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Matrix metalloproteinases and epileptogenesis

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ABSTRACT

Matrix metalloproteinases are vital drivers of synaptic remodeling in health and disease. It is suggested that at early stages of epileptogenesis, inhibition of matrix metalloproteinases may help ameliorate cell death, aberrant network rewiring, and neuroinflammation and prevent development of epilepsy.

No MeSH data available.


Structure of matrix metalloproteinases (adopted and modified from Huntley [6]).
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Fig1: Structure of matrix metalloproteinases (adopted and modified from Huntley [6]).

Mentions: MMPs are multidomain proteins named according to a sequential numbering scheme (FigureĀ 1). In humans, 24 MMP genes encode 23 distinct MMPs (two identical genes located on chromosome 1 encode MMP23). MMPs all possess an N-terminal signal peptide, an autoinhibitory pro-domain, and a catalytic domain. Most MMPs also possess a C-terminal haemopexin domain which contributes to the target specificity of MMP proteolysis by coordinating interactions with substrates. The haemopexin domain mediates protein-protein interactions and can anchor MMPs to other cell-surface proteins. MMPs can also act as ligands through their haemopexin domain by binding to receptors (see review by Huntley [6] and Rosenberg [4]).Figure 1


Matrix metalloproteinases and epileptogenesis
Structure of matrix metalloproteinases (adopted and modified from Huntley [6]).
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4530574&req=5

Fig1: Structure of matrix metalloproteinases (adopted and modified from Huntley [6]).
Mentions: MMPs are multidomain proteins named according to a sequential numbering scheme (FigureĀ 1). In humans, 24 MMP genes encode 23 distinct MMPs (two identical genes located on chromosome 1 encode MMP23). MMPs all possess an N-terminal signal peptide, an autoinhibitory pro-domain, and a catalytic domain. Most MMPs also possess a C-terminal haemopexin domain which contributes to the target specificity of MMP proteolysis by coordinating interactions with substrates. The haemopexin domain mediates protein-protein interactions and can anchor MMPs to other cell-surface proteins. MMPs can also act as ligands through their haemopexin domain by binding to receptors (see review by Huntley [6] and Rosenberg [4]).Figure 1

View Article: PubMed Central

ABSTRACT

Matrix metalloproteinases are vital drivers of synaptic remodeling in health and disease. It is suggested that at early stages of epileptogenesis, inhibition of matrix metalloproteinases may help ameliorate cell death, aberrant network rewiring, and neuroinflammation and prevent development of epilepsy.

No MeSH data available.