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中国生物工程杂志

China Biotechnology
China Biotechnology  2011, Vol. 31 Issue (9): 103-108    DOI:
    
Peptidylarginine Deiminase 4 Affects Pathogenesis and Development of Rheumatoid Arthrisits
LIU Xiao-shuai, GE Lu-na, HAN Jin-xiang, CHANG Xiao-tian, ZHU You-ming, WANG Shi-li
Shandong Medicinal Biotechnology Centre,Key Laboratory for Biotech-Drugs Ministry of Health,Key Laboratory for Rare & Uncommon Diseases of Shandong Province,Shandong Academy of Medical Sciences, Jinan 250062, China
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Abstract  

Rheumatoid arthrisits(RA) is a systemic autoimmune disease that exact pathogeny is unknown. Generally speaking, the pathogenic factors of RA are due to environmental factors and genetic factors. In genetic factors histocompatibility leukocyte antigen(HLA) is one of the most important elements. In addition, peptidylarginine deiminase 4 (PADI4) which does not belong to HLA has been thought to participate in the development of RA recently. PADI4 can catalyse peptidylarginine to citrulline in the presence of Ca2+. This action leads to posttranslational modification of protein. Citrullination brings to conformation change in peptide chains and active sites transformation. In various population, the relation between the SNP which located in PADI4 gene and pothogenesy of RA is different. PADI4 is up-regulated in RA patient’s blood serum and results in autoimmune antibody. PADI4 also citrullinates various protein induced autoimmune response which contributes to the development of RA. Lately other reports show that PADI4 is also relative to tumors, ulcerative colitis as well as multiple sclerosis. Although researches about PADI4 have been made a lot of significant progresses, abundant of unknow have always been existing.



Key wordsRheumatoid arthristis      Peptidylarginine deiminase 4      SNP      Citrullination      Anti-PADI4 antibady     
Received: 05 January 2011      Published: 25 September 2011
ZTFLH:  Q51  
Cite this article:

LIU Xiao-shuai, GE Lu-na, HAN Jin-xiang, CHANG Xiao-tian, ZHU You-ming, WANG Shi-li. Peptidylarginine Deiminase 4 Affects Pathogenesis and Development of Rheumatoid Arthrisits. China Biotechnology, 2011, 31(9): 103-108.

URL:

https://manu60.magtech.com.cn/biotech/     OR     https://manu60.magtech.com.cn/biotech/Y2011/V31/I9/103


[1] Vossenaar E R, Zendman A J, van Nenrooij W J, et al.PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease. bioessays, 2003, 25(11): 1106-1118.

[2] Fujisaki M, Suqawara K. Properties of petidylarginine deiminease from the epidermis of newborn rats. J Biochem, 1981, 89(1): 257-263.

[3] Iida A, Nakamura Y. Identification of 45 novel SNP in the 83Kb region containing peptidylarginine deiminase types 1 and 3 loci on chromosomal band 1P36.13. J Hum Genet, 2004, 49(7): 387-390.

[4] Guerrin M, shigami A, Mechin M C, et al. cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type I. Biochem J, 2003, 370(Pt 1):167-174.

[5] Cuthbert G L, Daujat S, Snowden A W, et al. Histone deimination antagonizes arginine methylation. Cell, 2004, 118: 545-553.

[6] Tanikawa C, Ueda K, Nakagawa H, et al. Regulation of protein citrullination trough p53/PADI4 network in DNA damage response. Cancer Res, 2009, 69(22):8761-8769.

[7] Guo Q, Bedford M T, Fast W. Discovery of peptidylarginine deiminase-4 substrates by protein array: antagonistic citrullination and methylation of human ribosomal protein S2. Mol Biosyst. 2011,7(7):2286-2295.

[8] Chang X, Fang K. PADI4 and tumourigenesis. Cancer Cell Int. 2010, 10:7.

[9] Chang X, Han J, Pang L, et al. Experssion of peptidylarginine deiminase type 4 (PAD4) in various tumors. Molecular carcinogenesis, 2006, 45: 183-196.

[10] Denis H, Deplus R, Putmans P. Functional connection between deimination and deacetylation of histones. Mol Cell Biol,2009, 29(18):4982-4993.

[11] 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.

[12] Suzuki A, Yamada R, Chang X, et al. Functional haplotype of PADI4, encoding citrullinating enzyme peptidylargine deiminase 4, are associated with rheumatoid arthritis. Nature Genet, 2003, 34(4): 395-402.

[13] Nakashima K, Hagiwara T, Ishigami A, et al. Cterization of peptidylarginine deiminase in HL-60 cells induced by retinoic acid and 1alpha, 25-dihydroxyvitamin D(3). J Biol Chem,1999, 274:27786-27792.

[14] Hagiwara T, Nakashima K, Hirano H, et al. Deimination of arginine residues in nucleophosmin/B23 and histones in HL-60 granulocytes. Biochem Biophys Res Commun, 2002, 290(3): 979-983.

[15] Asaga H, Nakashima H, Senshu T, et al. Immunocytochemical Localization of peptidylargine deiminase in houman eosinophils and neutrophils. J Leukoc Biol, 2001, 70(1): 46-51.

[16] Vossenaar E R, Radstake T R, vander-Heijden A, et al. Expression and activity of citrullinating peptidylarginie deiminase enzymes in monocytes and macrophages. Ann Rheum Dis, 2004, 63(4):373-381.

[17] Nakashima K, Hagiwara T, Yamada M. Nuclear localization of peptidylarginine deiminase V and histone deimination in granulocytes. J Biol Chem, 2002, 277(51):49562-49568.

[18] Kang C P, Lee H S, Ju H, et al. A functional haplotype of the PADI4 gene associated with increased rheumatoid arthritis susceptibility in Koreans. Arthritis Rheum, 2006, 54:90-96.

[19] Freudenberg J, Lee H S, Han B G, et al. Genome-wide association study of rheumatoid arthritis in Koreans: population-specific loci as well as overlap with European susceptibility loci. Arthritis Rheum, 2011, 63(4): 884-893.

[20] Bang S Y, Han T U, Choi C B, et al. Peptidyl arginine deiminase type IV (PADI4) haplotypes interact with share epitope regardless of anti-cyclic citrullinated peptide antibody or erosive joint status in rheumatoid arthritis: a case control study. Arthritis Res Ther, 2010, 12(3): R115.

[21] Barton A, Bowes J, Eyer S, et al. A functional haplotype of the PADI4 gene associated with rheumatoid arthritis in a Japanese population is not associated in a united kindom population. Arthritis Rheum, 2004, 50: 1117-1121.

[22] Caponi L, Ptit-Teixeira E, Sebbag M, et al. A family based stedy shows no association between rheumatoid arthritis and the PADI4 gene in a white French population. Ann Rheum Dis, 2005, 64: 587-593.

[23] Hoppe B, Haupl R, Gruber R, et al. Detailed analysis of the variability of peptidylarginine deiminase type 4 in German patients with rheumatoid arthritis: a case-control study. Arthritis Res Ther, 2006, 8: R34.

[24] Martinez A, Valdivia A, Pascual-Salcedo D, et al. PADI4 polymorphisms are not associated with rheumatoid arthritis in the Spanish population. Rheumatology, 2005, 44:1263-1266.

[25] Chen R, Wei Y, Cai Q, et al. The PADI4 gene dose not contribute to genetic susceptibility to rheumatoid arthritis in Chinese Han population. Rheumatol Int, In Press.

[26] Fan L Y, Wang W J, Wang Q, et al. Association of peptidylarginine deiminase Ⅳ gene polymorphisms ad its expression with rheumatoid arthritis in Chinese patients. Tissue Antigens, 2008, 72(5):469-473.

[27] Hill J A, Southwoed S, Sette A, et al. Cutting edge:the conversion of arginine to critruline allows for a high—affinity peptide interaction with the rheumatoid arthritis—associated HLA—DRBl*040l MHC classⅡmolecule. J Immunol, 2003, 171: 38-541.

[28] Suzuki M, Miyagi J, Kuribayashi M, et al. Evaluation of allele frequencies in the PADI4 gene and anti-cyclic citrullinated peptide antibodies of patients with rheumatoid arthritis in a Japanese population. Ann Rheum Dis, 2006, 65: 1399-1400.

[29] Burr M L Naseem H, Hinks A, et al. PADI4 genotype is not associated with rheumatoid arthritis in a large UK Caucasian population. Ann Rheum Dis, 2010, 69: 666-670.

[30] Gandjbakbch F, Fajardy I, Ferre B, et al. A functional haplotype of PADI4 gene in rheumatoid arthritis: positive correlation in a French population. J Rheumatol, 2009, 36: 881-886.

[31] Chang X, Yamada R, Suzuki A, et al. Citrullination of fibronectin in rheumatoid arthritis synovial tissue. Rheumatology, 2005, 44:1374-1382.

[32] Chang X, Yamada R, Suzuki A, et al. Localization of peptidylarginine deiminase 4 (PADI4) and citrullinated protein in synovial tissue of rheumatoid arthritis. Rheumatology, 2005, 44: 40-50.

[33] Klareskog L, Malmstrom V, Lundberg K. Smoking, citrullination and genetic variability in the immunopathogenesis of rheumatoid arthritis. Semin Immunol, 2011, 23: 92-98.

[34] Van Venrooij W J, Pruijn GY. Citrullin: a small change for a protein with great consequences for rheumatoid arthritis. Arthritis Res, 2000, 2: 249-251.

[35] Kuhn K A, Kulik L, Tomooka B, et al. Antibodies against citrullinated proteins enhance tissue injury in experimental autoimmune arthritis. J Clin Invest, 2006,116:961-973.

[36] 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(9):2085-2097.

[37] Loos T,Mortier A, Gouwy M, et al. Citrullination of CXCL10 and CXCL11 by peptidylarginine deiminase: a naturally occurring posttranslational modification of chemokines and newdimension of immunoregulation. Blood, 2008,112 (7):2648-2656.

[38] Takizawa Y, Sawada T, Suzuki A, et al. Peptidylarginine deiminase 4 (PADI4) identified as a conformation-dependent autoanti-gen in rheumatoid arthritis. Scand J Rheumatol, 2005, 34: 212-215.

[39] Harris M L, Darrah E, Lam GK, et al. Association of autoimmunity to peptidyl arginine deiminase type 4 with genotype and disease severity in rheumatoid arthritis. Arthritis Rheum, 2008,58:1958-1967.

[40] Halvorsen E H, Pollmann S, Gilboe I M, et al. Serum IgG antibodies to peptidylarginine deiminase 4 in rheumatoid arthritis and associations with disease severity. Ann Rheum Dis, 2008,67(3):414-417.

[41] Anzilotti C, Pratesi F, Tommasi C, et al. Peptidylarginine deiminase 4 and citrullination in health and disease. Autoimmunity Reviews, 2010, 9: 158-160.

[42] Nissinen R, Paimela L, Julkunen H, et al. Peptidylarginine deiminase, the arginine to citrulline converting enzyme, is frequently recognized by sera of patients with rheumatoid arthritis, lupus erythematosus and primary sjogren syndrome. Scand J Rheumatol, 2003, 32: 340-345.

[43] Harris M L, Darrah E, Lam G K, et al. Association of autoimmunity to peptidylargine deiminase type 4 with genotype and disease a everity in rheumatoid arthritis. Arthritis Rheum, 2008, 58(70): 1958-1967.

[44] Zhao J, Zhao Y, He J, et al. Prevalence and significance of anti-peptidylarginine deiminase 4 antibodies in rheumatoid arthritis. J Rheumatol, 2008, 35(6): 969-974.

[45] Shi H X, Qian L, Li X P, et al. The significance of serum anti-peptidylarginie deiminase 4 antibodies in the diagnosis of rheumatoid arthritis. Immunological Journal, 2010, 26(4): 329-332.

[46] Wang W, Li J. Predominace of IgG1 and IgG3 subclasses of autoantibodies to peptidylarginine deiminase 4 in rheumatoid arthritis. Clin Rheumatol, 2011, 30(4): 563-567.

[47] Auger I, Martin M, Balandraud N, et al. Rheumatoid arthritis specific autoantibodies to peptidyl arginine deiminase type 4 inhibit citrullination of fibrinogen. Arthritis Rheum, 2010, 62:126-131.

[48] Qian L, Shi H X, Li X P, et al. The significance of serum peptidylarginine deiminase 4 in rheumatoid arthritis. Chinese Journal of Internal Medicine, 2011, 50(2): 107-110.

[49] 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.

[50] Chen C C, Isomoto H, Narumi Y, et al. Haplotypes of PADI4 susceptible to rheumatoid arthritis are also associated with ulcerative colitis in the Japanese population. Clin Immunol, 2008, 126(2): 165-171.

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