Matrix metalloproteinase-9 (MMP-9) and tissue inhibitor of matrix metalloproteinase (TIMP-1) in patients with relapsing–remitting multiple sclerosis treated with interferon beta

  title={Matrix metalloproteinase-9 (MMP-9) and tissue inhibitor of matrix metalloproteinase (TIMP-1) in patients with relapsing–remitting multiple sclerosis treated with interferon beta},
  author={Cavit Boz and Mehmet Ozmenoğlu and Sibel K. Velioğlu and Kağan Kilinç and Asım Orem and Zekeriya Alioǧlu and Vildan Altunayoğlu},
  journal={Clinical Neurology and Neurosurgery},

Increased expression ratio of matrix metalloproteinase-9 (MMP9) and tissue inhibitor of matrix metalloproteinase (TIMP-1) RNA levels in Iranian multiple sclerosis patients.

Although there was no significant decrease in TIMP-1 expression level, the MMP-9/TIMp-1 RNA ratio in RRMS was significantly higher than normal subjects, and further studies are recommended to compare M MP-9-to-TIMP-2RNA ratio in patients before and after taking IFN-beta in order to find out if it can function as a proper marker of the bio efficacy of IFn-beta treatment of MS.

Analysis of MMP2-1306C/T and TIMP2G-418C polymorphisms with relapsing remitting multiple sclerosis

Results indicate that MMP2 might play a role in the pathogenesis of MS even during the inflammation stage.

T-cell production of matrix metalloproteinases and inhibition of parasite clearance by TIMP-1 during chronic Toxoplasma infection in the brain

A role for MMPs and TIMP-1 in the trafficking of lymphocytes into the CNS during chronic infection in the brain is demonstrated.

Anti-inflammatory Property of β-D-Mannuronic Acid (M2000) on Expression and Activity of Matrix Metalloproteinase-2 and -9 through CD147 Molecule in Phorbol Myristate Acetate-differentiated THP-1 Cells.

According to the results, M2000 can reduce inflammation through inhibition of the cellular surface expression of CD147 and decrease the gene expression and gelatinolytic activity of MMP-2 and M MP-9 in PMA-differentiated THP-1 cells.

Long-term expression of tissue-inhibitor of matrix metalloproteinase-1 in the murine central nervous system does not alter the morphological and behavioral phenotype but alleviates the course of experimental allergic encephalomyelitis.

The data demonstrate that long-term CNS expression of TIMP1 with complete suppression of gelatinolytic activity does not interfere with physiological brain function and Timp1 might constitute a promising candidate for long- term therapeutic treatment of inflammatory CNS diseases such as multiple sclerosis.

Elevation of matrix metalloproteinases (MMPs) in multiple sclerosis and impact of immunomodulators

Functional MMP-9 polymorphisms modulate plasma MMP-9 levels in multiple sclerosis patients

Perspectives and new aspects of metalloproteinases' inhibitors in therapy of CNS disorders: from chemistry to medicine.

The role of metalloproteinase inhibition in the context of physiological function of adult brain as well as pathological conditions including neurodegenerative diseases, brain injuries and others is discussed.

Persistent macrophage/microglial activation and myelin disruption after experimental autoimmune encephalomyelitis in tissue inhibitor of metalloproteinase-1-deficient mice.

It is suggested that induction of TIMP-1 by astrocytes during EAE in WT mice represents an inherent cytoprotective response that mitigates CNS myelin injury through the regulation of both immune cell infiltration and microglial activation.



Effect of interferon β-1a on serum matrix metalloproteinase—9 (MMP-9) and tissue inhibitor of matrix metalloproteinase (TIMP-1) in relapsing remitting multiple sclerosis patients

The MMP-9 levels showed no significant changes while TIMP-1 levels gradually and significantly increased during 3rd and 6th months of therapy compared with pretreatment levels, in this present study.

Matrix metalloproteinase-9 (gelatinase B) is selectively elevated in CSF during relapses and stable phases of multiple sclerosis.

The sustained increase of MMP-9 in clinically stable multiple sclerosis supports the concept that multiple sclerosis is associated with ongoing proteolysis that may result in progressive tissue damage and could be a useful approach for the prevention of disease progression in multiple sclerosis.

Interferon-β-1 b decreased matrix metalloproteinase-9 serum levels in primary progressive multiple sclerosis

The suppression of MMP-9 by IFN-β1b indicates that this drug is immunomodulatory active in PPMS patients, and further studies are necessary to test if IFn-β exerts a beneficial effect in PP MS.

Serum gelatinase B/MMP-9 in primary progressive multiple sclerosis patients treated with interferon-beta-1a

The sustained correlation between serum MMP-9 and changes in T2 volumes, and the lack of correlation with clinical or MRI measures of disease progression may suggest that M MP-9 is more directly related to non-specific central nervous system damage than to axonal loss.

IFNβ lowers MMP-9/TIMP-1 ratio, which predicts new enhancing lesions in patients with SPMS

Objective: To 1)determine serum levels of matrix metalloproteinase-2 (MMP-2), MMP-9, tissue inhibitor of metalloproteinase-1 (TIMP-1), and TIMP-2 in patients with secondary progressive (SP) MS;

IFN-β1a May Increase Serum Levels of TIMP-1 in Patients with Relapsing-Remitting Multiple Sclerosis

Preliminary data suggest that IFN-β1a therapy may increase TIMP-1 levels, and within- patient median MMP-9 levels were unchanged on treatment, while within-patient median TIMP -1 levels were higher during months 1-6.

Serum gelatinase B, TIMP-1 and TIMP-2 levels in multiple sclerosis. A longitudinal clinical and MRI study.

It is proposed that an abnormality in the inhibitory response to metalloproteinases may play an aetiological role in the chronicity of multiple sclerosis.

Matrix metalloproteinases and tissue inhibitors of metalloproteinases in cerebrospinal fluid differ in multiple sclerosis and Devic's neuromyelitis optica.

It is concluded that multiple sclerosis patients have higher MMP-9 levels in the CSF than patients with DNO, which supports the different pathological mechanisms of these diseases.