Effects of sulfasalazine and tofacitinib on the protein profile of articular chondrocytes

References

• O’Dell JR, Mikuls TR, Taylor TH, Ahluwalia V, Brophy M, Warren SR, et al. Therapies for active rheumatoid arthritis after methotrexate failure. N Engl J Med. 2013;369(4):307–3018.
   PubMed Web of Science ®Google Scholar
• Box SA, Pullar T. Sulphasalazine in the treatment of rheumatoid arthritis. Br J Rheumatol. 1997;36(3):382–6.
   Google Scholar
• Neumann VC, Taggart AJ, Le Gallez P, Astbury C, Hill J, Bird HA. A study to determine the active moiety of sulphasalazine in rheumatoid arthritis. J Rheumatol. 1986;13(2):285–7.
   Google Scholar
• Stenson WF, Mehta J, Spilberg I. Sulfasalazine inhibition of binding of N-formyl-methionyl-leucyl-phenylalanine (FMLP) to its receptor on human neutrophils. Biochem Pharmacol. 1984;33(3):407–12.
   Google Scholar
• Kanerud L, Hafstrom I, Ringertz B. Effect of sulphasalazine and sulphapyridine on neutrophil superoxide production: role of cytosolic free calcium. Ann Rheum Dis. 1990;49(5):296–300
   Google Scholar
• Rodenburg RJ, Ganga A, van Lent PL, van de Putte LB, van Venrooij WJ. The antiinflammatory drug sulfasalazine inhibits tumor necrosis factor alpha expression in macrophages by inducing apoptosis. Arthritis Rheum. 2000;43(9):1941–50.
   Google Scholar
• Morabito L, Montesinos MC, Schreibman DM, Balter L, Thompson LF, Resta R, et al. Methotrexate and sulfasalazine promote adenosine release by a mechanism that requires ecto-5’-nucleotidase-mediated conversion of adenine nucleotides. J Clin Invest. 1998;101(2):295–300.
   Google Scholar
• Nose M, Sasano M, Kawashima Y. Salazosulfapyridine suppresses chondrocyte mediated degradation induced by interleukin 1beta. J Rheumatol. 1997;24(3):550–4.
   Google Scholar
• Lakey RL, Cawston TE. Sulfasalazine blocks the release of proteoglycan and collagen from cytokine stimulated cartilage and down-regulates metalloproteinases. Rheumatology 2009;48(10):1208–12.
   Google Scholar
• O’Shea JJ, Kontzias A, Yamaoka K, Tanaka Y, Laurence A. Janus kinase inhibitors in autoimmune diseases. Ann Rheum Dis. 2013;72(Suppl 2):ii111–5.
   Google Scholar
• Kontzias A, Kotlyar A, Laurence A, Changelian P, O’Shea JJ. Jakinibs: a new class of kinase inhibitors in cancer and autoimmune disease. Curr Opin Pharmacol. 2012;12(4):464–70.
   PubMedGoogle Scholar
• van Vollenhoven RF, Fleischmann R, Cohen S, Lee EB, García Meijide JA, Wagner S, et al. Tofacitinib or adalimumab versus placebo in rheumatoid arthritis. N Engl J Med. 2012;367(6):508–19.
   PubMedGoogle Scholar
• Tanaka Y, Yamaoka K. JAK inhibitor tofacitinib for treating rheumatoid arthritis: from basic to clinical. Mod Rheumatol. 2013;23(3):415–24.
   PubMedGoogle Scholar
• Milici AJ, Kudlacz EM, Audoly L, Zwillich S, Changelian P. Cartilage preservation by inhibition of Janus kinase 3 in two rodent models of rheumatoid arthritis. Arthritis Res Ther. 2008;10(1):R14.
   PubMed Web of Science ®Google Scholar
• Aigner T, Soeder S, Haag J. IL-1beta and BMPs–interactive players of cartilage matrix degradation and regeneration. Eur Cell Mater. 2006;12:49–56.
   PubMed Web of Science ®Google Scholar
• Yasuda T. Cartilage destruction by matrix degradation products. Mod Rheumatol. 2006;16(4):197–205.
   Google Scholar
• Yoshida M, Tsuji M, Funasaki H, Kan I, Fujii K. Analysis for the major contributor of collagenase to the primary cleavage of type II collagens in cartilage degradation. Mod Rheumatol. 2005;15(3):180–6.
   Google Scholar
• Kellgren JH, Lawrence JS. Radiological assessment of osteo-arthrosis. Ann Rheum Dis. 1957;16(4):494–502.
   PubMed Web of Science ®Google Scholar
• Kivirikko KI, Myllylä R. Collagen glycosyltransferases. Int Rev Connect Tissue Res. 1979;8:23–72.
   PubMedGoogle Scholar
• Kivirikko KI, Myllylä R. The hydroxylation of prolyl and lysyl residues. In: Freedman BR, Hawkins HC, editors. The Enzymology of Post-Translational Modifications of Proteins. London Academic Press, 1980. p. 53–104.
   Google Scholar
• Kivirikko KI, Myllylä R, Pihlajaniemi T. Hydroxylation of proline and lysine residues in collagens and other animal and plant proteins. In: Harding JJ, Crabbe M, editors Post-Translational Modifications of Proteins. Boca Raton, FL: CRC Press; 1992. p. 1–51.
   Google Scholar
• Notbohm H, Nokelainen M, Myllyharju J, Fietzek PP, Müller PK, Kivirikko KI. Recombinant human type II collagens with low and high levels of hydroxylysine and its glycosylated forms show marked differences in fibrillogenesis in vitro. J Biol Chem. 1999;274(13): 8988–92.
   Google Scholar
• Verzijl N, DeGroot J, Ben ZC, Brau-Benjamin O, Maroudas A, Bank RA, et al. Crosslinking by advanced glycation end products increases the stiffness of the collagen network in human articular cartilage: a possible mechanism through which age is a risk factor for osteoarthritis. Arthritis Rheum. 2002;46(1):114–23.
   Google Scholar
• Willett TL, Kandel R, De Croos JN, Avery NC, Grynpas MD. Enhanced levels of non-enzymatic glycation and pentosidine crosslinking in spontaneous osteoarthritis progression. Osteoarthritis Cartilage. 2012;20(7):736–44.
   Google Scholar
• Lushak VI. AMP-deaminase: regulation and physiological role of the enzyme. Ukr Biokhim Zh. 2000;72(1):9–20.
   Google Scholar
• Haskó G, Cronstein B. Regulation of inflammation by adenosine. Front Immunol. 2013;4:85.
   PubMed Web of Science ®Google Scholar
• Gadangi P, Longaker M, Naime D, Levin RI, Recht PA, Montesinos MC, et al. The anti-inflammatory mechanism of sulfasalazine is related to adenosine release at inflamed sites. J Immunol. 1996;156(5):1937–41.
   PubMedGoogle Scholar
• Kanter JE, Kramer F, Barnhart S, Averill MM, Vivekanandan-Giri A, Vickery T, et al. Diabetes promotes an inflammatory macrophage phenotype and atherosclerosis through acyl-CoA synthetase 1. Proc Natl Acad Sci U S A. 2012;109(12):E715–24.
   Google Scholar
• Golej DL, Askari B, Kramer F, Barnhart S, Vivekanandan-Giri A, Pennathur S, Bornfeldt KE. Long-chain acyl-CoA synthetase 4 modulates prostaglandin E2 release from human arterial smooth muscle cells. J Lipid Res. 2011;52(4):782–93.
   Google Scholar
• Lambrecht S, Dhaenens M, Almqvist F, Verdonk P, Verbruggen G, Deforce D, Elewaut D. Proteome characterization of human articular chondrocytes leads to novel insights in the function of small heat-shock proteins in chondrocyte homeostasis. Osteoarthritis Cartilage. 2010;18(3):440–6.
   Google Scholar
• Voegeli TS, Wintink AJ, Chen Y, Currie RW. Heat shock proteins 27 and 70 regulating angiotensin II-induced NF-kappaB: a possible connection to blood pressure control?Appl Physiol Nutr Metab. 2008;33(5):1042–9.
   Google Scholar
• Alford KA, Glennie S, Turrell BR, Rawlinson L, Saklatvala J, Dean JL. Heat shock protein 27 functions in inflammatory gene expression and transforming growth factor-beta-activated kinase-1 (TAK1)-mediated signaling. J Biol Chem. 2007;282(9):6232–6241.
   Google Scholar
• Zender L, Xue W, Zuber J, Semighini CP, Krasnitz A, Ma B, et al. An oncogenomics-based in vivo RNAi screen identifies tumor suppressors in liver cancer. Cell 2008;135(5):852–64.
   Google Scholar
• Marszalek JR, Weiner JA, Farlow SJ, Chun J, Goldstein LS. Novel dendritic kinesin sorting identified by different process targeting of two related kinesins: KIF21A and KIF21B. J Cell Biol. 1999;145(3):469–79.
   Google Scholar