, Issue 5, 2012, Pages 431-436

  Baka, Zsuzsanna ^a   György, Bence ^a   Géher, Pál ^a   Buzás, Edit I ^a   Falus, András ^a   Nagy, György ^a  

^a SEMMELWEIS UNIVERSITY   (Hungary)

Author keywords

Anti citrullinated protein antibodies; Citrullination; Gene regulation; Peptidylarginine deiminase; Rheumatoid arthritis; Smoking; Tumorigenesis

Indexed keywords

AMIDINE; CHEMOKINE RECEPTOR CXCR3; CHEMOKINE RECEPTOR CXCR4; CXCL11 CHEMOKINE; CYCLIC CITRULLINATED PEPTIDE ANTIBODY; ESTROGEN; FILAGGRIN; GAMMA INTERFERON INDUCIBLE PROTEIN 10; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE 2; HISTONE H3; HISTONE H4; HLA DRB1 ANTIGEN; HYDROLASE INHIBITOR; INTERLEUKIN 8; KERATIN; NON RECEPTOR PROTEIN TYROSINE PHOSPHATASE 22; PROTEIN ARGININE DEIMINASE; PROTEIN ARGININE DEIMINASE INHIBITOR; PROTEIN ARGININE METHYLTRANSFERASE; PROTEIN P53; TRICHOSTATIN A; UNCLASSIFIED DRUG;

BINDING SITE; CARCINOGENESIS; CELL DIFFERENTIATION; CENTRAL NERVOUS SYSTEM; CITRULLINATION; CONFORMATIONAL TRANSITION; ENVIRONMENTAL FACTOR; FUNCTIONS OF THE SKIN AND ITS APPENDAGES; GENE CONTROL; HALF LIFE TIME; HISTONE METHYLATION; HUMAN; INNATE IMMUNITY; KERATINIZATION; KERATINOCYTE; LYMPHOCYTE ACTIVATION; MULTIPLE SCLEROSIS; NERVE CELL PLASTICITY; NONHUMAN; PORPHYROMONAS GINGIVALIS; PROTEIN BINDING; PROTEIN CLEAVAGE; PROTEIN CROSS LINKING; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PROCESSING; PSORIASIS; RHEUMATOID ARTHRITIS; SHORT SURVEY; SMOKING;

ARTHRITIS, RHEUMATOID; CELL TRANSFORMATION, NEOPLASTIC; CENTRAL NERVOUS SYSTEM; CITRULLINE; GENE EXPRESSION REGULATION; HUMANS; IMMUNE SYSTEM; MULTIPLE SCLEROSIS; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEINS; PSORIASIS; SKIN PHYSIOLOGICAL PHENOMENA;

EID: 84867985009     PISSN: 1297319X     EISSN: 17787254     Source Type: Journal    
DOI: 10.1016/j.jbspin.2012.01.008     Document Type: Short Survey

References (62)

1. Diaz F.J., Rojas-Villarraga A., Salazar J.C., et al. Anti-CCP antibodies are associated with early age at onset in patients with rheumatoid arthritis. Joint Bone Spine 2011, 78:175-178.
2. Vossenaar E.R., Zendman A.J., van Venrooij W.J., et al. PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease. Bioessays 2003, 25:1106-1118.
3. Chang X., Han J. Expression of peptidylarginine deiminase type 4 (PAD4) in various tumors. Mol Carcinog 2006, 45:183-196.
4. Foulquier C., Sebbag M., Clavel C., et al. 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, 56:3541-4353.
5. Berthelot J.M., Le Goff B. Rheumatoid arthritis and periodontal disease. Joint Bone Spine 2010, 77:537-541.
6. György B., Tóth E., Tarcsa E., et al. Citrullination: a posttranslational modification in health and disease. Int J Biochem Cell Biol 2006, 38:1662-1677.
7. Union A., Meheus L., Humbel R.L., et al. Identification of citrullinated rheumatoid arthritis-specific epitopes in natural filaggrin relevant for antifilaggrin autoantibody detection by line immunoassay. Arthritis Rheum 2002, 46:1185-1195.
8. Masson-Bessière C., Sebbag M., Girbal-Neuhauser E., et al. The major synovial targets of the rheumatoid arthritis-specific antifilaggrin autoantibodies are deiminated forms of the alpha- and beta-chains of fibrin. J Immunol 2001, 166:4177-4184.
9. Wang Y., Wysocka J., Sayegh J., et al. Human PAD4 regulates histone arginine methylation levels via demethylimination. Science 2004, 306:279-283.
10. Tanikawa C., Ueda K., Nakagawa H., et al. Regulation of protein Citrullination through p53/PADI4 network in DNA damage response. Cancer Res 2009, 69:8761-8879.
11. Liu G.Y., Liao Y.F., Chang W.H., et al. Overexpression of peptidylarginine deiminase IV features in apoptosis of haematopoietic cells. Apoptosis 2006, 11:183-196.
12. Yao H., Li P., Venters B.J., et al. Histone Arg modifications and p53 regulate the expression of OKL38, a mediator of apoptosis. J Biol Chem 2008, 283:20060-20068.
13. Li P., Yao H., Zhang Z., et al. Regulation of p53 target gene expression by peptidylarginine deiminase 4. Mol Cell Biol 2008, 28:4745-4758.
14. Li P., Wang D., Yao H., et al. Coordination of PAD4 and HDAC2 in the regulation of p53-target gene expression. Oncogene 2010, 29:3153-3162.
15. Guo Q., Fast W. Citrullination of inhibitor of growth 4 (ING4) by peptidylarginine deminase 4 (PAD4) disrupts the interaction between ING4 and p53. J Biol Chem 2011, 286:17069-17078.
16. Dong S., Zhang Z., Takahara H. Estrogen-enhanced peptidylarginine deiminase type IV gene (PADI4) expression in MCF-7 cells is mediated by estrogen receptor-alpha-promoted transfactors activator protein-1, nuclear factor-Y, and Sp1. Mol Endocrinol 2007, 21:1617-1629.
17. Denis H., Deplus R., Putmans P., et al. Functional connection between deimination and deacetylation of histones. Mol Cell Biol 2009, 29:4982-4993.
18. Brinkmann V., Reichard U., Goosmann C., et al. Neutrophil extracellular traps kill bacteria. Science 2004, 303:1532-1535.
19. Li P., Li M., Lindberg M.R., et al. PAD4 is essential for antibacterial innate immunity mediated by neutrophil extracellular traps. J Exp Med 2010, 207:1853-1862.
20. Lee H.J., Joo M., Abdolrasulnia R., et al. Peptidylarginine deiminase 2 suppresses inhibitory {kappa}B kinase activity in lipopolysaccharide-stimulated RAW 264.7 macrophages. J Biol Chem 2010, 285:39655-43962.
21. Proost P., Loos T., Mortier A., et al. Citrullination of CXCL8 by peptidylarginine deiminase alters receptor usage, prevents proteolysis, and dampens tissue inflammation. J Exp Med 2008, 205:2085-2097.
22. Loos T., Opdenakker G., Van Damme J., et al. Citrullination of CXCL8 increases this chemokine's ability to mobilize neutrophils into the blood circulation. Haematologica 2009, 94:1346-1353.
23. Struyf S., Noppen S., Loos T., et al. Citrullination of CXCL12 differentially reduces CXCR4 and CXCR7 binding with loss of inflammatory and anti-HIV-1 activity via CXCR4. J Immunol 2009, 182:666-674.
24. Mastronardi F.G., Wood D.D., Mei J., et al. Increased citrullination of histone H3 in multiple sclerosis brain and animal models of demyelination: a role for tumor necrosis factor-induced peptidylarginine deiminase 4 translocation. J Neurosci 2006, 26:11387-11396.
25. Alenius G.M., Berglin E., Rantapää Dahlqvist S. Antibodies against cyclic citrullinated peptide (CCP) in psoriatic patients with or without joint inflammation. Ann Rheum Dis 2006, 65:398-400.
26. Moscarello M.A., Wood D.D., Ackerley C., et al. Myelin in multiple sclerosis is developmentally immature. J Clin Invest 1994, 94:146-154.
27. Mastronardi F.G., Noor A., Wood D.D., et al. Peptidyl argininedeiminase 2 CpG island in multiple sclerosis white matter is hypomethylated. J Neurosci Res 2007, 85:2006-2016.
28. Raijmakers R., Vogelzangs J., Raats J., et al. Experimental autoimmune encephalomyelitis induction in peptidylarginine deiminase 2 knockout mice. J Comp Neurol 2006, 498:217-226.
29. Musse A.A., Li Z., Ackerley C.A., et al. Peptidylarginine deiminase 2 (PAD2) overexpression in transgenic mice leads to myelin loss in the central nervous system. Dis Model Mech 2008, 1:229-240.
30. Deraos G., Chatzantoni K., Matsoukas M.T., et al. Citrullination of linear and cyclic altered peptide ligands from myelin basic protein (MBP[87-99]) epitope elicits a Th1-polarized response by T cells isolated from multiple sclerosis patients: implications in triggering disease. J Med Chem 2008, 51:7834-7842.
31. Bodil Roth E., Theander E., Londos E., et al. Pathogenesis of autoimmune diseases: antibodies against transglutaminase, peptidylarginine deiminase and protein-bound citrulline in primary Sjögren's syndrome, multiple sclerosis and Alzheimer's disease. Scand J Immunol 2008, 67:626-631.
32. Baka Z., Barta P., Losonczy G., et al. Specific expression of PAD4 and citrullinated proteins in lung cancer is not associated with anti-CCP antibody production. Int Immunol 2011, 23:405-414.
33. Chang X., Han J., Pang L., et al. Increased PADI4 expression in blood and tissues of patients with malignant tumors. BMC Cancer 2009, 9:40.
34. Slack J.L., Causey C.P., Thompson P.R. Protein arginine deiminase 4: a target for an epigenetic cancer therapy. Cell Mol Life Sci 2011, 68:709-720.
35. Omary M.B., Ku N.O., Liao J., et al. Keratin modifications and solubility properties in epithelial cells and in vitro. Subcell Biochem 1998, 31:105-140.
36. Ordóńez A., Martínez-Martínez I., Corrales F.J., et al. Effect of citrullination on the function and conformation of antithrombin. FEBS 2009, 276:6763-6772.
37. Gregersen P.K., Silver J., Winchester R.J. The shared epitope hypothesis. An approach to understanding the molecular genetics of susceptibility to rheumatoid arthritis. Arthritis Rheum 1987, 30:1205-1213.
38. Gregersen P.K. Pathways to gene identification in rheumatoid arthritis: PTPN22 and beyond. Immunol Rev 2005, 204:74-86.
39. Scott D.L., Wolfe F., Huizinga T.W. Rheumatoid arthritis. Lancet 2010, 376:1094-1108.
40. Xuzhu G., Komai-Koma M., Leung B.P., et al. Resveratrol modulates murine collagen-induced arthritis by inhibiting Th17 and B-cell function. Ann Rheum Dis 2012, 71:129-135.
41. Baka Z., Buzás E., Nagy G. Rheumatoid arthritis and smoking: putting the pieces together. Arthritis Res Ther 2009, 11:238.
42. Klareskog L., Stolt P., Lundberg K., et al. A new model for an etiology of rheumatoid arthritis: smoking may trigger HLA-DR (shared epitope)-restricted immune reactions to autoantigens modified by citrullination. Arthritis Rheum 2006, 54:38-46.
43. Lee D.M., Phillips R., Hagan E.M., et al. Quantifying anti-cyclic citrullinated peptide titres: clinical utility and association with tobacco exposure in patients with rheumatoid arthritis. Ann Rheum Dis 2009, 68:201-208.
44. Makrygiannakis D., Hermansson M., Ulfgren A.K., et al. Smoking increases peptidylarginine deiminase 2 enzyme expression in human lungs and increases citrullination in BAL cells. Ann Rheum Dis 2008, 67:1488-1492.
45. Willemze A., van der Woude D., Ghidey W., et al. The interaction between HLA shared epitope alleles and smoking and its contribution to autoimmunity against several citrullinated antigens. Arthritis Rheum 2011, 63:1823-1832.
46. Bergström U., Jacobsson L.T., Nilsson Jå, et al. Pulmonary dysfunction, smoking, socioeconomic status and the risk of developing rheumatoid arthritis. Rheumatology (Oxford) 2011, 50:2005-2013.
47. Mikuls T.R., Payne J.B., Reinhardt R.A., et al. Antibody responses to Porphyromonas gingivalis (P. gingivalis) in subjects with rheumatoid arthritis and periodontitis. Int Immunopharmacol 2009, 9:38-42.
48. Wegner N., Wait R., Sroka A., et al. Peptidylarginine deiminase from Porphyromonas gingivalis citrullinates human fibrinogen and a-enolase: implications for autoimmunity in rheumatoid arthritis. Arthritis Rheum 2010, 62:2662-2672.
49. Lundberg K., Kinloch A., Fisher B.A., et al. Antibodies to citrullinated alpha-enolase peptide 1 are specific for rheumatoid arthritis and cross-react with bacterial enolase. Arthritis Rheum 2008, 58:3009-3019.
50. Kinloch A., Lundberg K., Wait R., et al. Synovial fluid is a site of citrullination of autoantigens in inflammatory arthritis. Arthritis Rheum 2008, 58:2287-2295.
51. Kinloch A.J., Alzabin S., Brintnell W., et al. Immunisation with Porphyromonas gingivalis enolase induces autoimmunity to mammalian a-enolase and arthritis in DR4-IE transgenic mice. Arthritis Rheum 2011, 63:3818-3823.
52. James E.A., Moustakas A.K., Bui J., et al. HLA-DR1001 presents "altered-self" peptides derived from joint-associated proteins by accepting citrulline in three of its binding pockets. Arthritis Rheum 2010, 62:2909-2918.
53. Hill J.A., Southwood S., Sette A., et al. Cutting edge: the conversion of arginine to citrulline allows for a high-affinity peptide interaction with the rheumatoid arthritis associated HLA-DRB10401 MHC class II molecule. J Immunol 2003, 171:538-541.
54. Dumonde D.C., Glynn L.E. The production of arthritis in rabbits by an immunological reaction to fibrin. Br J Exp Pathol 1962, 43:373-383.
55. Snir O., Widhe M., von Spee C., et al. Multiple antibody reactivities to citrullinated antigens in sera from patients with rheumatoid arthritis: association with HLA-DRB1 alleles. Ann Rheum Dis 2009, 68:736-743.
56. Zhao X., Okeke N.L., Sharpe O., et al. Circulating immune complexes contain citrullinated fibrinogen in rheumatoid arthritis. Arthritis Res Ther 2008, 10:R94.
57. Hill J.A., Bell D.A., Brintnell W., et al. Arthritis induced by posttranslationally modified (citrullinated) fibrinogen in DR4-IE transgenic mice. J Exp Med 2008, 205:967-979.
58. Duplan V., Foulquier C., Clavel C., et al. In the rat, citrullinated autologous fibrinogen is immunogenic but the induced autoimmune response is not arthritogenic. Clin Exp Immunol 2006, 145:502-512.
59. Lundberg K., Nijenhuis S., Vossenaar E.R., et al. Citrullinated proteins have increased immunogenicity and arthritogenicity and their presence in arthritic joints correlates with disease severity. Arthritis Res Ther 2005, 7:R458-R467.
60. Mangat P., Wegner N., Venables P.J., et al. Bacterial and human peptidylarginine deiminases: targets for inhibiting the autoimmune response in rheumatoid arthritis?. Arthritis Res Ther 2010, 12:209.
61. Willis V.C., Gizinski A.M., Banda N.K., et al. N-a-benzoyl-N5-(2-chloro-1-iminoethyl)-L-ornithine amide, a protein arginine deiminase inhibitor, reduces the severity of murine collagen-induced arthritis. J Immunol 2011, 186:4396-4404.
62. Jüngel A., Baresova V., Ospelt C., et al. Trichostatin A sensitises rheumatoid arthritis synovial fibroblasts for TRAIL-induced apoptosis. Ann Rheum Dis 2006, 65:910-912.