Serum MMP-7 is increased in diabetic renal disease and diabetic diastolic dysfunction

Diabetes Research and Clinical Practice

Volumn 87, Issue 3, 2010, Pages 335-341

  Ban, C R ^a,b   Twigg, S M ^b,c   Franjic, B ^c   Brooks, B A ^b,c   Celermajer, D ^c   Yue, D K ^b,c   McLennan, S V ^b,c  

^a Alesd Hospital   (Romania)

^b UNIVERSITY OF SYDNEY   (Australia)

^c ROYAL PRINCE ALFRED HOSPITAL   (Australia)

Author keywords

Albuminuria; Diabetic complications; Diastolic dysfunction; Echocardiographic indices; MMP 7

Indexed keywords

COLLAGEN; GELATINASE A; GELATINASE B; HEMOGLOBIN A1C; INTERSTITIAL COLLAGENASE; MATRILYSIN; PROCOLLAGEN; PROCOLLAGEN TYPE 3 AMINOPROPEPTIDE; STROMELYSIN; TISSUE INHIBITOR OF METALLOPROTEINASE 1;

ALBUMINURIA; ARTICLE; BLOOD PRESSURE MEASUREMENT; CLINICAL ARTICLE; COLLAGEN DEGRADATION; CONTROLLED STUDY; DIABETIC NEPHROPATHY; DIASTOLIC BLOOD PRESSURE; DIASTOLIC DYSFUNCTION; DISEASE SEVERITY; ENZYME LINKED IMMUNOSORBENT ASSAY; FEMALE; GLOMERULUS FILTRATION; HUMAN; MALE; NON INSULIN DEPENDENT DIABETES MELLITUS; PROTEIN BLOOD LEVEL; RADIOIMMUNOASSAY; SYSTOLIC BLOOD PRESSURE; ZYMOGRAPHY;

AGED; CARDIOMYOPATHIES; DIABETES MELLITUS, TYPE 2; DIABETIC NEPHROPATHIES; ECHOCARDIOGRAPHY; ENZYME-LINKED IMMUNOSORBENT ASSAY; FEMALE; HUMANS; MALE; MATRIX METALLOPROTEINASES, SECRETED; MIDDLE AGED; NAPHTHALENES; OXEPINS; TISSUE INHIBITOR OF METALLOPROTEINASE-1;

EID: 77649179598     PISSN: 01688227     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.diabres.2010.01.004     Document Type: Article

References (47)

1. Scheinman J.I., Fish A.J., and Michael A.F. The immunohistopathology of glomerular antigens. The glomerular basement membrane, collagen, and actomyosin antigens in normal and diseased kidneys. J Clin Invest 54 (1974) 1144-1154
2. Makino H., Yamasaki Y., Haramoto T., Shikata K., Hironaka K., Ota Z., and Kanwar Y.S. Ultrastructural changes of extracellular matrices in diabetic nephropathy revealed by high resolution scanning and immunoelectron microscopy. Lab Invest 68 (1993) 45-55
3. Ikeda S., Makino H., Haramoto T., Shikata K., Kumagai I., and Ota Z. Changes in glomerular extracellular matrices components in diabetic nephropathy. J Diabet Complications 5 (1991) 186-198
4. Farquhar A., MacDonald M.K., and Ireland J.T. The role of fibrin deposition in diabetic glomerulosclerosis: a light, electron and immunofluorescence microscopy study. J Clin Pathol 25 (1972) 657-667
5. Thompson E.W. Structural manifestations of diabetic cardiomyopathy in the rat and its reversal by insulin treatment. Am J Anat 182 (1988) 270-282
6. Bakth S., Arena J., Lee W., Torres R., Haider B., Patel B.C., Lyons M.M., and Regan T.J. Arrhythmia susceptibility and myocardial composition in diabetes. Influence of physical conditioning. J Clin Invest 77 (1986) 382-395
7. Nelson R.G., Bennett P.H., Beck G.J., Tan M., Knowler W.C., Mitch W.E., and Hirschman G.H. et al, Development and progression of renal disease in Pima Indians with non-insulin-dependent diabetes mellitus. Diabetic Renal Disease Study Group. N Engl J Med 335 (1996) 1636-1642
8. Schannwell C.M., Schneppenheim M., Perings S., Plehn G., and Strauer B.E. Left ventricular diastolic dysfunction as an early manifestation of diabetic cardiomyopathy. Cardiology 98 (2002) 33-39
9. Fang Z.Y., Prins J.B., and Marwick T.H. Diabetic cardiomyopathy: evidence, mechanisms, and therapeutic implications. Endocr Rev 25 (2004) 543-567
10. Razzaque M.S., Koji T., Taguchi T., Harada T., and Nakane P.K. In situ localization of type III and type IV collagen-expressing cells in human diabetic nephropathy. J Pathol 174 (1994) 131-138
11. Glick A.D., Jacobson H.R., and Haralson M.A. Mesangial deposition of type I collagen in human glomerulosclerosis. Hum Pathol 23 (1992) 1373-1379
12. Stokes M.B., Holler S., Cui Y., Hudkins K.L., Eitner F., Fogo A., and Alpers C.E. Expression of decorin, biglycan, and collagen type I in human renal fibrosing disease. Kidney Int 57 (2002) 487-498
13. Schaefer L., Raslik I., Grone H.J., Schonherr E., Macakova K., Ugorcakova J., Budny S., et al. Small proteoglycans in human diabetic nephropathy: discrepancy between glomerular expression and protein accumulation of decorin, biglycan, lumican, and fibromodulin. Faseb J 15 (2001) 559-561
14. Makino H., Shikata K., Wieslander J., Wada J., Kashihara N., Yoshioka K., and Ota Z. Localization of fibril/microfibril and basement membrane collagens in diabetic glomerulosclerosis in type 2 diabetes. Diabet Med 11 (1994) 304-311
15. Makino H., Kashihara N., Sugiyama H., Kanao K., Sekikawa T., Okamoto K., Maeshima Y., et al. Phenotypic changes of the mesangium in diabetic nephropathy. J Diabetes Complications 9 (1996) 282-284
16. Zannad F., Alla F., Dousset B., Perez A., and Pitt B. Limitation of excessive extracellular matrix turnover may contribute to survival benefit of spironolactone therapy in patients with congestive heart failure: insights from the randomized aldactone evaluation study (RALES). Rales Investigators, Circulation 102 (2002) 2700-2706
17. D'Armiento J. Matrix metalloproteinase disruption of the extracellular matrix and cardiac dysfunction, rends. Cardiovasc Med 12 (2002) 97-101
18. Bishop J.E., and Laurent G.J. Collagen turnover and its regulation in the normal and hypertrophying heart. Eur Heart J 16 Suppl C (1995) 38-44
19. Weber K.T. Extracellular matrix remodeling in heart failure: a role for de novo angiotensin II generation. Circulation 96 (1997) 4065-4082
20. Risteli J., and Risteli L. Analysing connective tissue metabolites in human serum. Biochemical, physiological and methodological aspects. J Hepatol 22 (1995) 77-81
21. Jensen L.T., Horslev-Petersen K., Toft P., Bentsen K.D., Grande P., Simonsen E.E., and Lorenzen I. Serum aminoterminal type III procollagen peptide reflects repair after acute myocardial infarction. Circulation 81 (1990) 52-57
22. Fleischmajer R., Perlish J.S., and Timpl R. Collagen fibrillogenesis in human skin. Ann N Y Acad Sci 460 (1985) 246-257
23. McLennan S.V., Kelly D.J., Schache M., Waltham M., Dy V., Langham R.G., Yue D.K., et al. Advanced glycation end products decrease mesangial cell MMP-7: a role in matrix accumulation in diabetic nephropathy?. Kidney Int 72 (2007) 481-488
24. Brooks B.A., Franjic B., Ban C.R., Swaraj K., Yue D.K., Celermajer D.S., and Twigg S.M. Diastolic dysfunction and abnormalities of the microcirculation in type 2 diabetes. Diabetes Obes Metab 10 (2008) 739-746
25. Levey A.S., Bosch J.P., Lewis J.B., Greene T., Rogers N., and Roth D. A more accurate method to estimate glomerular filtration rate from serum creatinine: a new prediction equation. Modification of Diet in Renal Disease Study Group. Ann Intern Med 130 (1990) 461-470
26. Lubien E., DeMaria A., Krishnaswamy P., Clopton P., Koon J., Kazanegra R., Gardetto N., et al. Utility of B-natriuretic peptide in detecting diastolic dysfunction: comparison with Doppler velocity recordings. Circulation 105 (2002) 595-601
27. Min D., Lyons J.G., Jia J., Lo L., and McLennan S.V. 2-Methoxy-2,4-diphenyl-3(2H)-furanone-labeled gelatin zymography and reverse zymography: a rapid real-time method for quantification of matrix metalloproteinases-2 and -9 and tissue inhibitors of metalloproteinases. Electrophoresis 27 (2006) 357-364
28. Nakamura T., Fukui M., Ebihara I., Osada S., Tomino Y., and Koide H. Abnormal gene expression of matrix metalloproteinases and their inhibitor in glomeruli from diabetic rats. Ren Physiol Biochem 17 (1994) 316-325
29. Ishimura E., Nishizawa Y., Shoji S., and Mori H. Serum type III, IV collagens and TIMP in patients with type II diabetes mellitus. Life Sci 58 (1996) 1331-1337
30. Shankland S.J., Ly H., Thai K., and Scholey J.W. Glomerular expression of tissue inhibitor of metalloproteinase (TIMP-1) in normal and diabetic rats. J Am Soc Nephrol 7 (1996) 97-104
31. Suzuki D., Miyazaki M., Jinde K., Koji T., Yagame M., Endoh M., Nomoto Y., et al. In situ hybridization studies of matrix metalloproteinase-3, tissue inhibitor of metalloproteinase-1 and type IV collagen in diabetic nephropathy. Kidney Int 52 (1997) 111-119
32. Li Y.Y., Feldman A.M., Sun Y., and McTiernan C.F. Differential expression of tissue inhibitors of metalloproteinases in the failing human heart. Circulation 98 (1998) 1728-1734
33. Spinale F.G. Matrix metalloproteinases: regulation and dysregulation in the failing heart. Circ Res 90 (2002) 520-530
34. DiBattista J.A., Pelletier J.P., Zafarullah M., Iwata K., and Martel-Pelletier J. Interleukin-1 beta induction of tissue inhibitor of metalloproteinase (TIMP-1) is functionally antagonized by prostaglandin E2 in human synovial fibroblasts. J Cell Biochem 57 (1995) 619-629
35. Lichtinghagen R., Michels D., Haberkorn C.I., Arndt B., Bahr M., Flemming P., Manns M.P., et al. Matrix metalloproteinase (MMP)-2, MMP-7, and tissue inhibitor of metalloproteinase-1 are closely related to the fibroproliferative process in the liver during chronic hepatitis C. J Hepatol 34 (2001) 239-247
36. Huang C.C., Chuang J.H., Chou M.H., Wu C.L., Chen C.M., Wang C.C., Chen Y.S., et al. Matrilysin (MMP-7) is a major matrix metalloproteinase upregulated in biliary atresia-associated liver fibrosis. Mod Pathol 18 (2005) 941-950
37. Surendran K., Simon T.C., Liapis H., and McGuire J.K. Matrilysin (MMP-7) expression in renal tubular damage: association with Wnt4. Kidney Int 65 (2004) 2212-2222
38. Zuo F., Kaminski N., Eugui E., Allard J., Yakhini Z., Ben-Dor A., Lollini L., et al. Gene expression analysis reveals matrilysin as a key regulator of pulmonary fibrosis in mice and humans. Proc Natl Acad Sci USA 99 (2002) 6292-6297
39. Boixel C., Fontaine V., Rucker-Martin C., Milliez P., Louedec L., Michel J.B., Jacob M.P., et al. Fibrosis of the left atria during progression of heart failure is associated with increased matrix metalloproteinases in the rat. J Am Coll Cardiol 42 (2002) 336-344
40. Marti H.P., McNeil L., Thomas G., Davies M., and Lovett D.H. Molecular characterization of a low-molecular-mass matrix metalloproteinase secreted by glomerular mesangial cells as PUMP-1. Biochem J 285 Pt 3 (1992) 899-905
41. Abdel Wahab N., and Mason R.M. Modulation of neutral protease expression in human mesangial cells by hyperglycaemic culture. Biochem J 320 Pt 3 (1996) 777-783
42. Nilsson L., Jonasson L., Nijm J., Hamsten A., and Eriksson P. Increased plasma concentration of matrix metalloproteinase-7 in patients with coronary artery disease. Clin Chem 52 (2006) 1522-1527
43. Ausma J., Wijffels M., Thone F., Wouters L., Allessie M., and Borgers M. Structural changes of atrial myocardium due to sustained atrial fibrillation in the goat. Circulation 96 (1997) 3157-3163
44. Rucker-Martin C., Pecker F., Godreau D., et al. Dedifferentiation of atrial myocytes during atrial fibrillation: role of fibroblast proliferation in vitro. Cardiovasc Res 55 (2002) 38-52
45. Werb Z., Hembry R.M., Murphy G., and Aggeler J. Commitment to expression of the metalloendopeptidases, collagenase and stromelysin: relationship of inducing events to changes in cytoskeletal architecture. J Cell Biol 102 (1896) 697-702
46. Shiomi T., Inoki I., Kataoka F., Ohtsuka T., Hashimoto G., Nemori R., and Okada Y. Pericellular activation of proMMP-7 (promatrilysin-1) through interaction with CD151. Lab Invest 85 (2005) 1489-1506
47. Yu W.H., and Woessner Jr. J.F. Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7). J Biol Chem 275 (2000) 4183-4191