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Metzincin Proteases and Their Inhibitors: Foes or Friends in Nervous System Physiology?

Rivera, Santiago, Khrestchatisky, Michel, Kaczmarek, Leszek, Rosenberg, Gary A., Jaworski, Diane M.·2010·The Journal of Neuroscience
DOI 10.1523/jneurosci.3467-10.2010PMC PMC3072038
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Abstract

Members of the metzincin family of metalloproteinases have long been considered merely degradative enzymes for extracellular matrix molecules. Recently, however, there has been growing appreciation for these proteinases and their endogenous inhibitors, tissue inhibitors of metalloproteinases (TIMPs), as fine modulators of nervous system physiology and pathology. Present all along the phylogenetic tree, in all neural cell types, from the nucleus to the synapse and in the extracellular space, metalloproteinases exhibit a complex spatiotemporal profile of expression in the nervous parenchyma and at the neurovascular interface. The irreversibility of their proteolytic activity on numerous biofactors (e.g., growth factors, cytokines, receptors, DNA repair enzymes, matrix proteins) is ideally suited to sustain structural changes that are involved in physiological or postlesion remodeling of neural networks, learning consolidation or impairment, neurodegenerative and neuroinflammatory processes, or progression of malignant gliomas. The present review provides a state of the art overview of the involvement of the metzincin/TIMP system in these processes and the prospects of new therapeutic strategies based on the control of metalloproteinase activity.

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  • α-secretase cleavage of APP is performed by ADAMs of the metzincin superfamily, constitutively by ADAM10 or in a regulated manner by ADAM17/TACE.

    “This is performed by a disintegrin and metalloproteinases (ADAMs) of the metzincin superfamily of metalloproteinases (Rivera et al., 2010; Paschkowsky et al., 2019), in a constitutive (ADAM10) or regulated manner (ADAM17; also known as TACE for TNF-α converting enzyme) (Lammich et al., 1999; Jorissen et al., 2010; Kuhn et al., 2010).”

    From Emerging Alternative Proteinases in APP Metabolism and Alzheimer’s Disease Pathogenesis: A Focus on MT1-MMP and MT5-MMP (2019) · cites this paper as Rivera et al., 2010

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Metadata

Authors
Rivera, S., Khrestchatisky, M., Kaczmarek, L., Rosenberg, G. A., & Jaworski, D. M.
Venue
The Journal of Neuroscience
Publisher
Society for Neuroscience
Published
2010-11-17
Volume
30
Issue
46
Pages
15337-15357
ISSN
  • 0270-6474
  • 1529-2401
DOI
10.1523/jneurosci.3467-10.2010
PMC
PMC3072038
Cited by
223
References
26
Language
en
Licence
creativecommons.org/licenses/by-nc-sa/4.0/ (vor, 181 d)

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