Plasma levels and zymographic activities of matrix metalloproteinases 2 and 9 in type II diabetics with peripheral arterial disease

Vascular Medicine

Volumn 10, Issue 1, 2005, Pages 1-6

  Signorelli, Salvatore Santo ^a,c   Malaponte, Grazia ^a   Libra, Massimo ^a   Di Pino, Luigi ^a   Celotta, Gabriella ^a   Bevelacqua, Valentina ^a   Petrina, Marcello ^a   Nicotra, Giuseppina S ^a   Indelicato, Manuela ^a   Navolanic, Patrick M ^a,b   Pennisi, Giuseppe ^a   Mazzarino, Maria Clorinda ^a  

^a UNIVERSITY OF CATANIA   (Italy)

^b EAST CAROLINA UNIVERSITY   (United States)

^c NONE   (Italy)

Author keywords

MMP 2; MMP 9; Type II diabetes; Vascular disease

Indexed keywords

BIOLOGICAL MARKER; GELATINASE A; GELATINASE B;

ADULT; AGED; ARTICLE; CONTROLLED STUDY; CORRELATION FUNCTION; DISEASE MARKER; ENZYME ACTIVITY; ENZYME BLOOD LEVEL; FEMALE; HUMAN; MAJOR CLINICAL STUDY; MALE; NON INSULIN DEPENDENT DIABETES MELLITUS; PERIPHERAL OCCLUSIVE ARTERY DISEASE; PERIPHERAL VASCULAR DISEASE; PRIORITY JOURNAL; VOLUNTEER; ZYMOGRAPHY;

AGED; BIOLOGICAL MARKERS; DIABETES MELLITUS, TYPE 2; DIABETIC ANGIOPATHIES; ENZYME-LINKED IMMUNOSORBENT ASSAY; FEMALE; HUMANS; MALE; MATRIX METALLOPROTEINASE 2; MATRIX METALLOPROTEINASE 9; MIDDLE AGED; PERIPHERAL VASCULAR DISEASES;

EID: 20844448886     PISSN: 1358863X     EISSN: None     Source Type: Journal    
DOI: 10.1191/1358863x05vm582oa     Document Type: Article

References (37)

1. Van den Steen PE, Opdenakker G, Wormald MR, Dwek RA, Rudd PM. Matrix remodelling enzymes, the protease cascade and glycosylation. Biochim Biophys Acta 2001; 1528: 61-63.
2. Borkakoti N. Structural studies of matrix metalloproteinases. J Mol Med 2000; 78: 261-68.
3. Gijbels K, Proost P, Masure S, Carton H, Billisu A, Opdenakker G. Gelatinase B is present in the cerebrospinal fluid during experimental autoimmune encephalomyelitis and cleaves myelin basic protein. J Neurosci Res 1993; 36: 432-40.
4. Ito A, Mukaiyama A, Itoh Y et al. Degradation of interleukin 1β by matrix metalloproteinases. J Biol Chem 1996; 271: 14 657-60.
5. Gearing AJH, Beckett P, Christodoulou M et al. Processing of tumour necrosis factor-α precursor by metalloproteinases. Nature 1994; 370: 555-57.
6. Bartholome EJ, Van Aelst I, Koyen E et al. Human monocyte-derived dendritic cells produce bioactive gelatinase B: inhibition by IFN-β. J Interferon Cytokine Res 2001; 21: 495-501.
7. Lein M, Nowak L, Jung K et al. Analytical aspects regarding the measurement of metalloproteinases and their inhibitors in blood. Clin Biochem 1997; 30: 491-96.
8. Sawicki G, Sanders EJ, Salas E, Wozniak M, Rodrigo J, Radomski MW. Localization and translocation of MMP-2 during aggregation of human platelets. Thromb Haemost 1998; 80: 836-39.
9. Creemers EE, Cleutjens JP, Smits JF, Daemen MJ. Matrix metalloproteinase inhibition after myocardial infarction: a new approach to prevent heart failure? Circ Res 2001; 89: 201-10.
10. Itoh Y, Nagase H. Matrix metalloproteinases in cancer. Essays Biochem 2002; 38: 21-36.
11. Death AK, Fisher EJ, McGrath KC, Yue DK. High glucose alters matrix metalloproteinase expression in two key vascular cells: potential impact on atherosclerosis in diabetes. Atherosclerosis 2003; 168: 263-69.
12. Uzui H, Harpf A, Liu M et al. Increased expression of membrane type 3-matrix metalloproteinase in human atherosclerotic plaque: role of activated macrophages and inflammatory cytokines. Circulation 2002; 106: 3024-30.
13. 1, attenuates myocardial ischemia-reperfusion injury via inhibition of upregulation of MMP-1. Am J Physiol Heart Circ Physiol 2003; 284: 1612-17.
14. Gurjar MV, DeLeon J, Sharma RV, Bhalla RC. Mechanism of inhibition of matrix metalloproteinase-9 induction by NO in vascular smooth muscle cells. J Appl Physiol 2001; 91: 1380-86.
15. Brew K, Dinakarpandian D, Nagase H. Tissue inhibitors of metalloproteinases: evolution, structure and function. Biochim Biophys Acta 2000; 1477: 267-83.
16. Visse R, Nagase H. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ Res 2003; 92: 827-39.
17. Dollery CM, McEwan JR, Henney AM. Matrix metalloproteinases and cardiovascular disease. Circ Res 1995; 77: 863-68.
18. Gohlke U, Gomis-Ruth FX, Crabbe T, Murphy G, Docherty AJ, Bode W. The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function. FEBS Lett 1996; 378: 126-30.
19. Asanuma K, Magid R, Johnson C, Nerem RM, Galis ZS. Uniaxial strain upregulates matrix-degrading enzymes produced by human vascular smooth muscle cells. Am J Physiol Heart Circ Physiol 2003; 284: H1778-84.
20. Opdenakker G, Van den Steen PE, Dubois B et al. Gelatinase B functions as regulator and effector in leukocyte biology. J Leukoc Biol 2001; 69: 571-79.
21. Galis ZS, Khatri JJ. Matrix metalloproteinases in vascular remodeling and atherogenesis: the good, the bad, and the ugly. Circ Res 2002; 90: 251-62.
22. Galis ZS, Johnson C, Godin D et al. Targeted disruption of the matrix metalloproteinase-9 gene impairs smooth muscle cell migration and geometrical arterial remodeling. Circ Res 2002; 91: 852-59.
23. Galis ZS, Sukhova GK, Lark MW, Libby P. Increased expression of matrix metalloproteinases and matrix degrading activity in vulnerable regions of human atherosclerotic plaques. J Clin Invest 1994; 94: 2493-503.
24. Shah PK, Galis ZS. Matrix metalloproteinase hypothesis of plaque rupture: players keep piling up but questions remain. Circulation 2001; 104: 1878-80.
25. Gao CQ, Sawicki G, Suarez-Pinzon WL et al. Matrix metalloproteinase-2 mediates cytokine-induced myocardial contractile dysfunction. Cardiovasc Res 2003; 57: 426-33.
26. Shah PK, Falk E, Badimon JJ et al. Human monocyte-derived macrophages induce collagen breakdown in fibrous caps of atherosclerotic plaques: potential role of matrix-degrading metalloproteinases and implications for plaque rupture. Circulation 1995; 92: 1565-69.
27. Schneider DJ, Sobel BE. Determinants of coronary vascular disease in patients with type II diabetes mellitus and their therapeutic implications. Clin Cardiol 1997; 20: 433-40.
28. Lorenzl S, Albers DS, Narr S, Chirichigno J, Beal MF. Expression of MMP-2, MMP-9, and MMP-1 and their endogenous counterregulators TIMP-1 and TIMP-2 in postmortem brain tissue of Parkinson's disease. Exp Neurol 2002; 178: 13-20.
29. Gruber BL, Sorbi D, French DL et al. Markedly elevated serum MMP-9 (gelatinase B) levels in rheumatoid arthritis: a potentially useful laboratory marker. Clin Immunol Immunopathol 1996; 78: 161-71.
30. Signorelli S, Mazzarino MC, Di Pino L et al. High circulating levels of cytokines (IL-6 and TNFalpha), adhesion molecules (VCAM-1 and ICAM-1) and selectins in patients with peripheral arterial disease at rest and after a treadmill test. Vasc Med 2003; 8: 15-19.
31. Ridker PM, Hennekens CH, Buring JE, Rifai N. C-reactive protein and other markers of inflammation in the prediction of cardiovascular disease in women. N Engl J Med 2000; 342: 836-43.
32. Pradhan AD, Manson JE, Rifai N, Buring JE, Ridker PM. C-reactive protein, interleukin 6, and risk of developing type 2 diabetes mellitus. JAMA 2001; 286: 327-34.
33. Loftus IM, Naylor AR, Bell PR, Thompson MM. Plasma MMP-9 - a marker of carotid plaque instability. Eur J Vasc Endovasc Surg 2001; 21: 17-21.
34. Loftus IM, Naylor AR, Goodall S, et al. Increased matrix metalloproteinase-9 activity in unstable carotid plaques. A potential role in acute plaque disruption. Stroke 2000; 31: 40-47.
35. Haffner SM, Greenberg AS, Weston WM, Chen H, Williams K, Freed MI. Effect of rosiglitazone treatment on nontraditional markers of cardiovascular disease in patients with type 2 diabetes mellitus. Circulation 2002; 106: 679-84.
36. Marx N, Froehlich J, Siam L et al. Antidiabetic PPARγ-activator rosiglitazone reduces MMP-9 serum levels in type 2 diabetic patients with coronary artery disease. Arterioscler Thromb Vasc Biol 2003; 23: 283-88.
37. Portik-Dobos V, Anstadt MP, Hutchinson J, Bannan M, Ergul A. Evidence for a matrix metalloproteinase induction/activation system in arterial vasculature and decreased synthesis and activity in diabetes. Diabetes 2002; 51: 3063-68.