Results 261 to 270 of about 19,663,610 (303)

Tissue inhibitor of metalloproteinases‐3 and matrix metalloproteinase‐3 regulate neuronal sensitivity to doxorubicin‐induced apoptosis

European Journal of Neuroscience, 2003
AbstractMetalloproteinase activity at the cell surface influences cellular sensitivity to extrinsic death vs. survival signals in a variety of cell types, through proteolytic shedding of cell surface signalling molecules. Tissue inhibitor of metalloproteinases‐3 (TIMP‐3) is a unique natural metalloproteinase inhibitor that plays a pro‐apoptotic role ...
M, Wetzel, G A, Rosenberg, L A, Cunningham   +2 more
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Matrix Metalloproteinase-3 on Ligamentum Flavum in Degenerative Lumbar Spondylolisthesis

Spine, 2009
Study Design. Human ligamentum flavum (LF) was examined for the activity level of matrix metalloproteinase-3 (MMP-3) in degenerative spondylolithesis (DS) patients using immunohistochemistry, Western blot, reverse transcriptase-polymerase chain reaction (RT-PCR), and quantitative real-time PCR.
In-Soo, Oh, Kee-Yong, Ha
openaire   +2 more sources

Evaluation of serum matrix metalloproteinase-3 as a biomarker for diagnosis of epilepsy

Journal of the Neurological Sciences, 2016
Reliable molecular biomarkers for epilepsy have yet to be identified. The present study aims to evaluate the utility of serum metalloproteinase-3 as a diagnostic biomarker for epilepsy.Serum MMP-3 levels were assessed in 227 individuals with epilepsy and 97 healthy control subjects.
Rui, Wang, Guang Qun, Zeng, Xu, Liu, Rui Zhan, Tong, Dong, Zhou, Zhen, Hong   +5 more
openaire   +2 more sources

A Protective Role for Matrix Metalloproteinase-3 in Squamous Cell Carcinoma

Cancer Research, 2004
AbstractElevated expression of matrix metalloproteinase-3 (MMP-3/stromelysin-1) is associated with a variety of tumor types, although its in vivo functional role remains unclear. In human and murine squamous cell carcinoma (SCC), MMP-3 is expressed in the stromal compartment at all of the stages of tumor progression and is expressed by the malignant ...
Lisa J, McCawley, Howard C, Crawford, Lloyd E, King, John, Mudgett, Lynn M, Matrisian   +4 more
openaire   +2 more sources

An Aberrant Cerebellar Development in Mice Lacking Matrix Metalloproteinase-3

Molecular Neurobiology, 2011
Cell-cell and cell-matrix interactions are necessary for neuronal patterning and brain wiring during development. Matrix metalloproteinases (MMPs) are proteolytic enzymes capable of remodelling the pericellular environment and regulating signaling pathways through cleavage of a large degradome. MMPs have been suggested to affect cerebellar development,
Inge, Van Hove, Mieke, Verslegers, Tom, Buyens, Nathalie, Delorme, Kim, Lemmens, Stijn, Stroobants, Ilse, Gantois, Rudi, D'Hooge, Lieve, Moons   +8 more
openaire   +2 more sources

Role of matrix metalloproteinase-3 in neurodegeneration.

Journal of neurochemistry, 2013
Matrix metalloproteinase-3 (MMP-3) is a member of the class of zinc-dependent proteases known to degrade the extracellular matrix. MMP-3 activity is regulated at three different levels: gene expression, proteolytic activation of the zymogen, and inhibition by the endogenous tissue inhibitors of metalloproteinase.
Eun-Mee, Kim, Onyou, Hwang
openaire   +1 more source

Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin)

Biochemistry, 1990
The mechanism of activation of tissue procollagenase by matrix metalloproteinase 3 (MMP-3)/stromelysin was investigated by kinetic and sequence analyses. MMP-3 slowly activated procollagenase by cleavage of the Gln80-Phe81 bond to generate a fully active collagenase of Mr = 41,000.
Suzuki, K, Enghild, J J; id_orcid 0000-0001-9292-9172, Morodomi, T, Salvesen, G, Nagase, H   +4 more
openaire   +3 more sources

Production of human matrix metalloproteinase 3 (stromelysin) in Escherichia coli

Gene, 1994
Full-length human matrix metalloproteinase 3 (prostomelysin or proMMP-3) was produced in Escherichia coli as an intracellular insoluble aggregate that could be solubilized and refolded to yield an activatable proenzyme. The refolded protein was purified to > 95% homogeneity.
S A, Rosenfeld, O H, Ross, J I, Corman, M A, Pratta, D L, Blessington, W S, Feeser, B D, Freimark   +6 more
openaire   +2 more sources

Matrix Metalloproteinase-3 Production by Human Degenerated Intervertebral Disc

Journal of SPINAL DISORDERS, 1997
To assess its possible role in the pathophysiology of intervertebral disc degeneration, we investigated the production of matrix metalloproteinase-3 (MMP-3) using human intervertebral disc explant culture. Five normal and 10 degenerated disc specimens were used. The levels of MMP-3 released in the medium were measured with use of an enzyme immunoassay.
O, Nemoto, M, Yamagishi, H, Yamada, T, Kikuchi, H, Takaishi   +4 more
openaire   +2 more sources

Matrix Metalloproteinase-3 Gene Polymorphisms Are Associated with Ischemic Stroke

Journal of Interferon & Cytokine Research, 2012
Stroke is a heterogeneous disease caused by different pathogenic mechanisms. Several candidate genes for stroke have been proposed, but few have been replicated. Matrix metalloproteinases (MMPs) are expressed following stroke. We investigated the association of single nucleotide polymorphisms (SNPs) of the MMP3 gene with stroke in the Korean population.
Su Kang, Kim, Sung Wook, Kang, Dong Hwan, Kim, Dong Hwan, Yun, Joo-Ho, Chung, Ju Yeon, Ban   +5 more
openaire   +2 more sources