Interleukin-1 is a key regulator of matrix metalloproteinase-9 expression in human neurons in culture and following mouse brain trauma in vivo

Vecil, Giacomo G.; Larsen, Peter H.; Corley, Shannon M.; Herx, Leonie; Besson, Arnaud; Goodyer, Cynthia G.; Yong, V. Wee

doi:10.1002/1097-4547(20000715)61:2<212::aid-jnr12>3.0.co;2-9

Cited by 175 publications

(100 citation statements)

References 57 publications

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“…It was shown in both most popular models of that disorder (controlled cortical impact and corticectomy) that already at 3 h post-injury, MMP-9 activity was increased and remained elevated even until 7 days. 11,31,32 Importantly, MMP-9 KO mice were found to be more resistant to traumatic brain injury, since they had smaller post-traumatic lesions after the head trauma, and recovered motor skills faster. 32 Another disorder of CNS in which MMP-9 plays a vital role is ischemia.…”

Section: Mmp-9 In Neuronal Deathmentioning

confidence: 99%

“…2 In the brain, the list includes laminin, b-dystroglycan, zonae occludens-1 and myelin basic protein as well as NG2 proteoglycan in the spinal cord. [6][7][8][9] MMP-9 is expressed ubiquitously, albeit at low levels, in various mammalian organs and tissues, including the adult brain 10,11 where it is produced mainly by neurons, and, to some extent, by glia. [12][13][14][15] Recently, we studied a subcellular localization of MMP-9 in the rat hippocampus, using highresolution morphological as well as biochemical approaches.…”

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confidence: 99%

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Matrix metalloproteinase-9 in glutamate-dependent adult brain function and dysfunction

Michaluk

Kaczmarek²

2007

Cell Death Differ

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Matrix metalloproteinase-9 (MMP-9) is extracellularly operating protease that is expressed by the adult brain neurons and released in response to enhanced neuronal activity driven by glutamate. In addition, MMP-9 can also be produced by glial and endothelial cells as well as by infiltrating leukocytes. Extracellularly, the protein is activated in a cascade of steps that involves also other proteases and then is inhibited by tissue inhibitors of matrix metalloproteinases (TIMPs). Under physiological conditions, MMP-9 is involved in neuronal plasticity, including long-term potentiation as well as learning and memory. This function of MMP-9 may relate to its synaptic action that is a consequence of post-synaptic/dendritic locus of mRNA and protein storage and release. Under pathological conditions that involve excessive function of glutamate, such as excitotoxicity, stroke and traumatic brain injury, MMP-9 is detrimental to the brain tissue, probably because of its excessive activity. This complex functionality and dysfunctionality of MMP-9 is well documented by studies on its expression patterns as well as with an aid of chemical inhibitors and knockout mice.Matrix metalloproteinase-9 (MMP-9) is a zinc-dependent endopeptidase that together with the most closely related MMP-2, forms a subfamily of gelatinases.1,2 MMPs operate extracellularly (predominantly secreted pericellularly, and some membrane-bound) and are locally inhibited by endogenous tissue inhibitors of metalloproteinases (TIMPs) that bind MMPs non-covalently.

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Section: Mmp-9 In Neuronal Deathmentioning

confidence: 99%

mentioning

confidence: 99%

Matrix metalloproteinase-9 in glutamate-dependent adult brain function and dysfunction

Michaluk

Kaczmarek²

2007

Cell Death Differ

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“…To determine if the Cdk-5-mediated Bcl-2 pathway also plays role in the survival of primary human neurons, we generated enriched (over 90% purity) cultures of human neurons (Figure 9a), based on the protocols as we previously reported. 33 The human neurons were first treated with various doses of camptothecin and the cell viability assay showed that camptothecin killed primary human neurons in a dose dependent manner with toxicity manifesting at camptothecin concentrations of more than 100 ng/ml (Figure 9b). Next, we examined the human neurons to determine if Cdk5-mediated ERK and Bcl-2 signal pathway contributes to BDNF-induced neuroprotection of the primary human neurons.…”

Section: Cdk5 Contributes To Bdnf Neuroprotection Of Primary Human Nementioning

confidence: 99%

“…33 In brief, 5-15 g of brain were diced into fragments of 1 mm and incubated for 15 min at 371C in 40 ml PBS containing 0.25% trypsin and 200 mg/ml DNAse I. The suspension was washed through a filter of 130 mM pore size and the filtrate was centrifuged at 1200 rpm for 10 min.…”

Section: Human Neuron Culturementioning

confidence: 99%

Cyclin-dependent kinase-5 prevents neuronal apoptosis through ERK-mediated upregulation of Bcl-2

Wang

Song

et al. 2005

Cell Death Differ

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Cyclin-dependent kinase-5 (Cdk5) is required for neuronal survival, but its targets in the apoptotic pathways remain unknown. Here, we show that Cdk5 kinase activity prevents neuronal apoptosis through the upregulation of Bcl-2. Treatment of SH-SY5Y cells with retinoid acid (RA) and brain-derived neurotrophic factor (BDNF) generates differentiated neuron-like cells. DNA damage triggers apoptosis in the undifferentiated cells through mitochondrial pathway; however, RA/BDNF treatment results in Bcl-2 upregulation and inhibition of the mitochondrial pathway in the differentiated cells. RA/BDNF treatment activates Cdk5-mediated PI3K/Akt and ERK pathways. Inhibition of Cdk5 inhibits PI3K/ Akt and ERK phosphorylation and Bcl-2 expression, and thus sensitizes the differentiated cells to DNA-damage. Inhibition of ERK, but not PI3K/Akt, abrogates Cdk5-medidated Bcl-2 upregulation and the protection of the differentiated cells. This study suggests that ERK-mediated Bcl-2 upregulation contributes to BDNF-induced Cdk5-mediated neuronal survival.

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“…RNase protection and polymerase chain reaction assays have shown constitutive expression of MMP-2, -3, -7, -8, -9, -11, -13, -14, -15, -16, -17, -19, -20, -21 and -23 in rodents [15,54,58]. In normal rat brain, MMP-2 expression has been described in astrocyte endfeet [45].…”

Section: Introductionmentioning

confidence: 99%

Multiple expression of matrix metalloproteinases in murine neurocysticercosis: Implications for leukocyte migration through multiple central nervous system barriers

Alvarez

Teale

2008

Brain Research

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During the course of murine neurocysticercosis (NCC), disruption of the unique protective barriers in the central nervous system (CNS) is evidenced by extravasation of leukocytes. This process varies according to the anatomical sites and diverse vascular beds analyzed. To examine mechanisms involved in the observed differences, the expression and activity of eight matrix metalloproteinases (MMPs) were analyzed in a murine model of NCC. The mRNA expression of the MMPs studied was upregulated as a result of infection, and active MMPs were mainly detected in leukocytes migrating into the brain. Polarized expression and gelatinolytic activity of several MMPs were identified in immune cells extravasating pial vessels as early as 1 day post infection. In contrast, leukocytes expressing active MMPs and extravasating parenchymal vessels were not observed until 5 weeks post infection. In ventricular areas, most of the MMP activity was detected in leukocytes traversing the ependyma from leptomeningeal infiltrates. In addition, immune cells continued to express active MMPs after exiting vessels suggesting that enzymatic activity of MMPs is not just required for diapedesis. These results correlate with our previous studies showing differential kinetics in the disruption of the CNS barriers upon infection and help document the important role of MMPs during leukocyte infiltration and inflammation.

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Interleukin-1 is a key regulator of matrix metalloproteinase-9 expression in human neurons in culture and following mouse brain trauma in vivo

Cited by 175 publications

References 57 publications

Matrix metalloproteinase-9 in glutamate-dependent adult brain function and dysfunction

Matrix metalloproteinase-9 in glutamate-dependent adult brain function and dysfunction

Cyclin-dependent kinase-5 prevents neuronal apoptosis through ERK-mediated upregulation of Bcl-2

Multiple expression of matrix metalloproteinases in murine neurocysticercosis: Implications for leukocyte migration through multiple central nervous system barriers

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