Differential regulation of tissue inhibitor of metalloproteinase mRNA expression in response to intracranial injury

Jaworski, Diane M.

doi:10.1002/(sici)1098-1136(200004)30:2<199::aid-glia9>3.0.co;2-#

Cited by 56 publications

(33 citation statements)

References 65 publications

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“…Tissue inhibitor of metalloproteinase-3 was found in normal tissues, suggesting that other factors are needed along with TIMP-3 to promote cell death. Although further studies will be necessary to resolve the effect on the normal tissue, the results of the mRNA, provide convincing support for an increase in TIMP-3 on the ischemic zone This is consistent with reports of TIMP-3 gene expression in brain injury and in Wobbler mice [10,11] . Programmed cell death occurs by release of caspaseactivating factors from mitochondria or by the stimulation of cell surface receptors that may or may not act through mitochondrial activation [12] .…”

Section: Discussionsupporting

confidence: 87%

Correlation Between MMP-3, TIMP-3 Expression and Neuronal Apoptosis After Ischemia -Reperfusion Injury in Rates

Zi¹,

Abuhamed²,

Yuan³

et al. 2007

American J. of Immunology

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Matrix metalloproteinases (MMPs) play a central role in many biological processes, such as embryogenesis, normal tissue remodeling, wound healing, and angiogenesis. How MMP3, TIMP3 expression and neuronal apoptosis (Fas, Fas-L and Bcl) may provide detrimental or beneficial actions during the injury and repair processes after cerebral ischemia-reperfusion injury in rates was studied. Adult rats underwent middle cerebral artery occlusion (MCAO) by the suture method. The expression of mRNA for TIMP-3, MMP-3, and neuronal apoptosis -were estimated in samples of Brain cortices of the ischemic penumbra (IPZ) and the core ischemic zone (ICZ) from70 Rates with Ischemic control group (ICG), 10 sham-operated group (SOG) and 60 Ischemic -sodium aescinate intervention group (I G) using the reverse-transcriptasepolymerase chain reaction with a synthetic multicompetitor standard. Also the amounts of neuronal apoptosis positive cells were evaluated by TUNEL assay. I G expressed significantly TIMP-3, MMP-3 mRNA more than the ICG..Also in the ischemic zone Bcl-2 mRNA was strikingly increased whereas Fas and Fas-L mRNA was considerably decreased. At same time, the amount of apoptosis cells was maximally increased at 3 hours and was lowest decreased at 72 hours after reperfusion. Altogether, these results strongly suggest that inappropriate MMP-3 expression combined with increased TIMP-3, the ratio of apoptotic cells shows positive correlation with TIMP-3 , negative correlation with MMP-3 and MMP-3, TIMP-3 Expression might modulate the process of type I and type II neuronal apoptosis through FAS pathway.

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Section: Discussionsupporting

confidence: 87%

Correlation Between MMP-3, TIMP-3 Expression and Neuronal Apoptosis After Ischemia -Reperfusion Injury in Rates

Zi¹,

Abuhamed²,

Yuan³

et al. 2007

American J. of Immunology

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“…Previously, we demonstrated that TIMP-2 expression is increased in response to a penetrating injury to the rat cerebral cortex (30). Therefore, we sought to determine whether DDC8's expression would be similarly up-regulated in response to injury (Fig.…”

Section: The Spatial Expression Of Ddc8 Mrna Mimics That Of Timp-2 Mrnamentioning

confidence: 99%

“…TIMPs are small (20)(21)(22)(23)(24)(25)(26)(27)(28)(29)(30) secreted molecules that are primarily recognized for their inhibition of matrix metalloproteinase (MMP) proteolytic activity (4). In addition to MMP inhibition, TIMPs play a role in MMP activation.…”

Section: Introductionmentioning

confidence: 99%

Potential regulatory relationship between the nested gene DDC8 and its host gene tissue inhibitor of metalloproteinase-2

Jaworski

Beem-Miller

Lluri

et al. 2007

Physiological Genomics

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Nested genes are fairly common within the mammalian nervous system, yet few studies have examined whether the guest and host genes might be coordinately regulated. TIMPs inhibit extracellular matrix proteolysis mediated by metzincin proteases. TIMP-2 is the only TIMP not nested within a synapsin gene. It does, however, serve as a host for DDC8, a testis-specific gene whose expression is up-regulated during spermatogenesis. Here, we demonstrate that DDC8 is not testis-specific. Furthermore, DDC8 expression in non-neural and neural tissues mimics that of TIMP-2, including its up-regulation in response to traumatic brain injury, suggesting a potential regulatory relationship. The most striking observation is that the TIMP-2 knockout mouse brain contains TIMP-2 mRNA encoding exons 2-5, which are down-stream of DDC8, but not exon 1 which contains the signal sequence and cysteine residue required for MMP inhibition, indicating a functional knockout. That TIMP-2 transcripts in wild-type brain contain DDC8 sequence suggests alternative splicing between the two genes.

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“…Prevailing data imply that MMPs are involved in glial functions. Results on MMP and TIMP localization in the CNS have been rather incoherent but do suggest that MMP expression is not specific to a given cell type (Rivera and Khrestchatisky, 1999;Jaworski, 2000). Changes in MMP expression have also been reported in various neuropathologies involving both neurons (neurodegeneration) and glial cells (inflammation and gliomas; Yong et al, 2001).…”

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confidence: 99%

Matrix Metalloproteinase-9 Undergoes Expression and Activation during Dendritic Remodeling in Adult Hippocampus

Szklarczyk

Lapinska²,

Rylski³

et al. 2002

J. Neurosci.

362

352

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Neurons of adult brain are able to remodel their synaptic connections in response to various stimuli. Modifications of the peridendritic environment, including the extracellular matrix, are likely to play a role during synapse remodeling. Proteolytic disassembly of ECM is a complex process using the regulated actions of specific extracellular proteinases. One of bestcharacterized families of matrix-modifying enzymes is the matrix metalloproteinase (MMP) family. Here, we describe changes in the expression and function of two well known MMPs, MMP-9 and MMP-2, in adult rat brain before and after systemic administration of the glutamate receptor agonist kainate. Kainate application results in enhanced synaptic transmission and seizures followed by selective tissue remodeling, primarily in hippocampal dentate gyrus. MMP-9 but not MMP-2 was highly expressed by neurons in normal adult rat brain. MMP-9 protein was localized in neuronal cell bodies and dendrites. Kainate upregulated the level of MMP-9 mRNA and protein within hours after drug administration. This was followed several hours later by MMP-9 enzymatic activation. Within hippocampus, MMP-9 mRNA and activity were increased selectively in dentate gyrus, including its dendritic layer. In addition, MMP-9 mRNA levels decreased in areas undergoing neuronal cell loss. This unique spatiotemporal pattern of MMP-9 expression suggests its involvement in activity-dependent remodeling of dendritic architecture with possible effects on synaptic physiology.

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Differential regulation of tissue inhibitor of metalloproteinase mRNA expression in response to intracranial injury

Cited by 56 publications

References 65 publications

Correlation Between MMP-3, TIMP-3 Expression and Neuronal Apoptosis After Ischemia -Reperfusion Injury in Rates

Correlation Between MMP-3, TIMP-3 Expression and Neuronal Apoptosis After Ischemia -Reperfusion Injury in Rates

Potential regulatory relationship between the nested gene DDC8 and its host gene tissue inhibitor of metalloproteinase-2

Matrix Metalloproteinase-9 Undergoes Expression and Activation during Dendritic Remodeling in Adult Hippocampus

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