Cisplatin induces changes in the matrix metalloproteinases and their inhibitors in the developing rat cerebellum

Piccolini, Valeria Maria; Avella, Debora; Bottone, Maria Grazia; Bottiroli, Giovanni; Bernocchi, Graziella

doi:10.1016/j.brainres.2012.09.025

Cited by 9 publications

(7 citation statements)

References 63 publications

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“…TIMP1, the endogenous inhibitor of MMPs, preferentially associates with MMP-9. Since crucial homoeostatic regulation of MMPs is mediated through the expression and actions of TIMPs, an imbalance in this ratio may result in an increase in proteolytic activity leading to neurological dysfunction (Piccolini et al, 2012). In the light of these findings, we ascertained the activities of MMP-9 and TIMP1 in the hippocampus using the immunohistochemistry and PCR assays.…”

Section: Discussionmentioning

confidence: 99%

Paeoniflorin attenuates amyloid-beta peptide-induced neurotoxicity by ameliorating oxidative stress and regulating the NGF-mediated signaling in rats

Lan

Chen

et al. 2013

Brain Research

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Section: Discussionmentioning

confidence: 99%

Paeoniflorin attenuates amyloid-beta peptide-induced neurotoxicity by ameliorating oxidative stress and regulating the NGF-mediated signaling in rats

Lan

Chen

et al. 2013

Brain Research

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“…MMP‐9 protein is also expressed in the internal granular layer, external granular layer, and molecular and Purkinje cell layers from PND11 to PND17 (Piccolini et al . ).…”

Section: Expression In the Brain And Physiological Rolesmentioning

confidence: 97%

“…In the cerebellum, MMP-9 protein can be detected in Purkinje cell dendrites, granule precursor cells, Bergmann glial cell bodies, and processes on PND10 (Vaillant et al 1999). MMP-9 protein is also expressed in the internal granular layer, external granular layer, and molecular and Purkinje cell layers from PND11 to PND17 (Piccolini et al 2012).…”

Section: Synaptic Plasticitymentioning

confidence: 99%

MMP‐9 in translation: from molecule to brain physiology, pathology, and therapy

Vafadari

Salamian

Kaczmarek

2016

Journal of Neurochemistry

301

257

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Matrix metalloproteinase-9 (MMP-9) is a member of the metzincin family of mostly extracellularly operating proteases. Despite the fact that all of these enzymes might be target promiscuous, with largely overlapping catalogs of potential substrates, MMP-9 has recently emerged as a major and apparently unique player in brain physiology and pathology. The specificity of MMP-9 may arise from its very local and time-restricted actions, even when released in the brain from cells of various types, including neurons, glia, and leukocytes. In fact, the quantity of MMP-9 is very low in the naive brain, but it is markedly activated at the levels of enzymatic activity, protein abundance, and gene expression following various physiological stimuli and pathological insults. Neuronal MMP-9 participates in synaptic plasticity by controlling the shape of dendritic spines and function of excitatory synapses, thus playing a pivotal role in learning, memory, and cortical plasticity. When improperly unleashed, MMP-9 contributes to a large variety of brain disorders, including epilepsy, schizophrenia, autism spectrum disorder, brain injury, stroke, neurodegeneration, pain, brain tumors, etc. The foremost mechanism of action of MMP-9 in brain disorders appears to be its involvement in immune/inflammation responses that are related to the enzyme's ability to process and activate various cytokines and chemokines, as well as its contribution to bloodbrain barrier disruption, facilitating the extravasation of leukocytes into brain parenchyma. However, another emerging possibility (i.e., the control of MMP-9 over synaptic plasticity) should not be neglected. The translational potential of MMP-9 has already been recognized in both the diagnosis and treatment domains. The most striking translational aspect may be the discovery of MMP-9 up-regulation in a mouse model of Fragile X syndrome, quickly followed by human studies and promising clinical trials that have sought to inhibit MMP-9. With regard to diagnosis, suggestions have been made to use MMP-9 alone or combined with tissue inhibitor of matrix metalloproteinase-1 or brain-derived neurotrophic factor as disease biomarkers.

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“…MMP-9 protein at P10 is detectable in granule precursor cells, Bergmann glial cell bodies and processes, and in Purkinje cell dendrites, a pattern which is similar to MMP-9 mRNA expression ( Vaillant et al, 1999 ). From P11 to P17, both MMP-9 and MMP-3 protein are expressed in the EGL, the IGL, and intensely in the molecular and Purkinje cell layers ( Piccolini et al, 2012 ) where MMP-9 labels the soma of granule and Purkinje cells ( Vaillant et al, 2003 ). At P12 MMP-9 expression in the EGL is concentrated in the premigratory pool of granule precursor cells and is present in migrating granule precursor cells dispersed in the molecular layer ( Vaillant et al, 2003 ).…”

Section: Brain Development and Critical Period Plasticitymentioning

confidence: 99%

A delicate balance: role of MMP-9 in brain development and pathophysiology of neurodevelopmental disorders

Reinhard

Razak

Ethell

2015

Front. Cell. Neurosci.

179

186

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The extracellular matrix (ECM) is a critical regulator of neural network development and plasticity. As neuronal circuits develop, the ECM stabilizes synaptic contacts, while its cleavage has both permissive and active roles in the regulation of plasticity. Matrix metalloproteinase 9 (MMP-9) is a member of a large family of zinc-dependent endopeptidases that can cleave ECM and several cell surface receptors allowing for synaptic and circuit level reorganization. It is becoming increasingly clear that the regulated activity of MMP-9 is critical for central nervous system (CNS) development. In particular, MMP-9 has a role in the development of sensory circuits during early postnatal periods, called ‘critical periods.’ MMP-9 can regulate sensory-mediated, local circuit reorganization through its ability to control synaptogenesis, axonal pathfinding and myelination. Although activity-dependent activation of MMP-9 at specific synapses plays an important role in multiple plasticity mechanisms throughout the CNS, misregulated activation of the enzyme is implicated in a number of neurodegenerative disorders, including traumatic brain injury, multiple sclerosis, and Alzheimer’s disease. Growing evidence also suggests a role for MMP-9 in the pathophysiology of neurodevelopmental disorders including Fragile X Syndrome. This review outlines the various actions of MMP-9 during postnatal brain development, critical for future studies exploring novel therapeutic strategies for neurodevelopmental disorders.

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Cisplatin induces changes in the matrix metalloproteinases and their inhibitors in the developing rat cerebellum

Cited by 9 publications

References 63 publications

Paeoniflorin attenuates amyloid-beta peptide-induced neurotoxicity by ameliorating oxidative stress and regulating the NGF-mediated signaling in rats

Paeoniflorin attenuates amyloid-beta peptide-induced neurotoxicity by ameliorating oxidative stress and regulating the NGF-mediated signaling in rats

MMP‐9 in translation: from molecule to brain physiology, pathology, and therapy

A delicate balance: role of MMP-9 in brain development and pathophysiology of neurodevelopmental disorders

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