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

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

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.

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.

THE MATRIX METALLOPROTEINASES AND THEIR INHIBITORS

2005 ◽  
pp. 3-16 ◽  
Author(s):  
M. M. Handsley ◽  
J. Cross ◽  
J. Gavrilovic ◽  
D. R. Edwards
Keyword(s):  
Matrix Metalloproteinases ◽  
The Matrix

Molecular regulation of cellular invasion— role of gelatinase A and TIMP-2

1996 ◽  
Vol 74 (6) ◽  
pp. 823-831 ◽  
Author(s):  
Anita E. Yu ◽  
Robert E. Hewitt ◽  
David E. Kleiner ◽  
William G. Stetler-Stevenson
Keyword(s):  
Extracellular Matrix ◽  
Matrix Metalloproteinases ◽  
Tissue Inhibitors Of Metalloproteinases ◽  
Gelatinase A ◽  
Cellular Mechanisms ◽  
Cell Matrix ◽  
Matrix Interactions ◽  
The Matrix ◽  
Cell Matrix Interactions

Extracellular matrix (ECM) turnover is an event that is tightly regulated. Much of the coordinate (physiological) or discoordinate (pathological) degradation of the ECM is catalyzed by a class of proteases known as the matrix metalloproteinases (MMPs) or matrixins. Matrixins are a family of homologous Zn atom dependent endopeptidases that are usually secreted from cells as inactive zymogens. Net degradative activity in the extracellular environment is regulated by specific activators and inhibitors. One member of the matrixin family, gelatinase A, is regulated differently from other MMPs, suggesting that it may play a unique role in cell–matrix interactions, including cell invasion. The conversion from the 72 kDa progelatinase A to the active 62 kDa species may be a key event in the acquisition of invasive potential. This discussion reviews some recent findings on the cellular mechanisms involved in progelatinase A activation and, in particular, the role of tissue inhibitor of matrix metalloproteinases-2 (TIMP-2) and transmembrane containing metalloproteinases (MT-MMP) in this process.Key words: tissue inhibitors of metalloproteinases, metalloproteinase, gelatinases, extracellular matrix, activation.

Selective cleavage of human IgG by the matrix metalloproteinases, matrilysin and stromelysin

2002 ◽  
Vol 81 (1) ◽  
pp. 41-48 ◽  
Author(s):  
Andrew J.H Gearing ◽  
Susan J Thorpe ◽  
Karen Miller ◽  
Matthew Mangan ◽  
Paul G Varley ◽  
...  
Keyword(s):  
Matrix Metalloproteinases ◽  
Human Igg ◽  
The Matrix

Matrix Metalloproteinases: Implication in Vascular Matrix Remodelling during Atherogenesis

1998 ◽  
Vol 94 (2) ◽  
pp. 103-110 ◽  
Author(s):  
Shu Ye ◽  
Steve Humphries ◽  
Adriano Henney
Keyword(s):  
Matrix Metalloproteinases ◽  
Plaque Rupture ◽  
Matrix Deposition ◽  
Naturally Occurring ◽  
Extracellular Matrix Components ◽  
The Matrix ◽  
Preferential Binding ◽  
Artery Disease ◽  
Matrix Accumulation ◽  
Functional Analyses

1. The matrix metalloproteinases are a family of at least 16 zinc-dependent endopeptidases possessing catalytic activity against extracellular matrix components. Some members of this family have been implicated in vascular matrix remodelling in the pathogenesis of atherosclerosis. 2. A common, naturally occurring variant has been identified in the promoter of the stromelysin gene with one allele having a run of five adenosines (5A) and the other having six adenosines (6A). Functional analyses have shown that the 6A allele has a lower promoter activity than the 5A allele, which is probably attributable to preferential binding of a putative transcriptional repressor protein. 3. In patients with coronary artery disease, the 6A allele has been found to be associated with progression of atherosclerosis assessed by sequential quantitative angiography. 4. In conclusion, the matrix metalloproteinases may be over-expressed in certain locations in atherosclerotic plaques, which might contribute to local destruction of connective tissue and thus plaque rupture. In the majority of lesional areas, however, matrix synthesis is likely to outstrip matrix degradation, because matrix accumulation is a major feature of most atheromas. This imbalance favouring matrix deposition is likely to be exacerbated in individuals with the 6A6A genotype in whom stromelysin expression is lower due to the weaker stromelysin promoter.

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