Expression and Activation of Matrix Metalloproteinase-2 and -9 in Rat Brain after Transient Focal Cerebral Ischemia

Planas, Anna M.; Solé, Sònia; Justicia, Carles

doi:10.1006/nbdi.2001.0435

Cited by 218 publications

(196 citation statements)

References 57 publications

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“…MMP-2 mRNA, protein, and enzymatic activity have been detected in various brain structures and reported to be preferably astroglial in origin [7,20,[37][38][39][40][41]. In addition, Planas et al [42] found MMP-2 also in some cortical neurons, and neuronal MMP-2 has also been described in the cerebellum, including the Purkinje neurons [17,[38][39][40]. In vitro studies have shown that MMP-2 activity is produced by astrocytes and microglia [43], oligodendrocytes [44,45] and even neurons [46].…”

Section: Mmps In the Brainmentioning

confidence: 99%

“…It is thus interesting that MMP-2 is expressed at a much higher level during postnatal cortical development than in the adult neocortex (Dzwonek et al, unpublished). Inducible expression of MMP-2 in glia has also been noted following brain ischemia [20,42], kainate (KA) treatment as well as traumatic and viral brain injury [32,37,40,[47][48][49]. Interestingly, Asahi et al [50] showed that MMP-2 gene knockout in mice has no effect on brain injury after permanent and transient focal ischemia.…”

Section: Mmps In the Brainmentioning

confidence: 99%

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Matrix metalloproteinases and their endogenous inhibitors in neuronal physiology of the adult brain

DZWONEK

2004

FEBS Letters

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More than 20 matrix metalloproteinases (MMPs) and four of their endogenous tissue inhibitors (TIMPs) act together to control tightly temporally restricted, focal proteolysis of extracellular matrix. In the neurons of the adult brain several components of the TIMP/MMP system are expressed and are responsive to changes in neuronal activity. Furthermore, functional studies, especially involving blocking of MMP activities, along with the identification of MMP substrates in the brain strongly suggest that this enzymatic system plays an important physiological role in adult brain neurons, possibly being pivotal for neuronal plasticity.

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Section: Mmps In the Brainmentioning

confidence: 99%

Section: Mmps In the Brainmentioning

confidence: 99%

Matrix metalloproteinases and their endogenous inhibitors in neuronal physiology of the adult brain

DZWONEK

2004

FEBS Letters

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“…These findings support the work by others who have demonstrated increases in MMP-9 activity SCI, 8 traumatic brain injury, 43 and ischemic brain injury. 32 This increased MMP-9 activity may reflect upregulation within endogenous cells, such as glia and macrophages, 28 and/or increased numbers of infiltrating leukocytes. Notably, neutrophils express MMP-9, 41 and their numbers increase in the traumatized cord with increasing injury severity.…”

Section: Relation Of Mmp-9 Activity Upregulation To Injury Severitymentioning

confidence: 99%

Differential temporal expression of matrix metalloproteinases after spinal cord injury: relationship to revascularization and wound healing

Goussev¹,

Hsu²,

Lin³

et al. 2003

Journal of Neurosurgery: Spine

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Object. Matrix metalloproteinases (MMPs), particularly MMP-9/gelatinase B, promote early inflammation and barrier disruption after spinal cord injury (SCI). Early blockade of MMPs after injury provides neuroprotection and improves motor outcome. There is recent evidence, however, that MMP-9 and MMP-2/gelatinase A participate in later wound healing in the injured cord. The authors therefore examined the activity of these gelatinases during revascularization and glial scar formation in the contused murine spinal cord. Methods. Gelatinase activity was evaluated using gelatin zymography 24 hours after a mild, moderate, or severe contusion injury. The active form of MMP-2 was not detected, whereas MMP-9 activity was evident in all SCI groups and rose with increasing injury severity. The temporal expression of gelatinases was then examined using gelatin zymography after a moderate SCI. The active form of MMP-9 was most prominent at 1 day, extended through the early period of revascularization, and returned to control by 14 days. The active form of MMP-2 appeared at 7 days postinjury and remained elevated compared with that documented in sham-treated mice for at least 21 days. Increased MMP-2 activity coincided with both revascularization and glial scar formation. Using in situ zymography, gelatinolytic activity was detected in the meninges, vascular elements, glia, and macrophage-like cells in the injured cord. Results of immunolabeling confirmed the presence of gelatinase in vessels during revascularization and in reactive astrocytes associated with glial scar formation. Conclusions. These findings suggest that although MMP-9 and -2 exhibit overlapping expression during revascularization, the former is associated with acute injury responses and the latter with formation of a glial scar.

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“…Both the PA-PG system and the MMP family have been implicated in the cascade of events leading to neuronal apoptosis in the central nervous system (31)(32)(33)(34)(35)(36). More specifically, mice deficient for tissue plasminogen activator or PG were found to be resistant to neuronal destruction induced by excitotoxins (37,38).…”

mentioning

confidence: 99%

Deficiency in Matrix Metalloproteinase Gelatinase B (MMP-9) Protects against Retinal Ganglion Cell Death after Optic Nerve Ligation

Chintala

Zhang

Austin

et al. 2002

Journal of Biological Chemistry

129

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Loss of retinal ganglion cells is the final end point in blinding diseases of the optic nerve such as glaucoma.To enable the use of mouse genetics to investigate mechanisms underlying ganglion cell loss, we adapted an experimental model of optic nerve ligation to the mouse and further characterized post-surgical outcome. We made the novel finding that apoptosis of retinal ganglion cells correlates with specific degradation of laminin from the underlying inner limiting membrane and an increase in gelatinolytic metalloproteinase activity. These changes co-localize with a specific increase in levels of the matrix metalloproteinase, gelatinase B (GelB; MMP-9). Using a transgenic mouse line harboring a reporter gene driven by the GelB promoter, we further show that increased GelB is controlled by activation of the GelB promoter. These findings led us to hypothesize that GelB activity plays a role in ganglion cell death and degradation of laminin. Applying the genetic approach, we demonstrate that GelB-deficient mice are protected against these pathological changes. This is the first report demonstrating a causal connection between GelB activity and pathological changes to the inner retina after optic nerve ligation.

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Expression and Activation of Matrix Metalloproteinase-2 and -9 in Rat Brain after Transient Focal Cerebral Ischemia

Cited by 218 publications

References 57 publications

Matrix metalloproteinases and their endogenous inhibitors in neuronal physiology of the adult brain

Matrix metalloproteinases and their endogenous inhibitors in neuronal physiology of the adult brain

Differential temporal expression of matrix metalloproteinases after spinal cord injury: relationship to revascularization and wound healing

Deficiency in Matrix Metalloproteinase Gelatinase B (MMP-9) Protects against Retinal Ganglion Cell Death after Optic Nerve Ligation

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