Metalloproteinases in biology and pathology of the nervous system
By V. W. Yong, C. Power, P. Forsyth, D. Edwards. Nature Reviews Neuroscience, 2001
1,081 citations recorded by the source corpus.
Matrix metalloproteinases (MMPs) have been implicated in several diseases of the nervous system. Here we review the evidence that supports this idea and discuss the possible mechanisms of MMP action. We then consider some of the beneficial functions of MMPs during neural development and speculate on their roles in repair after brain injury. We also introduce a family of proteins known as ADAMs (a disintegrin and metalloproteinase), as some of the properties previously ascribed to MMPs are possibly the result of ADAM activity.
Subfields: Cancer Research, Molecular Biology, Oncology
View Paper: https://www.semanticscholar.org/paper/2a273c8c6f294a1497fb672ac7d9770735d867c9
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In Cancer Research
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In Molecular Biology
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Citations in the corpus
- Matrix metalloproteinases (MMPs) in health and disease: an overview. (2006, background): “MMP-8 and MMP9, in particular, appear to mediate central nervous tissue injury in bacterial infections including meningitis (47), multiple sclerosis (48), Alzheimer’s disease (46), inflammatory myopathies (49) and tumors of the CNS such as glioma (50).”
- Nitric oxide in the central nervous system: neuroprotection versus neurotoxicity (2007, background): “Matrix metalloproteinases are involved in the pathogenesis of acute and chronic neurodegenerative disorders, such as stroke, Alzheimer's disease, HIV-associated dementia and multiple sclerosi”
- Biochemistry and Molecular Biology of Gelatinase B or Matrix Metalloproteinase-9 (MMP-9) (2002, background): “Gelatinase B belongs to the family of matrix metalloproteinases (Nagase and Woessner, 1999; Yong et al., 2001; Egeblad and Werb, 2002).”
- Matrix metalloproteinases in the brain and blood–brain barrier: Versatile breakers and makers (2016, background): “expressed in the brain in both their pro- and activated forms.(24,25) MMPs are generated and then secreted into the extracellular space in an inactive, latent pro-form (zymogen), which is activated through proteolysis of the N-terminal pro-domain (Figure 1).”
- Human and mouse proteases: a comparative genomic approach (2003, background): “These latter alterations are frequent in certain protease families such as MMPs, and have been linked to the development and progression of cancer, arthritis and inflammatory disease”
- Inflammation and its role in neuroprotection, axonal regeneration and functional recovery after spinal cord injury. (2008, background): “, MMPs) produced by neutrophils, macrophages and endothelia also have been implicated in secondary injury (44;119;178;186).”
- Tight junctions and the modulation of barrier function in disease (2008, background): “Tissue inhibitors of metalloproteinases (TIMPs) form complexes with either activated MMPs or with their pro-forms after their secretion, thus regulating MMP activity under physiological conditions (Brew et al. 2000; Yong et al. 2001).”
- Inflammation after Intracerebral Hemorrhage (2007, background): “Abundant evidence indicates that extracellular proteases are involved in and mediate neuronal cell death in many neurologic diseases (Gingrich and Traynelis, 2000; Nakanishi, 2003; Yong, 2005; Yong et al, 2001).”
- Matrix metalloproteinases in neuroinflammation (2002, background): “The ADAMs gene family of proteases have both MP and disintegrin domains (Schlondorff and Blobel, 1999).”