Publications by authors named "Evelyne Tremblay"
Article Synopsis
- TIMP-1 has diverse functions in the brain, particularly increasing in reactive astrocytes and neurons after injury or inflammation, but its specific effects on neuron growth and shape were previously unclear.
- After 24 hours of treatment, TIMP-1 notably decreased neurite length by 35%, while causing growth cones to enlarge and increasing the number of microprocesses, with effects lasting up to 48 hours.
- The changes induced by TIMP-1 do not stem from its ability to inhibit certain MMPs but may involve interactions with MMP-2, suggesting its role as a significant modulator of neuron morphology and growth in the context of brain injuries.
Article Synopsis
- Matrix metalloproteinases (MMPs) and tissue inhibitors (TIMPs) are involved in protein cleavage and are secreted from neuronal cells via specific vesicles, contributing to cellular processes.
- The study focuses on MMP-2, MMP-9, and TIMP-1, using advanced imaging techniques to reveal that they are secreted in vesicles that travel along microtubules and microfilaments.
- Findings indicate that these MMPs are localized in dendritic spines of neurons, highlighting their potential role in neuronal and synaptic plasticity.
The tissue inhibitor of metalloproteinases-1 (TIMP-1) belongs to a family of multifunctional proteins that inhibit matrix metalloproteinases (MMPs), but also regulate cell growth, proliferation, migration and apoptosis in non-nervous tissues. We had previously reported that kainate (KA)-mediated excitotoxic seizures induce the expression of TIMP-1 in resistant neurons and reactive astrocytes of the rat CNS, but the functional implications of these changes had not been elucidated. In the present work we used a targeted gene null mutation in mice to investigate in vivo the involvement of TIMP-1 in neuronal death and axonal sprouting following KA.
View Article and Find Full Text PDFThe matrix metalloproteinases (MMP) belong to a growing family of secreted or membrane-bound (MT-MMP) enzymes that cleave protein components of the extracellular matrix and bioactive factors involved in intercellular signaling. MMP activity is counterbalanced by their four physiological inhibitors, the tissue inhibitors of MMP (TIMPs). Together, MMP and TIMP control cell-cell and cell-matrix interactions associated with physiological processes.
View Article and Find Full Text PDFMatrix metalloproteinases (MMPs) and the tissue inhibitors of MMPs (TIMPs) are emerging as important modulators of brain physiopathology. Dramatic changes in the expression of MMPs and TIMPs occur during excitotoxic/neuroinflammatory processes. However, only the measurement of net protease activity is relevant physiologically, and the functional consequences of MMP/TIMP ratio modifications in the brain remain elusive.
View Article and Find Full Text PDFThe matrix metalloproteinases (MMPs) belong to a growing family of Zn2+-dependent endopeptidases, secreted or membrane-bound (MT-MMP), that regulate or degrade by proteolytic cleavage protein components of the extracellular matrix, cytokines, chemokines, cell adhesion molecules and a variety of membrane receptors. MMP activity is counterbalanced by their physiological inhibitors, the tissue inhibitors of MMPs (TIMPs), a family of 4 secreted multifunctional proteins that have growth promoting activities. In physiological conditions MMP activity is tightly regulated and altered MMP regulation is associated with pathological processes including inflammation, cell proliferation, cell death and tissue remodeling.
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