Effects of proteasome inhibitors on cytokines, metalloproteinases and their inhibitors and collagen type-I expression in periprosthetic tissues and fibroblasts from loose arthroplasty endoprostheses

References

• Noordin S, Masri B. Periprosthetic osteolysis: genetics, mechanisms and potential therapeutic interventions. Canad J Surg. 2012;55(6):408–417. doi:10.1503/cjs.003711.
   PubMed Web of Science ®Google Scholar
• Sukur E, Akman YE, Ozturkmen Y, Kucukdurmaz F. Particle disease: a current review of the biological mechanisms in periprosthetic osteolysis. After Hip Arthroplasty Open Orthop J. 2016;10:241–251. doi:10.2174/1874325001610010241.
   PubMedGoogle Scholar
• Gallo J, Goodman SB, Konttinen YT, Wimmer MA, Holinka M. Osteolysis around total knee arthroplasty: A review of pathogenetic mechanisms. Acta Biomater. 2013;9(9):8046–8058. doi:10.1016/j.actbio.2013.05.005.
   PubMed Web of Science ®Google Scholar
• Gallo J, Goodman SB, Konttinen YT, Raska M. Particle disease: biologic mechanisms of periprosthetic osteolysis in total hip arthroplasty. Innate Immun. 2012;19(2):213–224. doi:10.1177/1753425912451779.
   PubMed Web of Science ®Google Scholar
• Syggelos SA, Aletras AJ, Smirlaki I, Skandalis SS. Extracellular matrix degradation and tissue remodeling in periprosthetic loosening and osteolysis: focus on matrix metalloproteinases, their endogenous tissue inhibitors, and the proteasome. Biomed Res Int. 2013;2013:230805.
   PubMed Web of Science ®Google Scholar
• Wang ML, Hauschka PV, Tuan RS, Steinbeck MJ. Exposure to particles stimulates superoxide production by human THP-1 macrophages and avian HD-11EM osteoclasts activated by tumor necrosis factor-α and PMA. J Arthroplasty. 2002;17(3):335–346.
   PubMed Web of Science ®Google Scholar
• Syggelos SA, Eleftheriou SC, Giannopoulou E, Panagiotopoulos E, Aletras AJ. Gelatinolytic and collagenolytic activity in periprosthetic tissues from loose hip endoprostheses. Rheumatol. 2001;28(6):1319–1329.
   Web of Science ®Google Scholar
• Niarakis A, Giannopoulou E, Ravazoula P, Panagiotopoulos E, Zarkadis IK, Aletras AJ. Detection of a latent soluble form of membrane type 1 matrix metalloprotease bound with tissue inhibitor of matrix metalloproteinases-2 in periprosthetic tissues and fluids from loose arthroplasty endoprostheses. FEBS J. 2013;280(24):6541–6555. doi:10.1111/febs.12555.
   PubMed Web of Science ®Google Scholar
• Takei I, Takagi M, Santavirta S, Ida H, Ishii M, Ogino T, Ainola M, Konttinen YT. Messenger ribonucleic acid expression of 16 matrix metalloproteinases in bone-implant interface tissues of loose artificial hip joints. J Biomed Mater Res. 2000;52:613–620. doi:10.1002/(ISSN)1097-4636.
   PubMed Web of Science ®Google Scholar
• Sasaki K, Tagaki M, Mandelin J, Takei I, Santavirta S, Ida H, Ogino T, Konttinen YT. Quantitative analysis of mRNA expression of TIMPs in the periprosthetic interface tissue of loose hips by real-time PCR system. J Biomed Mater Res. 2001;58:605–612.
   PubMed Web of Science ®Google Scholar
• Li T-F, Santavirta S, Virtanen I, Kononen M, Takagi M, Konttinen YT. Increased expression of EMMPRIN in the tissue around loosened hip prostheses. Acta Orthop Scand. 1999;70(5):446–451. doi:10.3109/17453679909000979.
   PubMed Web of Science ®Google Scholar
• Nawrocki B, Polette M, Burlet H, Birembaut P, Adnet JJ. Expression of gelatinase A and its activator MT1-MMP in the inflammatory periprosthetic response to polyethylene. J Bone Miner Res. 1999;14:288–294. doi:10.1359/jbmr.1999.14.2.288.
   PubMed Web of Science ®Google Scholar
• Hembry RM, Bagga MR, Reynolds JJ, Hamblen DL. Stromelysin, gelatinase A and TIMP-1 in prosthetic interface tissue: a role for macrophages in tissue remodelling. Histopathology. 1995;27:149–159. doi:10.1111/his.1995.27.issue-2.
   PubMed Web of Science ®Google Scholar
• Takagi M. Neutral proteinases and their inhibitors in the loosening of total hip prostheses. Acta Orthop Suppl. 1996;271:3–29.
   Google Scholar
• Yokohama Y, Matsumoto T, Hirakawa M, Kuroki Y, Fujimoto N, Imai K, Okada Y. Production of matrix metalloproteinases at the bone-implant interface in loose total hip replacements. Lab Invest. 1995;73(6):899–911.
   PubMed Web of Science ®Google Scholar
• Takagi M, Konttinen YT, Lindy O, Sorsa T, Kurvinen H, Suda A, Santavirta S. Gelatinase/type IV collagenases in the loosening of total hip replacement endoprostheses. Clin Orthop. 1994;306:136–144.
   Google Scholar
• Takagi M, Konttinen YT, Kemppinen P, Sorsa T, Tschesche H, Blaser J, Suda A, Santavirta S. Tissue inhibitor of metalloproteinase 1, collagenolytic and gelatinolytic activity in loose hip endoprostheses. J Rheumatol. 1995;22(12):2285–2290.
   PubMed Web of Science ®Google Scholar
• Santavirta S, Takagi M, Konttinen YT, Sorsa T, Suda A. Inhibitory effect of cefalotin on matrix metalloproteinase activity around loose hip prostheses. Antimicrob Agents Chemother. 1996;40(1):244–246.
   PubMed Web of Science ®Google Scholar
• Ishiguro N, Ito T, Kurokouchi K, Iwahori Y, Nagaya I, Hasegawa Y, Iwata H. mRNA expression of matrix metalloproteinases and tissue inhibitors of metalloproteinase in interface tissue around implants in loosening total hip arthroplasty. J Biomed Mater Res. 1996;32:611–617. doi:10.1002/(ISSN)1097-4636.
   PubMed Web of Science ®Google Scholar
• Alexander K, Banos A, Abro S, Hoppensteadt D, Fareed J, Rees H, Hopkinson W. Levels of matrix metalloproteinases in arthroplasty patients and their correlation with inflammatory and thrombotic activation processes. Clin Appl Thromb Hemost. 2016;441–446. doi:10.1177/1076029616639704.
   PubMed Web of Science ®Google Scholar
• Adams J. The proteasome: structure, function, and role in the cell. Cancer Treat Rev. 2003;29(1):3–9. doi:10.1016/S0305-7372(03)00081-1.
   PubMedGoogle Scholar
• Wang J, Maldonado MA. The ubiquitin-proteasome system and its role in inflammatory and autoimmune diseases. Cell Mol Immunol. 2006;3:255–261.
   PubMedGoogle Scholar
• Chen ZJ. Ubiquitin signalling in the NF-kappaB pathway. Nat Cell Biol. 2005;7(8):758–765. doi:10.1038/ncb0805-758.
   PubMed Web of Science ®Google Scholar
• Wu H-M, Chi K-H, Lin -W-W. Proteasome inhibitors stimulate activator protein-1 pathway via reactive oxygen species production. FEBS Lett. 2002;526(1–3):101–105. doi:10.1016/S0014-5793(02)03151-4.
   PubMed Web of Science ®Google Scholar
• Meiners S, Ludwig A, Stangl V, Stangl K. Proteasome inhibitors: poisons and remedies. Med Res Rev. 2008;28:309–327. doi:10.1002/(ISSN)1098-1128.
   PubMed Web of Science ®Google Scholar
• Yannaki E, Papadopoulou A, Athanasiou E, Kaloyannidis P, Paraskeva A, Bougiouklis D, Palladas P, Yiangou M, Anagnostopoulos A. The proteasome inhibitor bortezomib drastically affects inflammation and bone disease in adjuvant-induced arthritis in rats. Arthritis Rheum. 2010;62:3277–3288. doi:10.1002/art.27631.
   PubMedGoogle Scholar
• Palombella VJ, Conner EM, Fuseler JW, Destree A, Davis JM, Laroux FS, Wolf RE, Huang J, Brand S, Elliott PJ, et al. Role of the proteasome and NF-κB in streptococcal cell wall-induced polyarthritis. Pnas. 1998;95:15671–15676.
   PubMed Web of Science ®Google Scholar
• Ludwig A, Fechner M, Wilck N, Meiners S, Grimbo N, Baumann G, Stangl V, Stangl K. Potent anti-inflammatory effects of low-dose proteasome inhibition in the vascular system. J Mol Med. 2009;87:793–802. doi:10.1007/s00109-009-0469-9.
   PubMed Web of Science ®Google Scholar
• Elliott PJ, Pien CS, McCormack TA, Chapman ID, Adams J. Proteasome inhibition: a novel mechanism to combat asthma. J Allergy Clin Immunol. 1999;104:294–300. doi:10.1016/S0091-6749(99)70369-6.
   PubMed Web of Science ®Google Scholar
• Ortiz-Lazareno PC, Hernandez-Flores G, Dominguez-Rodriguez JR, Lerma-Diaz JM, Jave-Suarez LF, Aguilar-Lemarroy A, Gomez-Contreras PC, Scott-Algara D, Bravo-Cuellar A. MG132 proteasome inhibitor modulates proinflammatory cytokines production and expression of their receptors in U937 cells: involvement of nuclear factor-κB and activator protein-1. Immunology. 2008;124:534–541. doi:10.1111/imm.2008.124.issue-4.
   PubMed Web of Science ®Google Scholar
• Mao X, Pan X, Peng X, Cheng T, Zhang X. Inhibition of titanium particle-induced inflammation by the proteasome inhibitor bortezomib in murine macrophage-like RAW 264.7 cells. Inflammation. 2012;35(4):1411–1418. doi:10.1007/s10753-012-9454-5.
   PubMed Web of Science ®Google Scholar
• Meiners S, Hocher B, Weller A, Laule M, Stangl V, Guenther C, Godes M, Mrozikiewicz A, Baumann G, Stangl K. Downregulation of matrix metalloproteinases and collagens and suppression of cardiac fibrosis by inhibition of the proteasome. Hypertension. 2004;44:471–477. doi:10.1161/01.HYP.0000142772.71367.65.
   PubMed Web of Science ®Google Scholar
• Carmignac V, Quéré R, Durbeej M. Proteasome inhibition improves the muscle of laminin α2 chain-deficient mice. Hum Mol Genet. 2011;20:541–552. doi:10.1093/hmg/ddq499.
   PubMed Web of Science ®Google Scholar
• Fineschi S, Reith W, Guerne PA. Dayer JM and Chizzolini C. Proteasome blockade exerts an antifibrotic activity by coordinately down-regulating type I collagen and tissue inhibitor of metalloproteinase-1 and up-regulating metalloproteinase-1 production in human dermal fibroblasts. FASEB J. 2006;20:562–564. doi:10.1096/fj.05-4870fje.
   PubMed Web of Science ®Google Scholar
• Pujols L, Fernández-Bertolín L, Fuentes-Prado M, Alobid I, Roca-Ferrer J, Agell N, Mullol J and Picado C. Proteasome inhibition reduces proliferation, collagen expression, and inflammatory cytokine production in nasal mucosa and polyp fibroblasts. J Pharmacol Exp Ther. 2012;343(1):184–197. doi:10.1124/jpet.111.190710.
   PubMed Web of Science ®Google Scholar
• Pavlaki M, Giannopoulou E, Niarakis A, Ravazoula P, Aletras AJ. Walker 256 cancer cells secrete tissue inhibitor of metalloproteinase-free metalloproteinase-9. Mol Cell Biochem. 2009;328:189–199. doi:10.1007/s11010-009-0089-2.
   PubMed Web of Science ®Google Scholar
• Okada Y, Tsuchiya H, Shimizu H, Tomita K, Nakanishi I, Sato H, Seiki M, Yamashita K, Hayakawa T. Induction and stimulation of 92-kDa gelatinase/type IV collagenase production in osteosarcoma and fibrosarcoma cell lines by tumor necrosis factor alpha. Biochem Biophys Res Commun. 1990;171:610–617. doi:10.1016/0006-291X(90)91190-4.
   PubMed Web of Science ®Google Scholar
• Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227:680–685.
   PubMed Web of Science ®Google Scholar
• Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Pnas. 1979;76:4350–4354. doi:10.1073/pnas.76.9.4350.
   PubMed Web of Science ®Google Scholar
• Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976;72:248–254.
   PubMed Web of Science ®Google Scholar
• Schmidt M, Finley D. Regulation of proteasome activity in health and disease. Biochim Biophys Acta. 2014;1843:13–25. doi:10.1016/j.bbamcr.2013.11.025.
   PubMed Web of Science ®Google Scholar
• Skandalis SS, Aletras AJ, Gialeli C, Theocharis AD, Afratis N, Tzanakakis GN, Karamanos NK. Targeting the tumor proteasome as a mechanism to control the synthesis and bioactivity of matrix macromolecules. Curr Mol Med. 2012;12:1068–1082. doi:10.2174/156652412802480943.
   PubMed Web of Science ®Google Scholar
• Terpos E, Christoulas D. Effects of proteasome inhibitors on bone cancer. Bonekey Rep. 2013;2(Article number: 395). doi:10.1038/bonekey.2013.129.
   PubMedGoogle Scholar
• Sasaki K, Hattori T, Fujisawa T, Takahashi K, Inoue H, Takigawa M. Nitric oxide mediates interleukin-1- induced gene expression of matrix metalloproteinases and basic fibroblast growth factor in cultured rabbit articular chondrocytes. J Biochem. 1998;123:431–439. doi:10.1093/oxfordjournals.jbchem.a021955.
   PubMed Web of Science ®Google Scholar
• Kheradmand F, Werner E, Tremble P, Symons M, Werb Z. Role of Rac1 and oxygen radicals in collagenase-1 expression induced by cell shape change. Science. 1998;280:898–902. doi:10.1126/science.280.5365.898.
   PubMed Web of Science ®Google Scholar
• Yu H, Ye WB, Zhong ZM, Ding RT, Chen JT. Effect of advanced oxidation protein products on articular cartilage and synovium in a rabbit osteoarthritis model. Orthop Surg. 2015;(7):161–167. doi:10.1111/os.12179.
   PubMedGoogle Scholar
• Lepetsos P, Papavassiliou AG. ROS/oxidative stress signaling in osteoarthritis. Biochim Biophys Acta Molecular Basis of Disease. 2016;1862(4):576–591. doi:10.1016/j.bbadis.2016.01.003.
   PubMed Web of Science ®Google Scholar
• Soloviev A, Schwarz EM, Kuprash DV, Nedospasov SA, Puzas JE, Rosier RN, O‘Keefe RJ. The role of p105 protein in NF kappa B activation in ANA-1 murine macrophages following stimulation with titanium particles. J Orthop Res. 2002;20(4):714–722. doi:10.1016/S0736-0266(02)00071-2.
   PubMed Web of Science ®Google Scholar
• Chondrogianni N, Stratford FL, Trougakos IP, Friguet B, Rivett JA, Gonos ES. Central role of the proteasome in senescence and survival of human fibroblasts - induction of a senescence-like phenotype upon its inhibition and resistance to stress upon its activation. J Biol Chem. 2003;278:28026–28037. doi:10.1074/jbc.M301048200.
   PubMed Web of Science ®Google Scholar
• Meng L, Mohan R, Kwok BH, Elofsson M, Sin N, Crews CM. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Pnas. 1999;96(18):10403–10408. doi:10.1073/pnas.96.18.10403.
   PubMed Web of Science ®Google Scholar
• Sabokbar A, Rushton N. Role of inflammatory mediators and adhesion molecules in the pathogenesis of aseptic loosening in total hip arthroplasties. J Arthroplasty. 1995;10(6):810–816.
   PubMed Web of Science ®Google Scholar
• Konttinen YT, Xu JW, Waris E, Li TF, Gomez-Barrena E, Nordsletten L, Santavirta S. Interleukin-6 in aseptic loosening of total hip replacement prostheses. Clin Exp Rheumatol. 2002;20(4):485–490.
   PubMed Web of Science ®Google Scholar
• Moutzouris JP, Che W, Ramsay EE, Manetsch M, Alkhouri H, Bjorkman AM, Schuster F, Ge Q, Ammit AJ. Proteasomal inhibition upregulates the endogenous MAPK deactivator MKP-1 in human airway smooth muscle: mechanism of action and effect on cytokine secretion. Biochim Biophys Acta. 2010;1803:416–423. doi:10.1016/j.bbamcr.2009.12.007.
   PubMed Web of Science ®Google Scholar
• Hideshima T, Richardson P, Chauhan D, Palombella VJ, Elliott PJ, Adams J, Anderson KC. The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells. Cancer Res. 2001;61:3071–3076.
   PubMed Web of Science ®Google Scholar
• Henrotin YE, Zheng SX, Deby GP, Labasse AH, Crielaard JM, Reginster JY. Nitric oxide downregulates interleukin 1beta (IL-1beta) stimulated IL-6, IL-8, and prostaglandin E2 production by human chondrocytes. J Rheumatol. 1998;25:1595–1601.
   PubMed Web of Science ®Google Scholar
• Ginn-Pease ME, Whisler RL. Redox signals and NF-kappa B activation in T cells. Free Radic Biol Med. 1998;25:346–361. doi:10.1016/S0891-5849(98)00067-7.
   PubMed Web of Science ®Google Scholar
• Clark IM, Swingler TE, Sampieri CL, Edwards DR. The regulation of matrix metalloproteinases and their inhibitors. Int J Biochem Cell Biol. 2008;40:1362–1378. doi:10.1016/j.biocel.2008.02.019.
   PubMed Web of Science ®Google Scholar
• Goffin L, Seguin-Estévez Q, Alvarez M, Reith W, Chizzolini C. Transcriptional regulation of matrix metalloproteinase-1 and collagen 1A2 explains the anti-fibrotic effect exerted by proteasome inhibition in human dermal fibroblasts. Arthritis Res Ther. 2010;12(2):R73. doi:10.1186/ar2991.
   PubMed Web of Science ®Google Scholar
• Lu J, Guo JH, Tu XL, Zhang C, Zhao M, Zhang QW, Gao FH. Tiron Inhibits UVB-Induced AP-1 Binding Sites Transcriptional Activation on MMP-1 and MMP-3 Promoters by MAPK Signaling Pathway in Human Dermal Fibroblasts. PLoS One. 2016;11(8):e0159998. doi:10.1371/journal.pone.0159998.
   PubMed Web of Science ®Google Scholar
• Kypriotou M, Beauchef G, Chadjichristos C, Widom R, Renard E, Jimenez SA, Korn J, Maquart FX, Oddos T, Von Stetten O, Pujol JP, Galera P. Human collagen Krox up-regulates type I collagen expression in normal and scleroderma fibroblasts through interaction with Sp1 and Sp3 transcription factors. J Biol Chem. 2007;282:32000–32014. doi:10.1074/jbc.M705197200.
   PubMed Web of Science ®Google Scholar
• Awasthi N, Wang-Su ST, Wagner BJ. Downregulation of MMP-2 and −9 by proteasome inhibition: a possible mechanism to decrease LEC migration and prevent posterior capsular opacification. Invest Ophthalmol Vis Sci. 2008;49(5):1998–2003. doi:10.1167/iovs.07-0624.
   PubMed Web of Science ®Google Scholar
• Ye J, Qing Z, Ma J, Wang Z. Effect of proteasome inhibitor on NF-κB and MMP-9 expression in synovial tissues of osteoarthritis rats. Int J Clin Exp Med. 2017;10(1):402–409.
   Web of Science ®Google Scholar
• Vandooren J, Knoops S, Aldinucci Buzzo JL, Boon L, Martens E, Opdenakker G, Kolaczkowska E. Differential inhibition of activity, activation and gene expression of MMP-9 in THP-1 cells by azithromycin and minocycline versus bortezomib: A comparative study. PLoS One. 2017;12(4):e0174853. doi:10.1371/journal.pone.0174853.
   PubMed Web of Science ®Google Scholar
• Hu W, Zhang W, Li F, Guo F, Chen A. Bortezomib prevents the expression of MMP-13 and the degradation of collagen type 2 in human chondrocytes. Biochem Biophys Res Commun. 2014;452(3):526–530. doi:10.1016/j.bbrc.2014.08.102.
   PubMed Web of Science ®Google Scholar
• Xiao Y-P, Tian F-M, Dai M-W, Wang W-Y, Shao L-T, Zhang L. Are estrogen-related drugs new alternatives for the management of osteoarthritis? Arthritis Res Ther. 2016;18:151. doi:10.1186/s13075-016-1045-7.
   PubMed Web of Science ®Google Scholar
• Chen H, Zhu H, Zhang K, Chen K, Yang H. Estrogen deficiency accelerates lumbar facet joints arthritis. Sci Rep. 2017;7(1):1379. doi:10.1038/s41598-017-01427-7.
   PubMedGoogle Scholar
• Karsdal MA, Bay-Jensen AC, Leeming DJ, Henriksen K, Christiansen C. The pathogenesis of osteoarthritis involves bone, cartilage and synovial inflammation: may estrogen be a magic bullet? Menopause Int. 2012;18(4):139–146. doi:10.1258/mi.2012.012025.
   PubMedGoogle Scholar
• Roman-Blas JA, Castañeda S, Largo R, Herrero-Beaumont G. Osteoarthritis associated with estrogen deficiency. Arthritis Res Ther. 2009;11:241. doi:10.1186/ar2684.
   PubMed Web of Science ®Google Scholar
• Reed JL, Dimayuga FO, Davies LM, Keller JN, Bruce-Keller AJ. Estrogen increases proteasome activity in murine microglial cells. Neurosci Lett. 2004;367(1):60–65. doi:10.1016/j.neulet.2004.05.077.
   PubMed Web of Science ®Google Scholar
• Huang L, Chen CH. Proteasome regulators: activators and inhibitors. Curr Med Chem. 2009;16(8):931–939. doi:10.2174/092986709787581860.
   PubMed Web of Science ®Google Scholar
• Stadtmueller BM, Hill CP. Proteasome activators. Mol Cell. 2011;41:8–19. doi:10.1016/j.molcel.2010.12.020.
   PubMed Web of Science ®Google Scholar