scholarly journals The Matrix Metalloproteinases and Cerebral Ischemia

10.5772/33861 ◽  
2012 ◽  
Author(s):  
Wan Yang ◽  
Guangqin Li
Keyword(s):  
Cerebral Ischemia ◽  
Matrix Metalloproteinases ◽  
The Matrix

Neuroprotection by μ-calpain and matrix metalloproteinases inhibition by Piroxicam in cerebral ischemia: an in silico study

2013 ◽  
Vol 22 (11) ◽  
pp. 5112-5119 ◽  
Author(s):  
Pallab Bhattacharya ◽  
Anand Kumar Pandey ◽  
Swet Chand Shukla ◽  
Sudip Paul ◽  
Ranjana Patnaik
Keyword(s):  
Cerebral Ischemia ◽  
Matrix Metalloproteinases ◽  
In Silico ◽  
In Silico Study

The matrix metalloproteinases inhibitor Ro 26-2853 extends survival in transgenic ALS mice

2006 ◽  
Vol 200 (1) ◽  
pp. 166-171 ◽  
Author(s):  
Stefan Lorenzl ◽  
Sabine Narr ◽  
Barabara Angele ◽  
Hans Willi Krell ◽  
Jason Gregorio ◽  
...  
Keyword(s):  
Matrix Metalloproteinases ◽  
The Matrix

VEGF signaling activates the matrix metalloproteinases, MmpL7 and MmpL5 at the sites of active skeletal growth and MmpL7 regulates skeletal elongation

2021 ◽  
Vol 473 ◽  
pp. 80-89
Author(s):  
Miri Morgulis ◽  
Mark R. Winter ◽  
Ligal Shternhell ◽  
Tsvia Gildor ◽  
Smadar Ben-Tabou de-Leon
Keyword(s):  
Matrix Metalloproteinases ◽  
Skeletal Growth ◽  
Vegf Signaling ◽  
The Matrix

Progression of mycosis fungoides is associated with changes in angiogenesis and expression of the matrix metalloproteinases 2 and 9

1997 ◽  
Vol 33 (10) ◽  
pp. 1685-1692 ◽  
Author(s):  
A. Vacca ◽  
S. Moretti ◽  
D. Ribatti ◽  
A. Pellegrino ◽  
N. Pimpinelli ◽  
...  
Keyword(s):  
Matrix Metalloproteinases ◽  
Mycosis Fungoides ◽  
The Matrix

Understanding the P1‘ Specificity of the Matrix Metalloproteinases:  Effect of S1‘ Pocket Mutations in Matrilysin and Stromelysin-1†

Biochemistry ◽  
1996 ◽  
Vol 35 (31) ◽  
pp. 10103-10109 ◽  
Author(s):  
Anthony R. Welch ◽  
Christopher M. Holman ◽  
Martin Huber ◽  
Mitchell C. Brenner ◽  
Michelle F. Browner ◽  
...  
Keyword(s):  
Matrix Metalloproteinases ◽  
The Matrix

scholarly journals Proteolytic Events of Wound-Healing — Coordinated Interactions Among Matrix Metalloproteinases (MMPs), Integrins, and Extracellular Matrix Molecules

2001 ◽  
Vol 12 (5) ◽  
pp. 373-398 ◽  
Author(s):  
Bjorn Steffensen ◽  
Lari Häkkinen ◽  
Hannu Larjava
Keyword(s):  
Extracellular Matrix ◽  
Wound Healing ◽  
Matrix Metalloproteinases ◽  
Wound Repair ◽  
Enzyme Activation ◽  
Processing Enzymes ◽  
The Matrix ◽  
Signaling Receptors ◽  
State Of Rest ◽  
And Function

During wound-healing, cells are required to migrate rapidly into the wound site via a proteolytically generated pathway in the provisional matrix, to produce new extracellular matrix, and, subsequently, to remodel the newly formed tissue matrix during the maturation phase. Two classes of molecules cooperate closely to achieve this goal, namely, the matrix adhesion and signaling receptors, the integrins, and matrix-degrading and -processing enzymes, the matrix metalloproteinases (MMPs). There is now substantial experimental evidence that blocking key molecules of either group will prevent or seriously delay wound-healing. It has been known for some time now that cell adhesion by means of the integrins regulates the expression of MMPs. In addition, certain MMPs can bind to integrins or other receptors on the cell surface involved in enzyme activation, thereby providing a mechanism for localized matrix degradation. By proteolytically modifying the existing matrix molecules, the MMPs can then induce changes in cell behavior and function from a state of rest to migration. During wound repair, the expression of integrins and MMPs is simultaneously up-regulated. This review will focus on those aspects of the extensive knowledge of fibroblast and keratinocyte MMPs and integrins in biological processes that relate to wound-healing.

scholarly journals Novel Role of MCP-Induced Protein 1 in Ischemic Brain Damage in Animals of Transient Focal Ischemia

2018 ◽  
Author(s):  
Zhuqing Jin ◽  
Jian Liang ◽  
Jiaqi Li ◽  
Pappachan E. Kolattukudy
Keyword(s):  
Cerebral Ischemia ◽  
Matrix Metalloproteinases ◽  
Tight Junction ◽  
Western Blot ◽  
Blood Brain Barrier ◽  
Wild Type Mouse ◽  
Brain Barrier ◽  
Wild Type ◽  
Blood Brain

Focal cerebral ischemia can lead to blood-brain barrier (BBB) breakdown, which is implicated in neuroinflammation and elevation of matrix metalloproteinases (MMPs). The role of the anti-inflammatory protein, monocyte chemotactic protein–induced protein 1 (MCPIP1) plays in the injury of BBB in stroke has not yet been reported. This study was conducted to identify and characterize the role MCPIP1 plays in BBB breakdown. Transient middle cerebral artery occlusion (MCAO) is induced in both wild-type and Mcpip1-/- mice for 2 hours of occlusion periods followed by reperfusion for 24 or 48 hours. BBB permeability was measured by FITC-dextran extravasation, MMP-9/3 expression was analyzed by western blot, and claudin-5 and zonula occludens-1 (ZO-1) were analyzed by immunohistochemistry and western blot. After MCAO in wild type mouse is induced, there is significantly increase in MCPIP1 mRNA and protein levels. Absence of MCPIP1 leaded to significant increase in FITC-dextran leakage in peri-infarct brain, significant upregulation of MMP-9, MMP-3 and reduced levels of tight junction components, claudin-5 and ZO-1 in the brain after MCAO. Our data demonstrate that absence of MCPIP1 exacerbates ischemia-induced blood-brain barrier disruption by enhancing the expression of matrix metalloproteinases and degradation of tight junction proteins. Overall data indicate that MCPIP1 is important protective role against BBB disruption in cerebral ischemia.

Matrix Metalloproteinases: Biologic Activity and Clinical Implications

2000 ◽  
Vol 18 (5) ◽  
pp. 1135-1135 ◽  
Author(s):  
Amy R. Nelson ◽  
Barbara Fingleton ◽  
Mace L. Rothenberg ◽  
Lynn M. Matrisian
Keyword(s):  
Matrix Metalloproteinases ◽  
Tumor Growth ◽  
Tumor Progression ◽  
Metastatic Tumor ◽  
The Body ◽  
Genetic Changes ◽  
Biologic Activity ◽  
The Matrix ◽  
Degradative Enzymes

ABSTRACT: Tumor progression is a complex, multistage process by which a normal cell undergoes genetic changes that result in phenotypic alterations and the acquisition of the ability to spread and colonize distant sites in the body. Although many factors regulate malignant tumor growth and spread, interactions between a tumor and its surrounding microenvironment result in the production of important protein products that are crucial to each step of tumor progression. The matrix metalloproteinases (MMPs) are a family of degradative enzymes with clear links to malignancy. These enzymes are associated with tumor cell invasion of the basement membrane and stroma, blood vessel penetration, and metastasis. They have more recently been implicated in primary and metastatic tumor growth and angiogenesis, and they may even have a role in tumor promotion. This review outlines our current understanding of the MMP family, including the association of particular MMPs with malignant phenotypes and the role of MMPs in specific steps of the metastatic cascade. As scientific understanding of the MMPs has advanced, therapeutic strategies that capitalize on blocking the enzymes have rapidly developed. The preclinical and clinical evolution of the synthetic MMP inhibitors (MMPIs) is also examined, with the discussion encompassing important methodologic issues associated with determining clinical efficacy of MMPIs and other novel therapeutic agents.

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