基质金属蛋白酶与动脉内膜损伤后再狭窄的研究

基质金属蛋白酶是一类蛋白水解酶家族,能降解各种细胞外基质.动物实验和临床病例分析显示基质金属蛋白酶及其抑制剂的平衡对再狭窄的形成至关重要,本文就动脉损伤后基质金属蛋白酶在再狭窄中的作用加以综述.     

基质金属蛋白酶与动脉内膜损伤后再狭窄的研究

基质金属蛋白酶是一类蛋白水解酶家族,能降解各种细胞外基质.动物实验和临床病例分析显示基质金属蛋白酶及其抑制剂的平衡对再狭窄的形成至关重要,本文就动脉损伤后基质金属蛋白酶在再狭窄中的作用加以综述.     

基质金属蛋白酶与动脉内膜损伤后再狭窄的研究

基质金属蛋白酶是一类蛋白水解酶家族,能降解各种细胞外基质.动物实验和临床病例分析显示基质金属蛋白酶及其抑制剂的平衡对再狭窄的形成至关重要,本文就动脉损伤后基质金属蛋白酶在再狭窄中的作用加以综述.     

基质金属蛋白酶与动脉内膜损伤后再狭窄的研究

基质金属蛋白酶是一类蛋白水解酶家族,能降解各种细胞外基质.动物实验和临床病例分析显示基质金属蛋白酶及其抑制剂的平衡对再狭窄的形成至关重要,本文就动脉损伤后基质金属蛋白酶在再狭窄中的作用加以综述.     

基质金属蛋白酶与动脉内膜损伤后再狭窄的研究

基质金属蛋白酶是一类蛋白水解酶家族,能降解各种细胞外基质.动物实验和临床病例分析显示基质金属蛋白酶及其抑制剂的平衡对再狭窄的形成至关重要,本文就动脉损伤后基质金属蛋白酶在再狭窄中的作用加以综述.     

基质金属蛋白酶与动脉内膜损伤后再狭窄的研究

基质金属蛋白酶是一类蛋白水解酶家族,能降解各种细胞外基质.动物实验和临床病例分析显示基质金属蛋白酶及其抑制剂的平衡对再狭窄的形成至关重要,本文就动脉损伤后基质金属蛋白酶在再狭窄中的作用加以综述.     

基质金属蛋白酶与动脉内膜损伤后再狭窄的研究

基质金属蛋白酶是一类蛋白水解酶家族,能降解各种细胞外基质.动物实验和临床病例分析显示基质金属蛋白酶及其抑制剂的平衡对再狭窄的形成至关重要,本文就动脉损伤后基质金属蛋白酶在再狭窄中的作用加以综述.     

基质金属蛋白酶与动脉内膜损伤后再狭窄的研究

基质金属蛋白酶是一类蛋白水解酶家族,能降解各种细胞外基质.动物实验和临床病例分析显示基质金属蛋白酶及其抑制剂的平衡对再狭窄的形成至关重要,本文就动脉损伤后基质金属蛋白酶在再狭窄中的作用加以综述.     

基质金属蛋白酶与动脉内膜损伤后再狭窄的研究

基质金属蛋白酶是一类蛋白水解酶家族,能降解各种细胞外基质.动物实验和临床病例分析显示基质金属蛋白酶及其抑制剂的平衡对再狭窄的形成至关重要,本文就动脉损伤后基质金属蛋白酶在再狭窄中的作用加以综述.     

乳腺癌基质金属蛋白酶的表达及其意义

目的 研究基质金属蛋白酶（ＭＭＰｓ）与乳腺癌的关系。方法 采用文献回顾的方法对基质金属蛋白酶在乳腺癌中的表达及其意义加以综述。结果 正常状态下，人体内基质金属蛋白酶与其组织抑制剂保持一种平衡状态，而在体外及体内的多项研究中发现，在乳腺癌中多种基质金属蛋白酶有增强的表达。结论 乳腺癌的生长，浸润及转移与基质金属蛋白酶的表达及其抑制剂的关系密切。基质金属蛋白酶可能为一个新的有价值的乳腺癌预后指标，基质     

Induction of metalloproteinases by glomerular mesangial cells stimulated by proteins of the extracellular matrix

Human glomerular mesangial cells (HMC) are embedded in the mesangial matrix (MM) and control its turnover through a dynamic equilibrium between synthesis and degradation. Degradation is controlled by matrix metalloproteinases (MMP), whose activity has been causally implicated in the progression of glomerular disease. In other systems, MMP secretion may be directly affected by exposure to specific matrix proteins. The present study, therefore, investigated the effect of different matrix components on the adherence of HMC and on their secretion and activation of the gelatinases MMP2 and MMP9. HMC adhered strongly (quantified using crystal violet staining) to collagen IV and collagen I (P < 0.01, relative to binding to control, bovine serum albumin (BSA)-coated wells) and to a lesser extent to gelatin IV and fibronectin (P < 0.05). Binding to vitronectin and laminin was not statistically different to control wells. After the addition of these matrix proteins (0.1 microg/ml to 100 microg/ml) to growth-arrested HMC for 72 h, zymography of the conditioned medium established that only fibronectin and collagens I and IV dose-dependently increased latent (72 kD) MMP2 secretion and activation. Fibronectin, however, also induced the secretion of MMP9. Membranes from HMC that had been co-cultured with fibronectin for 72 h were prepared to investigate whether the activation of MMP2 in this system was due to the action of membrane-type (MT)-MMP. When incubated with latent MMP2 for times up to 24 h, these membranes activated the enzyme in a time- and dose-dependent manner. The results demonstrate that specific matrix components increased the secretion of MMP2 and MMP9 from HMC. In addition, MT-MMP activity, selectively induced by fibronectin, was implicated in the activation of the secreted proteinases.     

Oxidative stress-induced c-Jun N-terminal kinase (JNK) activation in tendon cells upregulates MMP1 mRNA and protein expression.

To explore the potential mechanisms of tendon degeneration, we investigated the role of c-Jun N-terminal Kinase (JNK) activation and the regulation of matrix metalloproteinase 1 (MMP1) in tendon matrix degradation under oxidative stress. JNK and MMP1 activity in samples from normal and ruptured human supraspinatus tendons was evaluated by immunohistochemistry. Real-time quantitative PCR was utilized to evaluate MMP1 mRNA expression and Western blotting for MMP1 and JNK protein detection. JNK activation and increased MMP1 activity were found in the torn human supraspinatus tendon tissue, as well as in human tendon cells under in vitro oxidative stress. Inhibition of JNK prevented MMP1 overexpression in oxidative stressed human tendon cells. Results from the current study indicated that stress activated JNK plays an important role in tendon matrix degradation, possibly through upregulating of MMP1.     

Improved bioengineered cartilage tissue formation following cyclic compression is dependent on upregulation of MT1‐MMP

The generation of bioengineered cartilage tissue suitable for transplantation is a potential therapy to treat damaged cartilage. We have shown previously that the physical and biomechanical properties of bioengineered cartilage can be improved by the application of 30 min of cyclic compression by a mechanism involving sequential upregulation of gene and protein levels of membrane type‐1 matrix metalloproteinase (MT1‐MMP) and MMP‐13. In the current study, we demonstrated that MT1‐MMP is critical to this response, as blocking the upregulation of MT1‐MMP prevented the improvement in tissue formation. MT1‐MMP seems to act by inducing tissue remodeling as evidenced by the presence of aggrecan degradation products by Western blot analysis and increased release of matrix molecules into the media. Release of these molecules was diminished when MT1‐MMP upregulation was prevented. This matrix degradation was likely due to MT1‐MMP, as under conditions where MMP‐13 expression is maintained (stimulation in the presence of MT1‐MMP siRNA) the release of these matrix molecules into the media was still prevented. It also appears that MT1‐MMP does not regulate MMP‐13 gene expression, as MT1‐MMP‐siRNA pretreatment had no effect on MMP‐13 expression following mechanical stimulation. Further analysis of the anabolic genes and proteins involved in mechanically stimulated cartilage will lead to better understanding of the mechanism(s) underlying tissue formation yielding improved bioengineered cartilage. © 2010 Orthopaedic Research Society. Published by Wiley Periodicals, Inc. J Orthop Res 28:921–927, 2010