Urinary matrix metalloproteinase -8, -9, -14 and their regulators (TRY-1, TRY-2, TATI) in patients with diabetic nephropathy

References

• Zaoui P, Cantin J, Alimardani-Bessette M, Monier F, Halimi S, Morel F, et al. Role of metalloproteinases and inhibitors in the occurrence and progression of diabetic renal lesions. Diabetes Metab. 2000; 26(Suppl 4)25–9
   Google Scholar
• Egeblad M, Werb Z. New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer. 2002; 2: 161–74
   PubMed Web of Science ®Google Scholar
• Owen CA, Hu Z, Lopez-Otin C, Shapiro SD. Membrane-bound matrix metalloproteinase-8 on activated polymorphonuclear cells is a potent, tissue inhibitor of metalloproteinase-resistant collagenase and serpinase. J Immunol. 2004; 72: 7791–803
   Google Scholar
• Gueders MM, Balbin M, Rocks N, Foidart JM, Gosset P, Louis R, et al. Matrix metalloproteinase-8 deficiency promotes granulocytic allergen-induced airway inflammation. J Immunol. 2005; 175: 2589–97
   PubMed Web of Science ®Google Scholar
• Lauhio A, Sorsa T, Lindy O, Suomalainen K, Saari H, Golub LM, et al. The anticollagenolytic potential of lymecycline in the long-term treatment of reactive arthritis. Arthritis Rheum. 1992; 35: 195–8
   PubMed Web of Science ®Google Scholar
• Sorsa T, Salo T, Koivunen E, Tyynelä J, Konttinen Y, Bergmann U, et al. Activation of type IV procollagenases by human tumor-associated trypsin-2. J Biol Chem. 1997; 272: 21067–74
   PubMed Web of Science ®Google Scholar
• Marti HP. The role of matrix metalloproteinases in the activation of mesangial cells. Transpl Immunol. 2002; 9: 97–110
   PubMed Web of Science ®Google Scholar
• Holopainen JM, Moilanen JA, Sorsa T, Kivela-Rajamaki M, Tervahartiala T, Vesaluoma MH, et al. Activation of matrix metalloproteinas-8 by membrane type 1-MMP and their expression in human tears after photorefractive keratectomy. Invest Ophthalmol Vis Sci. 2003; 44: 2550–6
   PubMed Web of Science ®Google Scholar
• Moilanen M, Sorsa T, Stenman M, Nyberg P, Lindy O, Vesterinen J, et al. Tumor-associated trypsinogen-2 (trypsinogen-2) activates procollagenases (MMP-1, -8, -13) and stromelysin-1 (MMP-3) and degrades type I collagen. Biochemistry. 2003; 42: 5414–20
   PubMed Web of Science ®Google Scholar
• Ebihara I, Nakamura T, Shimada N, Koide H. Increased plasma metalloproteinase-9 concentrations precede development of microalbuminuria in non-insulin-dependent diabetes mellitus. Am J Kidney Dis. 1998; 32: 544–50
   PubMed Web of Science ®Google Scholar
• Tashiro K, Koyanagi I, Ohara I, Ito T, Saitoh A, Horikoshi S, et al. Levels of urinary matrix metalloproteinase-9 (MMP-9) and renal injuries in patients with type 2 diabetic nephropathy. J Clin Lab Anal. 2004; 18: 206–10
   PubMedGoogle Scholar
• Honkanen E, Teppo AM, Törnroth T, Groop PH, Grönhagen-Riska. Urinary transforming growth factor--1 in membranous glomerulonephritis. Nephrol Dial Transplant. 1997;12:2562–8.
   PubMed Web of Science ®Google Scholar
• Lindy O, Konttinen YT, Sorsa T, Ding Y, Santavirta S, Ceponis A, et al. Matrix metalloproteinase 13 (collagenase 3) in human rheumatoid synovium. Arthritis Rheum. 1997; 40: 1391–9
   PubMed Web of Science ®Google Scholar
• Maisi P, Prikk K, Sepper R, Pirilä E, Salo T, Hietanen J, et al. Soluble membrane-type 1 matrix metalloproteinase (MT1-MMP) and gelatinase A (MMP-2) in induced sputum and bronchoalveolar lavage fluid of human bronchial asthma and bronchiectasis. APMIS. 2002; 110: 771–82
   PubMed Web of Science ®Google Scholar
• Prikk K, Maisi P, Pirilä E, Reintman MA, Salo T, Sorsa T, et al. Airway obstruction correlates with collagenase-2 (MMP-8) expression and activation in bronchial asthma. Lab Invest. 2002; 82: 1535–45
   PubMed Web of Science ®Google Scholar
• Sorsa T, Ding Y, Salo T, Lauhio A, Teronen O, Ingman T, et al. Effects of tetracyclines on neutrophil, gingival, and salivary collagenases. A functional and western-blot assessment with special reference to their cellular sources in periodontal diseases. Ann N Y Acad Sci. 1994; 732: 112–31
   PubMed Web of Science ®Google Scholar
• Hanemaaijer R, Sorsa T, Konttinen YT, Ding Y, Sutinen M, Visser H, et al. Matrix metalloproteinase-8 is expressed in rheumatoid synovial fibroblasts and endothelial cells. Regulation by tumor necrosis factor-alpha and doxycycline. J Biol Chem. 1997; 272: 31504–9
   PubMed Web of Science ®Google Scholar
• Lee HM, Golub LM, Cao J, Teronen O, Laitinen M, Salo T, et al. CMT-3, a non-antimicrobial tetracycline (TC), inhibits MT1-MMP activity: relevance to cancer. Curr Med Chem. 2001; 8: 257–60
   Google Scholar
• Lukkonen A, Sorsa T, Salo T, Tervahartiala T, Koivunen E, Golub L, et al. Down-regulation of trypsinogen-2 expression by chemically modified tetracyclines: association with reduced cancer cell migration. Int J Cancer. 2000; 86: 577–81
   PubMed Web of Science ®Google Scholar
• Paju A, Sorsa T, Tervahartiala T, Koivunen E, Haglund C, Leminen A, et al. The levels of trypsinogen isoenzymes in ovarian tumour cyst fluids are associated with promatrix metalloproteinase-9 but not promatrix metalloproteinase-2 activation. Br J Cancer. 2001; 84: 1363–71
   PubMed Web of Science ®Google Scholar
• Itkonen O, Koivunen E, Hurme M, Alfthan H, Schroder T, Stenman UH. Time-resolved immunofluorometric assays for trypsinogen-1 and 2 in serum reveal preferential elevation of trypsinogen-2 in pancreatitis. J Lab Clin Med. 1990; 115: 712–8
   PubMed Web of Science ®Google Scholar
• Osman S, Turpeinen U, Itkonen O, Stenman UH. Activation of a time-resolved immunofluorometric assay for tumor-associated trypsin inhibitor (TATI) using the streptavidin-biotin system. J Immunol Methods. 1993; 161: 97–106
   PubMed Web of Science ®Google Scholar
• Hedstrom J, Leinonen J, Sainio V, Stenman UH. Time-resolved immunofluorometric assay of trypsin-2 complexed with alpha 1-antitrypsin in serum. Clin Chem. 1994; 40: 1761–5
   PubMed Web of Science ®Google Scholar
• Gutierrez-Fernnandez A, Inada M, Balbin M, Fueyo A, Ana S, Pitiot AS, et al. Increased inflammation delays wound healing in mice deficient collagenase-2 (MMP-8). FASEB J. 2007; 21: 2580–91
   Google Scholar
• Kazes I, Delarue F, Hagege JN, Bouzhir-Sima L, Rondeau E, Sraer JD, et al. Soluble latent membrane-type 1 matrix metalloproteinase secreted by human mesangial cells is activated by urokinase. Kidney Int. 1998; 54: 1976–84
   PubMed Web of Science ®Google Scholar
• Zhang Y, Wu XH, Cao GH, Li S. Relationship between expression of matrix metalloproteinase-9 (MMP-9) and angiogenesis in renal cell carcinoma. Ai Zheng. 2004; 23: 326–9
   Google Scholar
• Tervahartiala T, Pirilä E, Ceponis A, Bouzhir-Sima L, Rondeau E, Sraer JD, et al. The in vivo expression of the collagenolytic matrix metalloproteinases (MMP-2, -8, -13, and -14) and matrilysin (MMP-7) in adult and localized juvenile periodontitis. J Dent Res. 2000; 79: 1969–77
   PubMed Web of Science ®Google Scholar
• Overall CM, Lopez-Otin C. Strategies for MMP inhibition in cancer: innovations for the post-trial era. Nat Rev Cancer. 2002; 2: 657–72
   PubMed Web of Science ®Google Scholar
• Strongin AY, Collier I, Bannikov G, Marmer BL, Grant GA, Goldberg GI. Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J Biol Chem. 1995; 270: 5331–8
   PubMed Web of Science ®Google Scholar
• Knäuper V, Smith B, Lopez-Otin C, Murphy G. Activation of progelatinase B (proMMP-9) by active collagenase-3 (MMP-13). Eur J Biochem. 1997; 248: 369–73
   PubMedGoogle Scholar
• McLennan SV, Martell SY, Yue DK. High glucose concentration inhibits the expression of membrane type metalloproteinase by mesangial cells: possible role in mesangium accumulation. Diabetologia. 2000; 43: 642–8
   PubMed Web of Science ®Google Scholar
• Kolb SA, Lahrtz F, Paul R, Leppert D, Nadal D, Pfister HW, et al. Matrix metalloproteinases and tissue inhibitors of metalloproteinases in viral meningitis: upregulation of MMP-9 and TIMP-1 in cerebrospinal fluid. J Neuroimmunol. 1998; 84: 143–50
   PubMed Web of Science ®Google Scholar
• Adler AI, Stevens RJ, Manley SE, Bilous RW, Cull CA, Holman RR, et al. Development and progression of nephropathy in type 2 diabetes: the United Kingdom Prospective Diabetes Study (UKPDS 64). Kidney Int. 2003; 63: 225–32
   PubMed Web of Science ®Google Scholar
• Overall CM. Regulation of tissue inhibitor of matrix metalloproteinase expression. Ann NY Acad Sci. 1994; 732: 51–64
   Google Scholar
• Chow FY, Nikolic-Paterson DJ, Atkins RC, Tesch GH. Macrophages in streptozotocin-induced diabetic nephropathy: potential role in renal fibrosis. Nephrol Dial Transplant. 2004; 19: 2987–96
   PubMed Web of Science ®Google Scholar
• Locatelli F, Pozzoni P, Vecchio LD. Renal replacement therapy in patients with diabetes and end-stage renal failure. J Am Soc Nephrol. 2004; 15: 25–9
   PubMed Web of Science ®Google Scholar
• Wolf G, Chen S, Ziyadeh FN. From the periphery of the glomerular capillary wall toward the center of disease. Diabetes. 2005; 54: 1626–34
   PubMed Web of Science ®Google Scholar
• Lauhio A, Konttinen YT, Tscesche H, Nordström D, Salo T, Lähdevirta J, et al. Reduction of matrix metalloproteinases 8-neutrophil collagenase levels during long-term doxycycline treatment of reactive arthritis. Antimicrob Agents Chemother. 1994; 38: 400–2
   PubMed Web of Science ®Google Scholar
• Lauhio A, Salo T, Ding Y, Konttinen YT, Nordström D, Tschesche H, et al. In vivo inhibition of human neutrophil collagenase (MMP-8) activity during long-term combination therapy of doxycycline and non-steroidal anti-inflammatory drugs (NSAID) in acute reactive arthritis. Clin Exp Immunol. 1994; 98: 21–8
   PubMed Web of Science ®Google Scholar
• Golub LM, Lee HM, Ryan ME, Giannobile WV, Payne J, Sorsa T. Tetracyclines inhibit connective tissue breakdown by multiple non-antimicrobial mechanisms. Adv Dent Res. 1998; 12: 12–26
   PubMedGoogle Scholar
• Suomalainen K, Sorsa T, Golub LM, Ramamurthy N, Lee HM, Uitto VJ, et al. Specificity of the anticollagenase action of tetracyclines: relevance to their anti-inflammatory potential. Antimicrob Agents Chemother. 1992; 36: 227–9
   PubMed Web of Science ®Google Scholar
• Lauhio A, Salo T, Tjäderhane L, Lähdevirta J, Golub LM, Sorsa T. Tetracyclines in treatment of rheumatoid arthritis. Lancet. 1995; 346: 645–6
   PubMed Web of Science ®Google Scholar
• Greenwald RA, Golub LM, Ramamurthy NS, Chowdhury M, Moak SA, Sorsa T. In vitro sensitivity of the three mammalian collagenases to tetracycline inhibition: relationship to bone and cartilage degradation. Bone. 1998; 22: 33–8
   PubMed Web of Science ®Google Scholar
• Sorsa T, Ramamurthy NS, Vernillo AT, Zhang X, Konttinen YT, Rifkin BR, et al. Functional sites of chemically modified tetracyclines: inhibition of the oxidative activation of human neutrophil and chicken osteoclast pro-matrix metalloproteinases. J Rheumatol. 1998; 25: 975–8
   PubMed Web of Science ®Google Scholar
• Emingil G, Atilla G, Sorsa T, Savolainen P, Baylas H. Effectiveness of adjunctive low-dose doxycycline therapy on clinical parameters and gingival crevicular fluid laminin-5-gamma2 chain levels in chronic periodontitis. J Periodontol. 2004; 75: 1387–96
   PubMed Web of Science ®Google Scholar
• Sorsa T, Tjäderhane L, Salo T. Matrix metalloproteinases (MMPs) in oral diseases. Oral Dis. 2004; 10: 311–8
   PubMed Web of Science ®Google Scholar
• Meyer B, Meyer B, Salvatore M. Tetracyclines and chloramphenicol. Principles and practice of infectious diseases6th ed, D Mandell, G Bennett, R Douglas, JE Bennett, R Dolin. Elsevier, Churchill Livingstone, Philadelphia 2005; 356–72
   Google Scholar
• Naini EA, Harandi AA, Moghtaderi J, Bastani B, Amiran A. Doxycycline: a pilot study to reduce diabetic proteinuria. Am J Nephropathol. 2007; 27: 269–73
   PubMed Web of Science ®Google Scholar
• Ahuja TS. Doxicycline decreases proteinuria in glomerulonephritis. Am J Kidney Dis. 2003; 42: 376–80
   PubMed Web of Science ®Google Scholar
• Diamant M, Hanemaaijer R, Verheijen JH, Smith JW, Lemkes H. Elevated matrix metalloproteinase-2 and -9 in urine, but not in serum, are markers of type I diabetic nephropathy. Diabet Med. 2001; 18: 423–4
   Web of Science ®Google Scholar
• Chang HR, Yang SF, Li ML, Lin CC, Hsieh YS, Lian JD. Relationships between circulating matrix metalloproteinases -2 and -9 and renal function in patients with chronic kidney diseases. Clin Chim Acta. 2006; 366: 243–8
   PubMed Web of Science ®Google Scholar
• El Nahas MA, Bello AK. Chronic kidney disease: the global challenge. Lancet. 2005; 365: 331–40
   PubMed Web of Science ®Google Scholar
• Van Dijk PC, Jager KJ, Stengel B, Grönhagen-Riska C, Feest TG, Briggs JD. Renal replacement therapy for diabetic end-stage renal disease: data from 10 registries in Europe (1991–2000). Kidney Int. 2005; 67: 1489–99
   PubMed Web of Science ®Google Scholar