Gelatinase in the cerebrospinal fluid of patients with multiple sclerosis and other inflammatory neurological disorders

Gijbels, Koenraad; Masure, Stefan; Carton, Herwig; Opdenakker, Ghislain

doi:10.1016/0165-5728(92)90192-n

Cited by 278 publications

(164 citation statements)

References 24 publications

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“…Multiple sclerosis is a demyelinating disorder that is associated with an increase in the levels of MMP-9 in the CSF (Gijbels et al, 1992). Treatment with highdose methylprednisolone for 3 days dramatically reduced the levels of MMP-9 in patients with evidence of BBB damage on Gadolinium-enhanced magnetic resonance imaging (MRI) (Rosenberg et al, 1996a).…”

Section: Mmps In Neuroinflammation In the Absence Of Hypoxiamentioning

confidence: 99%

Matrix metalloproteinases in neuroinflammation

Rosenberg

2002

Glia

781

667

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Matrix metalloproteinases (MMPs) are a gene family of neutral proteases that are important in normal development, wound healing, and a wide variety of pathological processes, including the spread of metastatic cancer cells, arthritic destruction of joints, atherosclerosis, and neuroinflammation. In the central nervous system (CNS), MMPs have been shown to degrade components of the basal lamina, leading to disruption of the blood-brain barrier (BBB), and to contribute to the neuroinflammatory response in many neurological diseases. Brain cells express both constitutive and inducible MMPs in response to cellular stress. MMPs are tightly regulated to avoid unwanted proteolysis. Secreted as inactive enzymes, the MMPs require activation by other proteases and free radicals. The MMPs are part of a larger class of metalloproteinases (MPs), which includes the recently discovered ADAMs (a disintegrin and metalloproteinase domain) and ADAMTS (a disintegrin and metalloproteinase thrombospondin) families. MPs have complex roles at the cell surface and within the extracellular matrix. At the cell surface, they act as sheddases, releasing growth factors, death receptors, and death-inducing ligands, making them important in cell survival and death. Tissue inhibitors of metalloproteinases (TIMPs) are endogenous inhibitors that regulate the activity of the MMPs. Synthetic inhibitors have been developed for the treatment of arthritis and cancer. These hydroxymate-based compounds have been shown to reduce injury in experimental allergic encephalomyelitis (EAE), experimental allergic neuritis (EAN), cerebral ischemia, intracerebral hemorrhage, and viral and bacterial infections. MPs have both beneficial and detrimental roles; understanding their expression in various CNS insults will allow for the use of MMP inhibitors in the treatment of neurological disorders. GLIA 39: 279 -291, 2002.

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Section: Mmps In Neuroinflammation In the Absence Of Hypoxiamentioning

confidence: 99%

Matrix metalloproteinases in neuroinflammation

Rosenberg

2002

Glia

781

667

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“…MMP levels are increased in MS (Anthony et al, 1997;Cossins et al, 1997;Gijbels et al, 1992;Maeda and Sobel, 1996;Ozenci et al, 2000;Ozenci et al, 1999;Rosenberg et al, 1996;Sellebjerg et al, 2000;Trojano et al, 1999;Waubant et al, 1999) and in animal models of MS including experimental allergic encephalomyelitis (EAE) Gijbels et al, 1993;Graesser et al, 1998;Graesser et al, 2000;Jovanova-Nesic and Shoenfeld, 2006;Kieseier et al, 1998;Teesalu et al, 2001), and are very closely linked to pathogenesis and disease progression. Elevated serum MMP activity is detectable extremely early in the disease course, being present even in prodromal phases prior to development of clinically diagnosed MS (Correale and Bassani Molinas Mde, 2003).…”

Section: Introductionmentioning

confidence: 99%

Cleavage of myelin associated glycoprotein by matrix metalloproteinases

Milward

Kim

Szklarczyk

et al. 2008

Journal of Neuroimmunology

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Derivative myelin associated glycoprotein (dMAG) results from proteolysis of transmembrane MAG and can inhibit axonal growth. We have tested the ability of certain matrix metalloproteinases Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. NIH Public Access

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“…MMP-9 plays a role in tissue remodeling, tissue repair, and wound healing, and is a marker of inflammatory diseases such as rheumatoid arthritis (4) and multiple sclerosis (5). PMNs produce MMP-9 during the late stages of maturation in the bone marrow where it is stored in its latent form proMMP-9 within the gelatinase granules.…”

Section: P Olymorphonuclear Neutrophils (Pmns)mentioning

confidence: 99%

Intracellular and Cell Surface Localization of a Complex between αMβ2 Integrin and Promatrix Metalloproteinase-9 Progelatinase in Neutrophils

Stefanidakis

Ruohtula

Borregaard

et al. 2004

The Journal of Immunology

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We have recently demonstrated that promatrix metalloproteinases (proMMPs), particularly proMMP-9, are potent ligands of the leukocyte β2 integrins. We studied here the complex formation between proMMP-9 and αMβ2, the major MMP and integrin of neutrophils. On resting neutrophils, the proMMP-9/αMβ2 complex was primarily detected in intracellular granules, but after cellular activation it became localized to the cell surface, as demonstrated by immunoprecipitation and double immunofluorescence. Further indication of the complex formation was that neutrophils and αMβ2-transfected L cells, but not the wild-type L cells or leukocyte adhesion deficiency cells, bound to immobilized proMMP-9 or its recombinant catalytic domain in a β2 integrin-dependent manner. Peptides that bound to the αM integrin-I domain and inhibited its complex formation with proMMP-9 prevented neutrophil migration in a transendothelial assay in vitro and in a thioglycolate-elicited peritonitis in vivo. These results suggest that the translocating proMMP-9/αMβ2 complex may be part of the cell surface machinery guiding neutrophil migration.

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Gelatinase in the cerebrospinal fluid of patients with multiple sclerosis and other inflammatory neurological disorders

Cited by 278 publications

References 24 publications

Matrix metalloproteinases in neuroinflammation

Matrix metalloproteinases in neuroinflammation

Cleavage of myelin associated glycoprotein by matrix metalloproteinases

Intracellular and Cell Surface Localization of a Complex between αMβ2 Integrin and Promatrix Metalloproteinase-9 Progelatinase in Neutrophils

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