Analysis of the expression of nine secreted matrix metalloproteinases and their endogenous inhibitors in the brain of mice subjected to ischaemic stroke

Thrombosis and Haemostasis

Volumn 112, Issue 2, 2014, Pages 363-378

  Lenglet, Sébastien ^a   Montecucco, Fabrizio ^a,b   Mach, François ^a   Schaller, Karl ^a,c   Gasche, Yvan ^a,c   Copin, Jean Christophe ^a  

^a GENEVA UNIVERSITY HOSPITALS   (Switzerland)

^b UNIVERSITY OF GENOA   (Italy)

^c UNIVERSITY OF GENEVA   (Switzerland)

Author keywords

Animal model; Brain ischaemia; MMP; TIMP; tPA

Indexed keywords

ALTEPLASE; COLLAGENASE 3; GELATINASE A; GELATINASE B; HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE; INTERSTITIAL COLLAGENASE; MACROPHAGE ELASTASE; MATRILYSIN; MATRIX METALLOPROTEINASE; MESSENGER RNA; NEUTROPHIL COLLAGENASE; STROMELYSIN; STROMELYSIN 2; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TISSUE INHIBITOR OF METALLOPROTEINASE 2; FIBRINOLYTIC AGENT; TISSUE INHIBITOR OF METALLOPROTEINASE; TISSUE PLASMINOGEN ACTIVATOR;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; BRAIN BLOOD FLOW; BRAIN ISCHEMIA; CEREBRAL REPERFUSION; CONTROLLED STUDY; DOPPLER FLOWMETRY; ENZYME LINKED IMMUNOSORBENT ASSAY; GENE EXPRESSION; MALE; MIDDLE CEREBRAL ARTERY OCCLUSION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; REAL TIME POLYMERASE CHAIN REACTION; REPERFUSION; 129 MOUSE; ANIMAL; BRAIN; DISEASE MODEL; DRUG EFFECTS; ENZYMOLOGY; FIBRINOLYTIC THERAPY; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; STROKE; TIME; UPREGULATION;

ANIMALS; BRAIN; BRAIN ISCHEMIA; DISEASE MODELS, ANIMAL; FIBRINOLYTIC AGENTS; GENE EXPRESSION REGULATION; GENE EXPRESSION REGULATION, ENZYMOLOGIC; MALE; MATRIX METALLOPROTEINASES, SECRETED; MICE, 129 STRAIN; RNA, MESSENGER; STROKE; THROMBOLYTIC THERAPY; TIME FACTORS; TISSUE INHIBITOR OF METALLOPROTEINASES; TISSUE PLASMINOGEN ACTIVATOR; UP-REGULATION;

EID: 84905173637     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH14-01-0007     Document Type: Article

References (47)

1. Gasche Y, Soccal PM, Kanemitsu M, et al. Matrix metalloproteinases and diseases of the central nervous system with a special emphasis on ischaemic brain. Front Biosci 2006; 11: 1289-1301.
2. Sternlicht MD, Werb Z. How matrix metalloproteinases regulate cell behavior. Annu Rev Cell Dev Biol 2001; 17: 463-516.
3. Rodriguez D, Morrison CJ, Overall CM. Matrix metalloproteinases: what do they not do? New substrates and biological roles identified by murine models and proteomics. Biochim Biophys Acta 2010; 1803: 39-54.
4. Brew K, Nagase H. The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversity. Biochim Biophys Acta 2010; 1803: 55-71.
5. Justicia C, Panes J, Sole S, et al. Neutrophil infiltration increases matrix metalloproteinase-9 in the ischaemic brain after occlusion/reperfusion of the middle cerebral artery in rats. J Cereb Blood Flow Metab 2003; 23: 1430-1440.
6. Planas AM, Sole S, Justicia C. Expression and activation of matrix metalloproteinase-2 and-9 in rat brain after transient focal cerebral ischaemia. Neurobiol Dis 2001; 8: 834-846.
7. Gidday JM, Gasche YG, Copin JC, et al. Leukocyte-derived matrix metalloproteinase-9 mediates blood-brain barrier breakdown and is proinflammatory after transient focal cerebral ischaemia. Am J Physiol Heart Circ Physiol 2005; 289: H558-568.
8. Copin JC, Merlani P, Sugawara T, et al. Delayed matrix metalloproteinase inhibition reduces intracerebral hemorrhage after embolic stroke in rats. Exp Neurol 2008; 213: 196-201.
9. Rosenberg GA, Cunningham LA, Wallace J, et al. Immunohistochemistry of matrix metalloproteinases in reperfusion injury to rat brain: activation of MMP-9 linked to stromelysin-1 and microglia in cell cultures. Brain Res 2001; 893: 104-112.
10. Sole S, Petegnief V, Gorina R, et al. Activation of matrix metalloproteinase-3 and agrin cleavage in cerebral ischaemia/reperfusion. J Neuropathol Exp Neurol 2004; 63: 338-349.
11. Suzuki Y, Nagai N, Umemura K, et al. Stromelysin-1 (MMP-3) is critical for intracranial bleeding after t-PA treatment of stroke in mice. J Thromb Haemost 2007; 5: 1732-1739.
12. Rosenberg GA, Estrada EY, Dencoff JE. Matrix metalloproteinases and TIMPs are associated with blood-brain barrier opening after reperfusion in rat brain. Stroke 1998; 29: 2189-2195.
13. Rosenberg GA, Navratil M, Barone F, et al. Proteolytic cascade enzymes increase in focal cerebral ischaemia in rat. J Cereb Blood Flow Metabol 1996; 16: 360-366.
14. Romanic AM, White RF, Arleth AJ, et al. Matrix metalloproteinase expression increases after cerebral focal ischaemia in rats: inhibition of matrix metalloproteinase-9 reduces infarct size. Stroke 1998; 29: 1020-1030.
15. Lakhan SE, Kirchgessner A, Tepper D, et al. Matrix metalloproteinases and blood-brain barrier disruption in acute ischaemic stroke. Front Neurol 2013; 4: 32.
16. Cuadrado E, Rosell A, Penalba A, et al. Vascular MMP-9/TIMP-2 and neuronal MMP-10 up-regulation in human brain after stroke: a combined laser microdissection and protein array study. J Proteome Res 2009; 8: 3191-3197.
17. Ning M, Sarracino DA, Buonanno FS, et al. Proteomic Protease Substrate Profiling of tPA Treatment in Acute Ischaemic Stroke Patients: A Step Toward Individualizing Thrombolytic Therapy at the Bedside. Transl Stroke Res 2010; 1: 268-275.
18. Lees KR, Bluhmki E, von Kummer R, et al. Time to treatment with intravenous alteplase and outcome in stroke: an updated pooled analysis of ECASS, ATLANTIS, NINDS, and EPITHET trials. Lancet 2010; 375: 1695-1703.
19. Vivien D, Gauberti M, Montagne A, et al. Impact of tissue plasminogen activator on the neurovascular unit: from clinical data to experimental evidence. J Cereb Blood Flow Metab 2011; 31: 2119-2134.
20. Tsuji K, Aoki T, Tejima E, et al. Tissue plasminogen activator promotes matrix metalloproteinase-9 upregulation after focal cerebral ischaemia. Stroke 2005; 36: 1954-1959.
21. Wang X, Tsuji K, Lee SR, et al. Mechanisms of hemorrhagic transformation after tissue plasminogen activator reperfusion therapy for ischaemic stroke. Stroke 2004; 35 (11 Suppl 1): 2726-2730.
22. Jickling GC, Liu D, Stamova B, et al. Hemorrhagic transformation after ischaemic stroke in animals and humans. J Cereb Blood Flow Metab 2014; 34: 185-199.
23. Copin JC, Bengualid DJ, Da Silva RF, et al. Recombinant tissue plasminogen activator induces blood-brain barrier breakdown by a matrix metalloproteinase-9-independent pathway after transient focal cerebral ischaemia in mouse. Eur J Neurosci 2011; 34: 1085-1092.
24. Sumii T, Lo EH. Involvement of matrix metalloproteinase in thrombolysis-associated hemorrhagic transformation after embolic focal ischaemia in rats. Stroke 2002; 33: 831-836.
25. Copin JC, da Silva RF, Fraga-Silva RA, et al. Treatment with Evasin-3 reduces atherosclerotic vulnerability for ischaemic stroke, but not brain injury in mice. J Cereb Blood Flow Metab 2013; 33: 490-498.
26. Gubern C, Hurtado O, Rodriguez R, et al. Validation of housekeeping genes for quantitative real-time PCR in in-vivo and in-vitro models of cerebral ischaemia. BMC Mol Biol 2009; 10: 57.
27. Clark IM, Swingler TE, Sampieri CL, et al. The regulation of matrix metalloproteinases and their inhibitors. Int J Biochem Cell Biol 2008; 40: 1362-1378.
28. Li L, Li H. Role of microRNA-mediated MMP regulation in the treatment and diagnosis of malignant tumors. Cancer Biol Ther 2014; in press.
29. Bartel DP. MicroRNAs: genomics, biogenesis, mechanism, and function. Cell 2004; 116: 281-297.
30. Dalmay T, Edwards DR. MicroRNAs and the hallmarks of cancer. Oncogene 2006; 25: 6170-6175.
31. Vandooren J, Van den Steen PE, Opdenakker G. Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9): the next decade. Crit Rev Biochem Mol Biol 2013; 48: 222-272.
32. Zheng X, Chopp M, Lu Y, et al. MiR-15b and miR-152 reduce glioma cell invasion and angiogenesis via NRP-2 and MMP-3. Cancer Lett 2013; 329: 146-154.
33. Garbacki N, Di Valentin E, Piette J, et al. Matrix metalloproteinase 12 silencing: a therapeutic approach to treat pathological lung tissue remodeling? Pulm Pharmacol Ther 2009; 22: 267-278.
34. Vemuganti R. All's well that transcribes well: Non-coding RNAs and post-stroke brain damage. Neurochem Int 2013; 63: 438-449.
35. Jin R, Yang G, Li G. Inflammatory mechanisms in ischaemic stroke: role of inflammatory cells. J Leukoc Biol 2010; 87: 779-789.
36. Toft-Hansen H, Nuttall RK, Edwards DR, et al. Key metalloproteinases are expressed by specific cell types in experimental autoimmune encephalomyelitis. J Immunol 2004; 173: 5209-5218.
37. Gasche Y, Fujimura M, Morita-Fujimura Y, et al. Early appearance of activated matrix metalloproteinase-9 after focal cerebral ischaemia in mice: a possible role in blood-brain barrier dysfunction. J Cereb Blood Flow Metab 1999; 19: 1020-1028.
38. Nagel S, Sandy JD, Meyding-Lamade U, et al. Focal cerebral ischaemia induces changes in both MMP-13 and aggrecan around individual neurons. Brain Res 2005; 1056: 43-50.
39. Ramos-Fernandez M, Bellolio MF, Stead LG. Matrix metalloproteinase-9 as a marker for acute ischaemic stroke: a systematic review. J Stroke Cerebrovasc Dis 2011; 20: 47-54.
40. Cuadrado E, Rosell A, Borrell-Pages M, et al. Matrix metalloproteinase-13 is activated and is found in the nucleus of neural cells after cerebral ischaemia. J Cereb Blood Flow Metab 2009; 29: 398-410.
41. Rosell A, Alvarez-Sabin J, Arenillas JF, et al. A matrix metalloproteinase protein array reveals a strong relation between MMP-9 and MMP-13 with diffusionweighted image lesion increase in human stroke. Stroke 2005; 36: 1415-1420.
42. Kouwenhoven M, Carlstrom C, Ozenci V, et al. Matrix metalloproteinase and cytokine profiles in monocytes over the course of stroke. J Clin Immunol 2001; 21: 365-375.
43. Svedin P, Hagberg H, Mallard C. Expression of MMP-12 after neonatal hypoxicischaemic brain injury in mice. Dev Neurosci 2009; 31: 427-436.
44. Murphy G, Willenbrock F. Tissue inhibitors of matrix metalloendopeptidases. Methods Enzymol 1995; 248: 496-510.
45. Khokha R, Murthy A, Weiss A. Metalloproteinases and their natural inhibitors in inflammation and immunity. Nat Rev Immunol 2013; 13: 649-665.
46. Verstappen J, Von den Hoff JW. Tissue inhibitors of metalloproteinases (TIMPs): their biological functions and involvement in oral disease. J Dent Res 2006; 85: 1074-1084.
47. Fujimoto M, Takagi Y, Aoki T, et al. Tissue inhibitor of metalloproteinases protect blood-brain barrier disruption in focal cerebral ischaemia. J Cereb Blood Flow Metab 2008; 28: 1674-1685.