Cited by 57

The DOI matches its Crossref record.

The matrix metalloproteinases inhibitor Ro 26-2853 extends survival in transgenic ALS mice

Lorenzl, Stefan, Narr, Sabine, Angele, Barabara, Krell, Hans Willi, Gregorio, Jason, Kiaei, Mahmoud, Pfister, Hans-Walter, Beal, M. Flint·2006·Experimental Neurology

Abstract

In amyotrophic lateral sclerosis (ALS), there is increased expression of matrix metalloproteinases (MMPs) and degradation of the extracellular matrix in postmortem spinal cord tissue. We used zymography and in situ zymography to analyze the expression of MMP-2 and MMP-9 in spinal cord tissue from the G93A transgenic mouse model of ALS. Expression of MMP-9 was increased in the spinal cord of G93A mice. For functional analysis of the role of MMPs, we investigated the effects of oral administration of the MMP inhibitor Ro 28-2653 (100 mg/kg), starting at the age of 30 days (n = 19) and on disease onset (starting at the age of 90 days (n = 10)). Treatment with the MMP inhibitor Ro 28-2653 starting at 30 days of age improved motor performance and significantly (P < 0.05) prolonged the survival time of the animals (136 +/- 12 versus 123 +/- 12 days, mean +/- SD), however, administration at disease onset did not significantly improve survival time. Our experiments show that MMPs are expressed in an animal model of ALS and may play a role in the complex pathophysiologic changes. Early pharmacologic inhibition with a synthetic MMP inhibitor extends survival of the animals which suggest a role of MMPs in the early phase of the disease.

Overview

Integrity signals

Registry

Crossref · 10.1016/j.expneurol.2006.01.026

Cites

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Ro 28-2653 is an orally available, brain-penetrant inhibitor with high specificity for MT1-MMP, MMP2, and MMP9.

    “Ro 28-2653 is an orally available, brain-penetrant inhibitor with high specificity for MT1-MMP, MMP2, and MMP9.”
  • As a hydroxamic acid-based MMP inhibitor, Ro 28-2653 may also display lower binding affinity for other MMPs, as well as for ADAM and ADAMTS metalloproteinases.

    “As a hydroxamic acid-based MMP inhibitor, it may also display lower binding affinity for other MMPs, as well as for ADAM and A Disintegrin and Metalloproteinase with Thrombospondin Motifs (ADAMTS) metalloproteinases31–35.”

Citations

Cites

No references could be resolved yet.

Research works printed but not linked: 33

  1. Asahi, 2000, Role for matrix metalloproteinase 9 after focal cerebral ischemia: effects of gene knockout and enzyme inhibition with BB-94, J. Cereb. Blood Flow Metab., 20, 1681, 10.1097/00004647-200012000-00007 · DOI
  2. Asahina, 2001, Expression of matrix metalloproteinase-9 and urinary-type plasminogen activator in Alzheimer's disease brain, Clin. Neuropathol., 20, 60
  3. Bendotti, 2004, Activated p38MAPK is a novel component of the intracellular inclusions found in human amyotrophic lateral sclerosis and mutant SOD1 transgenic mice, J. Neuropathol. Exp. Neurol., 63, 113, 10.1093/jnen/63.2.113 · DOI
  4. Beuche, 2000, Matrix metalloproteinase-9 is elevated in serum of patients with amyotrophic lateral sclerosis, NeuroReport, 11, 3419, 10.1097/00001756-200011090-00003 · DOI
  5. Clements, 1997, Matrix metalloproteinase expression during experimental autoimmune encephalomyelitis and effects of a combined matrix metalloproteinase and tumour necrosis factor-alpha inhibitor, J. Neuroimmunol., 74, 85, 10.1016/S0165-5728(96)00210-X · DOI
  6. Demestre, 2004, The pro and the active form of matrix metalloproteinase-9 is increased in serum of patients with amyotrophic lateral sclerosis, J. Neuroimmunol., 159, 146, 10.1016/j.jneuroim.2004.09.015 · DOI
  7. Demeulemeester, 2005, Effect of matrix metalloproteinase inhibition on adipose tissue development, Biochem. Biophys. Res. Commun., 329, 105, 10.1016/j.bbrc.2005.01.103 · DOI
  8. Dewil, 2005, Role of matrix metalloproteinase-9 in a mouse model for amyotrophic lateral sclerosis, NeuroReport, 16, 321, 10.1097/00001756-200503150-00003 · DOI
  9. Gottschall, 1996, Regulation of matrix metalloproteinase expression in astrocytes, microglia and neurons, Neuroimmun. Mod., 3, 69, 10.1159/000097229 · DOI
  10. Gu, 2005, A highly specific inhibitor of matrix metalloproteinase-9 rescues laminin from proteolysis and neurons from apoptosis in transient focal cerebral ischemia, J. Neurosci., 25, 6401, 10.1523/JNEUROSCI.1563-05.2005 · DOI
  11. Holmes, 1909, The pathology of amyotrophic lateral sclerosis, Rev. Neurol. Psychiatry, 7, 693
  12. Kiaei, 2002, Life extension in a transgenic animal model of amyotrophic lateral sclerosis by crossing to matrix metalloproteinase, Soc. Neurosci., 789.6
  13. Lim, 1996, Matrix metalloproteinases in the neocortex and spinal cord of amyotrophic lateral sclerosis patients, J. Neurochem., 67, 251, 10.1046/j.1471-4159.1996.67010251.x · DOI
  14. Liu, 2002, Increased mitochondrial antioxidative activity or decreased oxygen free radical propagation prevent mutant SOD1-mediated motor neuron cell death and increase amyotrophic lateral sclerosis-like transgenic mouse survival, J. Neurochem., 80, 488, 10.1046/j.0022-3042.2001.00720.x · DOI
  15. Lorenzl, 2002, 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., 178, 13, 10.1006/exnr.2002.8019 · DOI
  16. Lorenzl, 2003, Increased plasma levels of matrix metalloproteinase-9 in patients with Alzheimer's disease, Neurochem. Int., 43, 191, 10.1016/S0197-0186(03)00004-4 · DOI · Paper page
  17. Lorenzl, 2004, Matrix metalloproteinase-9 is elevated in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced parkinsonism in mice, Neuromol. Med., 5, 119, 10.1385/NMM:5:2:119 · DOI
  18. Mattiazzi, 2002, Mutated human SOD1 causes dysfunction of oxidative phosphorylation in mitochondria of transgenic mice, J. Biol. Chem., 277, 29626, 10.1074/jbc.M203065200 · DOI
  19. Maquoi, 2004, Anti-invasive, antitumoral, and antiangiogenic efficacy of a pyrimidine-2,4,6-trione derivative, an orally active and selective matrix metalloproteinases inhibitor, Clin. Cancer Res., 10, 4038, 10.1158/1078-0432.CCR-04-0125 · DOI
  20. Menzies, 2002, Mitochondrial involvement in amyotrophic lateral sclerosis, Neurochem. Int., 40, 543, 10.1016/S0197-0186(01)00125-5 · DOI
  21. Miyazaki, 1993, A metallopreoteinase inhibitor domain in Alzheimer amyloid protein precursor, Nature, 362, 839, 10.1038/362839a0 · DOI
  22. Nelson, 2004, Mitochondrial redox control of matrix metalloproteinases, Free Radical Biol. Med., 37, 768, 10.1016/j.freeradbiomed.2004.06.008 · DOI
  23. Oh, 1999, Matrix metalloproteinase-9/Gelatinase B is required for process outgrowth by oligodendrocytes, J. Neurosci., 19, 8464, 10.1523/JNEUROSCI.19-19-08464.1999 · DOI
  24. Ono, 1998, Collagen abnormalities in the spinal cord from patients with amyotrophic lateral sclerosis, J. Neurol. Sci., 160, 140, 10.1016/S0022-510X(98)00223-8 · DOI
  25. Pasinelli, 2004, Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria, Neuron, 43, 19, 10.1016/j.neuron.2004.06.021 · DOI
  26. Ranganathan, 2001, Manganese superoxide dismutase signals matrix metalloproteinase expression via H2O2-dependent ERK1/2 activation, J. Biol. Chem., 276, 14264, 10.1074/jbc.M100199200 · DOI
  27. Schoser, 1999, Matrix metalloproteinases MMP-2, MMP-7 and MMP-9 in denervated human muscle, NeuroReport, 10, 2795, 10.1097/00001756-199909090-00018 · DOI
  28. Stetler-Stevenson, 1996, Dynamics of matrix turnover during pathological remodelling of the extracellular matrix, Am. J. Pathol., 148, 1345
  29. Tortarolo, 2003, Persistent activation of p38 mitogen-activated protein kinase in a mouse model of familial amyotrophic lateral sclerosis correlates with disease progression, Mol. Cell. Neurosci., 23, 180, 10.1016/S1044-7431(03)00022-8 · DOI
  30. Vijayergiya, 2005, Mutant superoxide dismutase 1 forms aggregates in the brain mitochondrial matrix of amyotrophic lateral sclerosis mice, J. Neurosci., 25, 2463, 10.1523/JNEUROSCI.4385-04.2005 · DOI
  31. Yong, 2001, Metalloproteinases in biology and pathology of the nervous system, Nat. Rev., Neurosci., 2, 1681, 10.1038/35081571 · DOI
  32. Zhang, 1997, Zymographic measurement of gelatinase activity in brain tissue after detergent extraction and affinity-support purification, J. Neurosci. Methods, 76, 15, 10.1016/S0165-0270(97)00065-4 · DOI
  33. Zhang, 2002, Activation of matrix metalloproteinase-2 by overexpression of manganese superoxide dismutase in human breast cancer MCF-7 cells involves reactive oxygen species, J. Biol. Chem., 277, 20919, 10.1074/jbc.M109801200 · DOI

Cited by

Sorted by citations

Metadata

Authors
Lorenzl, S., Narr, S., Angele, B., Krell, H. W., Gregorio, J., Kiaei, M., Pfister, H.-W., & Beal, M. F.
Venue
Experimental Neurology
Publisher
Elsevier BV
Published
2006-07
Volume
200
Issue
1
Pages
166-171
ISSN
0014-4886
Cited by
57
References
0
Language
en

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review