•  
  •  
 

Acta Universitatis Lodziensis, Folia Biologica et Oecologica

Abstract

Citrullination is one of the possible post-translational modifications of proteins. It is based on a conversion of L-arginine residue (L-Arg) to L-citrulline residue (L-Cit). The reaction is catalyzed by peptidylarginine deiminases (PAD). The change of L-Arg imino moiety results in a loss of a positive charge. This slight modification can contribute to significant changes in physicochemical properties of proteins, which may also cause a change of their functions. Citrullination is the modification observed in physiological processes such as epidermal keratinization, regulation of gene expression and the reorganization of myelin sheaths. The changes in the efficacy of citrullination may contribute to the pathogenesis of many different diseases including: psoriasis, multiple sclerosis, rheumatoid arthritis and cancer.

Keywords

deimination, peptidylarginine deiminase, citrulline, post-translational modification

References

Arita, K., Hashimoto, H., Shimizu, T. et al. 2004. Structural basis for Ca(2+)-induced activation of human PAD4. Nature structural & molecular biology, 11: 777–783. http://dx.doi.org/10.1038/nsmb799

Asaga, H., Yamada, M. & Senshu, T. 1998. Selective deimination of vimentin in calcium ionophoreinduced apoptosis of mouse peritoneal macrophages. Biochemical and biophysical research communications, 243: 641–646. http://dx.doi.org/10.1006/bbrc.1998.8148

Beniac, D.R., Wood, D.D., Palaniyar, N. et al. 2000. Cryoelectron microscopy of protein-lipid complexes of human myelin basic protein charge isomers differing in degree of citrullination. Journal of structural biology, 129: 80–95. http://dx.doi.org/10.1006/jsbi.1999.4200

Berlet, H.H. 1987. Cation-dependent extraction of basic protein from isolated human myelin. Independence of endogenous acid proteolysis. Neurochemical pathology, 7: 263–274.

Blombäck, B., Hessel, B., Hogg, D. & Therkildsen, L. 1978. A two-step fibrinogen--fibrin transition in blood coagulation. Nature, 275: 501–505.

Boggs, J.M., Rangaraj, G., Koshy, K.M. et al. 1999. Highly deiminated isoform of myelin basic protein from multiple sclerosis brain causes fragmentation of lipid vesicles. Journal of neuroscience research, 57: 529–535.

Cao, L., Goodin, R., Wood, D., et al. 1999. Rapid release and unusual stability of immunodominant peptide, 45–89 from citrullinated myelin basic protein. Biochemistry, 38: 6157–6163. http://dx.doi.org/10.1021/bi982960s

Chang, X., Hou, X., Pan, J. et al. 2011. Investigating the pathogenic role of PADI4 in oesophageal cancer. International journal of biological sciences, 7: 769–781.

Chang, X., Yamada, R., Suzuki, A. et al. 2005. Citrullination of fibronectin in rheumatoid arthritis synovial tissue. Rheumatology (Oxford, England), 44: 1374–1382. http://dx.doi.org/10.1093/rheumatology/kei023

Chavanas, S., Méchin, M-C., Nachat, R. et al. 2006. Peptidylarginine deiminases and deimination in biology and pathology: relevance to skin homeostasis. Journal of dermatological science, 44: 63–72. http://dx.doi.org/10.1016/j.jdermsci.2006.07.004

Cherrington, B.D., Morency, E., Struble, A.M. et al. 2010. Potential role for peptidylarginine deiminase 2 (PAD2) in citrullination of canine mammary epithelial cell histones. PloS one, 5: e11768. http://dx.doi.org/10.1371/journal.pone.0011768

Cherrington, B.D., Zhang, X., McElwee, J.L. et al. 2012. Potential role for PAD2 in gene regulation in breast cancer cells. PloS one, 7: e41242. http://dx.doi.org/10.1371/journal.pone.0041242

Curis, E., Nicolis, I., Moinard, C., et al. 2005. Almost all about citrulline in mammals. Amino acids, 29: 177–205. http://dx.doi.org/10.1007/s00726-005-0235-4

Ferreiro, E., Resende, R., Costa, R. et al. 2006. An endoplasmic-reticulum-specific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity. Neurobiology of disease 23: 669–678. http://dx.doi.org/10.1016/j.nbd.2006.05.011

Firestein, G.S. 2003. Evolving concepts of rheumatoid arthritis. Nature, 423: 356–361. http://dx.doi.org/10.1038/nature01661

Furie, B. & Furie, B.C. 1988. The molecular basis of blood coagulation. Cell, 53: 505–518.

György, B., Tóth, E., Tarcsa, E. et al. 2006. Citrullination: a posttranslational modification in health and disease. The international journal of biochemistry & cell biology, 38: 1662–1677. http://dx.doi.org/10.1016/j.biocel.2006.03.008

Hagiwara, T., Hidaka, Y. & Yamada, M. 2005. Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes. Biochemistry, 44: 5827–5834. http://dx.doi.org/10.1021/bi047505c

Harding, C.R. & Scott, I.R. 1983. Histidine-rich proteins (filaggrins): structural and functional heterogeneity during epidermal differentiation. Journal of molecular biology, 170: 651–673.

Ishida-Yamamoto, A., Senshu, T., Takahashi, H. et al. 2000. Decreased deiminated keratin K1 in psoriatic hyperproliferative epidermis. The Journal of investigative dermatology, 114: 701–705. http://dx.doi.org/10.1046/j.1523-1747.2000.00936.x

Jang, B., Kim, E., Choi, J-K. et al. 2008. Accumulation of citrullinated proteins by up-regulated peptidylarginine deiminase 2 in brains of scrapieinfected mice: a possible role in pathogenesis. The American journal of pathology, 173: 1129–1142. http://dx.doi.org/10.2353/ajpath.2008.080388

Karlić, R., Chung, H-R., Lasserre, J., et al. 2010. Histone modification levels are predictive for gene expression. Proceedings of the National Academy of Sciences of the United States of America, 107: 2926–2931. http://dx.doi.org/10.1073/pnas.0909344107

Kubilus, J. & Badenm, H.P. 1983. Purification and properties of a brain enzyme which deiminates proteins. Biochimica et biophysica acta, 745: 285–291.

Kursula, P. 2008. Structural properties of proteins specific to the myelin sheath. Amino acids, 34: 175–185. http://dx.doi.org/10.1007/s00726-006-0479-7

Lee, S.C., Kim, I.G., Marekov, L.N. et al. 1993. The structure of human trichohyalin. Potential multiple roles as a functional EF-hand-like calcium-binding protein, a cornified cell envelope precursor, and an intermediate filament-associated (cross-linking) protein. The Journal of biological chemistry, 268: 12164–12176.

Masson-Bessière, C., Sebbag, M., Girbal-Neuhauser, E. et al. 2001. The major synovial targets of the rheumatoid arthritis-specific antifilaggrin autoantibodies are deiminated forms of the alphaand beta-chains of fibrin. Journal of immunology (Baltimore, Md : 1950), 166: 4177–4184.

Mastronardi, F.G., Wood, D.D., Mei, J. et al. 2006. 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. The Journal of neuroscience: the official journal of the Society for Neuroscience, 26: 11387–1396. http://dx.doi.org/10.1523/JNEUROSCI.3349-06.2006

Mohanan, S., Cherrington, B.D., Horibata, S. et al. 2012. Potential role of peptidylarginine deiminase enzymes and protein citrullination in cancer pathogenesis. Biochemistry research international, 2012: 1–11. http://dx.doi.org/10.1155/2012/895343

Moscarello, M. A., Pritzker, L., Mastronardi, F.G. & Wood, D.D. 2002. Peptidylarginine deiminase: a candidate factor in demyelinating disease. Journal of neurochemistry, 81: 335–343.

Moscarello, M a, Wood, D.D., Ackerley, C. & Boulias, C. 1994. Myelin in multiple sclerosis is developmentally immature. The Journal of clinical investigation, 94: 146–154. http://dx.doi.org/10.1172/JCI117300

Méchin, M-C., Sebbag, M., Arnaud, J. et al. 2007. Update on peptidylarginine deiminases and deimination in skin physiology and severe human diseases. International journal of cosmetic science, 29: 147–168. http://dx.doi.org/10.1111/j.1467-2494.2007.00377.x

Nachat, R., Méchin, M-C., Takahara, H. et al. 2005. Peptidylarginine deiminase isoforms 1-3 are expressed in the epidermis and involved in the deimination of K1 and filaggrin. The Journal of investigative dermatology, 124: 384–93. http://dx.doi.org/10.1111/j.0022-202X.2004.23568.x

Nakayama-Hamada, M., Suzuki, A., Furukawa, H. et al. 2008. Citrullinated fibrinogen inhibits thrombincatalysed fibrin polymerization. Journal of biochemistry, 144: 393–398. http://dx.doi.org/10.1093/jb/mvn079

Okumura, N., Haneishi, A. & Terasawa, F. 2009. Citrullinated fibrinogen shows defects in FPA and FPB release and fibrin polymerization catalyzed by thrombin. Clinica chimica acta; international journal of clinical chemistry 401: 119–123. http://dx.doi.org/10.1016/j.cca.2008.12.002

O’Donovan, C.N., Tobin, D. & Cotter, T.G. 2001. Prion protein fragment PrP-(106-126) induces apoptosis via mitochondrial disruption in human neuronal SH-SY5Y cells. The Journal of biological chemistry, 276: 43516–43523. http://dx.doi.org/10.1074/jbc.M103894200

Pearton, D.J., Dale, B.A. & Presland, R.B. 2002. Functional Analysis of the Pro®laggrin N-Terminal Peptide: Identi®cation of Domains that Regulate Nuclear and Cytoplasmic Distribution. 661–669.

Pritzker, L.B., Joshi, S., Harauz, G. & Moscarello, M.A. 2000. Deimination of myelin basic protein. 2. Effect of methylation of MBP on its deimination by peptidylarginine deiminase. Biochemistry, 39: 5382–5388.

Rodenburg, R.J., Ganga, A., Van Lent, P.L. et al. 2000. The antiinflammatory drug sulfasalazine inhibits tumor necrosis factor alpha expression in macrophages by inducing apoptosis. Arthritis and rheumatism, 43: 1941–1950. http://dx.doi.org/10.1002/1529-0131(200009)43:9<1941::AID-ANR4>3.0.CO;2-O

Rodríguez, S.B., Stitt, B.L. & Ash, D.E. 2010. Cysteine 351 is an essential nucleophile in catalysis by Porphyromonas gingivalis peptidylarginine deiminase. Archives of biochemistry and biophysics, 504: 190–196. http://dx.doi.org/10.1016/j.abb.2010.09.008

Rubin, B. & Sønderstrup, G. 2004. Citrullination of self-proteins and autoimmunity. Scandinavian journal of immunology, 60: 112–120. http://dx.doi.org/10.1111/j.0300-9475.2004.01457.x

Sebbag, M., Chapuy-Regaud, S., Auger, I. et al. 2004. Clinical and pathophysiological significance of the autoimmune response to citrullinated proteins in rheumatoid arthritis. Joint, bone, spine: revue du rhumatisme, 71: 493–502. http://dx.doi.org/10.1016/j.jbspin.2004.07.004

Senshu, T., Akiyama, K. & Nomura, K. 1999. Identification of citrulline residues in the V subdomains of keratin K1 derived from the cornified layer of newborn mouse epidermis. Experimental dermatology, 8: 392–401.

Senshu, T., Kan, S., Ogawa, H. et al. 1996. Preferential Deimination of Keratin K1 and Filaggrin during the Terminal Differentiation of Human Epidermis The process of normal epidermal differentiation is characterized by a series of morphologic changes as keratinocytes progress from the germinative, 719: 712–719.

So, A.K., Varisco, P-A., Kemkes-Matthes, B. et al. 2003. Arthritis is linked to local and systemic activation of coagulation and fibrinolysis pathways. Journal of thrombosis and haemostasis: JTH, 1: 2510–2515.

Staquet, M.J., Haftek, M., Cordier, G. & Thivolet, J. 1987. Keratin filament composition of human epidermal spinous and granular cell fractions selected by flow cytometric sorting. Archives of dermatological research, 279: 273–275.

Steinert, P.M., Mack, J.W., Korge, B.P. et al. 1991. Glycine loops in proteins: their occurrence in certain intermediate filament chains, loricrins and single-stranded RNA binding proteins. International journal of biological macromolecules, 13: 130–139.

Suzuki, A., Yamada, R. & Yamamoto, K. 2007. Citrullination by Peptidylarginine Deiminase in Rheumatoid Arthritis. Annals of the New York Academy of Sciences, 1108: 323–339. http://dx.doi.org/10.1196/annals.1422.034

Takahara, H., Okamoto, H. & Sugawara, K. 1986. Calcium-dependent Properties of Peptidylarginine from Rabbit Skeletal Muscle. Agricultural and biological chemistry, 50: 2899–2904.

Takizawa, Y., Suzuki, A., Sawada, T. et al. 2006. Citrullinated fibrinogen detected as a soluble citrullinated autoantigen in rheumatoid arthritis synovial fluids. Annals of the rheumatic diseases, 65: 1013–1020. http://dx.doi.org/10.1136/ard.2005.044743

Tarcsa, E., Marekov, L.N., Andreoli, J. et al. 1997. The Fate of Trichohyalin. 272: 27893–27901.

Tarcsa, E., Marekov, L.N., Mei, G. et al. 1996a. Protein unfolding by peptidylarginine deiminase. Substrate specificity and structural relationships of the natural substrates trichohyalin and filaggrin. The Journal of biological chemistry, 271: 30709–30716.

Thompson, P.R. & Fast, W. 2006. Histone citrullination by protein arginine deiminase: is arginine methylation a green light or a roadblock? ACS chemical biology, 1: 433–441. http://dx.doi.org/10.1021/cb6002306

Vossenaar, E.R. 2004. Expression and activity of citrullinating peptidylarginine deiminase enzymes in monocytes and macrophages. Annals of the Rheumatic Diseases, 63: 373–381. http://dx.doi.org/10.1136/ard.2003.012211

Vossenaar, E.R., Zendman, A.J.W., Van Venrooij, W.J. & Pruijn, G.J.M. 2003. PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease. BioEssays: news and reviews in molecular, cellular and developmental biology, 25: 1106–1118. http://dx.doi.org/10.1002/bies.10357

Wang, L., Chang, X., Yuan, G. et al. 2010. Expression of peptidylarginine deiminase type 4 in ovarian tumors. International journal of biological sciences, 6: 454–464.

Whitaker, J.N., Bashir, R.M., Chou, C.H. & Kibler, R.F. 1980. Antigenic features of myelin basic protein-like material in cerebrospinal fluid. Journal of immunology (Baltimore, Md : 1950), 124: 1148–1153.

Wood, D.D., Bilbao, J.M., O’Connors, P. & Moscarello, M.A. 1996. Acute multiple sclerosis (Marburg type) is associated with developmentally immature myelin basic protein. Annals of neurology, 40: 18–24. http://dx.doi.org/10.1002/ana.410400106

Wysocka, J., Allis, C.D. & Coonrod, S. 2006. Histone arginine methylation and its dynamic regulation. Frontiers in bioscience : a journal and virtual library, 11: 344–355.

Ying, S., Simon, M., Serre, G. & Takahara, H. 2012. Peptidylarginine Deiminases and Protein Deimination in Skin Physiopathology. In: O'Daly J. (ed.), Psoriasis - A Systemic Disease, 118–132, InTech.

First Page

17

Last Page

25

Language

eng

Share

COinS