scholarly journals Cell-mediated degradation of type IV collagen and gelatin films is dependent on the activation of matrix metalloproteinases

1992 ◽  
Vol 288 (2) ◽  
pp. 605-611 ◽  
Author(s):  
S J Atkinson ◽  
R V Ward ◽  
J J Reynolds ◽  
G Murphy
Keyword(s):  
Matrix Metalloproteinases ◽  
Oxygen Radicals ◽  
Type Iv Collagen ◽  
Model System ◽  
Dermal Fibroblasts ◽  
Gelatinase A ◽  
Reactive Oxygen Metabolite ◽  
Gelatinase B ◽  
Type Iv ◽  
Gelatin Films

The ability of normal rabbit dermal fibroblasts to degrade films of type IV collagen and gelatin when stimulated by phorbol ester was shown to be dependent on the induction, secretion and activation of 95 kDa gelatinase B and the secretion and activation of 72 kDa gelatinase A and stromelysin. Degradation was inhibited by exogenous human recombinant tissue inhibitor of metalloproteinases-1, specific antibodies to gelatinase and stromelysin and by the reactive-oxygen-metabolite inhibitor catalase. We discuss the various pathways for activation of matrix metalloproteinases in this model system and conclude that, although plasmin may play a key role in the activation of gelatinase B and stromelysin, gelatinase A is activated by a mechanism which has yet to be elucidated. The involvement of oxygen radicals in the direct activation of matrix metalloproteinases in this model is thought to be unlikely.

scholarly journals Differential regulation of matrix metalloproteinases and their inhibitors in human glomerular epithelial cells in vitro.

1998 ◽  
Vol 9 (9) ◽  
pp. 1629-1637
Author(s):  
J Martin ◽  
R Steadman ◽  
J Knowlden ◽  
J Williams ◽  
M Davies
Keyword(s):  
Epithelial Cells ◽  
Matrix Metalloproteinases ◽  
Specific Inhibitor ◽  
Differential Regulation ◽  
Dependent Manner ◽  
Gelatinase A ◽  
Type Iv Collagenase ◽  
Gelatinase B ◽  
Type Iv ◽  
Glomerular Epithelial Cells

The present study examines the effect of transforming growth factor-beta1 (TGF-beta1) and interleukin-1beta (IL-1beta) on the regulation of gelatinase A, gelatinase B, tissue inhibitor of metalloproteinase-I (TIMP-I) and TIMP-II in human glomerular epithelial cells (GEC). The addition of TGF-beta1 resulted in the increased production and secretion of both gelatinase A (72-kD type IV collagenase) and gelatinase B (92-kD type IV collagenase), in a dose- and time-dependent manner. In contrast, the addition of IL-1beta to GEC resulted in the stimulation of secretion of gelatinase B but not gelatinase A. When the secretion of the regulatory inhibitors was examined, IL-1beta or TGF-beta1 both resulted in an increased secretion of TIMP-I, whereas the secretion of TIMP-II was downregulated. Such results demonstrate an independent and opposite regulation of the enzymes and their inhibitors. Of particular interest was the observation of the differential regulation of gelatinase A and its specific inhibitor TIMP-II (which binds to the latent form of this enzyme) in response to TGF-beta1. These results for the first time indicate that in human GEC, matrix metalloproteinases (MMP), as well as their specific inhibitors, are independently regulated by different cytokines. MMP and their regulatory tissue inhibitors (TIMP) play an important role in tissue remodeling. The results of the present study serve to emphasize both the complex regulation of matrix metabolism in the glomerulus and the potential pathologic role of an imbalance between the proteinases and their inhibitors in various forms of glomerular disease.

Comparative analysis of basal lamina type IV collagen α chains, matrix metalloproteinases-2 and -9 expressions in oral dysplasia and invasive carcinoma

2013 ◽  
Vol 115 (2) ◽  
pp. 113-119 ◽  
Author(s):  
Ryo Tamamura ◽  
Hitoshi Nagatsuka ◽  
Chong Huat Siar ◽  
Naoki Katase ◽  
Ichiro Naito ◽  
...  
Keyword(s):  
Comparative Analysis ◽  
Matrix Metalloproteinases ◽  
Basal Lamina ◽  
Type Iv Collagen ◽  
Invasive Carcinoma ◽  
Oral Dysplasia ◽  
Type Iv

Expression of matrix metalloproteinases, type IV collagen, and interleukin-10 in rabbits treated with morphine after lamellar keratectomy

2011 ◽  
Vol 15 (3) ◽  
pp. 153-163 ◽  
Author(s):  
Alexandre P. Ribeiro ◽  
Miguel L. Silva ◽  
Rodrigo L. Araújo ◽  
Danilo L. Ferrucci ◽  
Tiago Mineo ◽  
...  
Keyword(s):  
Matrix Metalloproteinases ◽  
Type Iv Collagen ◽  
Interleukin 10 ◽  
Type Iv

Distribution of gelatinase B (MMP-9) and type IV collagen in colorectal carcinoma

1994 ◽  
Vol 9 (3) ◽  
pp. 141-148 ◽  
Author(s):  
M. Jeziorska ◽  
N. Y. Haboubi ◽  
P. F. Schofield ◽  
Y. Ogata ◽  
H. Nagase ◽  
...  
Keyword(s):  
Colorectal Carcinoma ◽  
Type Iv Collagen ◽  
Gelatinase B ◽  
Type Iv

scholarly journals Proteolytic Cascade Enzymes Increase in Focal Cerebral Ischemia in Rat

1996 ◽  
Vol 16 (3) ◽  
pp. 360-366 ◽  
Author(s):  
Gary A. Rosenberg ◽  
Milo Navratil ◽  
Frank Barone ◽  
Giora Feuerstein
Keyword(s):  
Focal Cerebral Ischemia ◽  
Vasogenic Edema ◽  
Artery Occlusion ◽  
Tissue Type ◽  
Intracerebral Injection ◽  
Gelatinase A ◽  
Type Iv Collagenase ◽  
Gelatinase B ◽  
Type Iv ◽  
Wistar Kyoto

Cerebral infarction initiates a cascade of molecular events, leading to proteolytic cell death. Matrix-degrading metalloproteinases (MMPs) are neutral proteases involved in extracellular matrix damage. Type IV collagenase is an MMP that increases cerebral capillary permeability after intracerebral injection and may be important along with plasminogen activators (PA) in secondary brain edema in stroke. Therefore, we measured MMPs and PAs in spontaneously hypertensive (SHR) or Wistar-Kyoto (WKY) rats with permanent middle cerebral artery occlusion (MCAO). Brain tissue was assayed for MMPs and PAs at 1, 3, 12, and 24 h and 5 days after occlusion, using substrate gel Polyacrylamide electrophoresis (zymography). SHR showed an increase in 92-kDa type IV collagenase (gelatinase B) in the infarcted hemisphere compared with the opposite side at 12 and 24 h ( p < 0.05). Gelatinase A remained the same in both infarcted and normal tissue until 5 days after injury, when it increased significantly ( p < 0.05). Urokinase-type PA was increased significantly at 12 and 24 h and 5 days, while tissue-type PA was decreased significantly at 1, 12, and 24 h in the ischemic compared with the nonischemic hemisphere. Gelatinase B was markedly increased in SHR at 12 and 24 h compared with WKY ( p < 0.05). Secondary vasogenic edema is maximal 1–2 days after a stroke, which is the time that gelatinase B was elevated. The time of appearance of gelatinase B suggests a role in secondary tissue damage and vasogenic edema, while gelatinase A may be involved in tissue repair.

scholarly journals New insights about myofibrillar myopathies: the role of metalloproteinases 2 and 9 in the pathogenesis

2020 ◽  
Author(s):  
Alzira Alves de Siqueira Carvalho ◽  
Vinicius Gomes Silva ◽  
Roseli Corazzini ◽  
Alan Patricio Silva ◽  
Emmanuelle Lacene
Keyword(s):  
Gene Expression ◽  
Matrix Metalloproteinases ◽  
Basement Membrane ◽  
Type Iv Collagen ◽  
Statistical Significance ◽  
Myofibrillar Myopathy ◽  
Type Iv ◽  
Pattern Distribution ◽  
Membrane Methods

Abstract Background There are few reports suggesting that gene expression and activation of various matrix metalloproteinases (MMPs) are deregulated. MMP-2 and MMP-9 represent the two MMPs, which degrade type IV collagen, the component of basement membrane. Methods We analyzed the involvement of gelatinases, MMP-2 and MMP-9, in the pathogenesis of myofibrillar myopathy (MFM). Muscle specimens from 23 patients well diagnosed with MFM, were immunostained by MMP-2 and MMP-9. We analyzed qualitatively the immunoexpression in three compartments: subsarcolemmal (SSC), intracytoplasmic (ICC) and perinuclear (PNC). Results 95,7% and 100% samples showed MMP-2 and MMP-9 upregulation ICC, respectively. PNC showed MMP-2 (82,6%) and MMP-9 (8,7%) regulation (p<0.001). SSC and ICC did not present statistical significance. There was no correlation between mutated gene and immunohistochemical pattern distribution. Conclusion Our results suggest that MMP-2 and/or MMP-9 could participate in the pathomechanism of MFM, causing damage of sarcomere and deposition of protein aggregates.

Expression of mRNA for type IV collagen α1, α5 and α6 chains by cultured dermal fibroblasts from patients with X-linked Alport syndrome

1998 ◽  
Vol 17 (4) ◽  
pp. 279-291 ◽  
Author(s):  
Satoshi Sasaki ◽  
Bing Zhou ◽  
Wei Wei Fan ◽  
Youngki Kim ◽  
David F. Barker ◽  
...  
Keyword(s):  
Alport Syndrome ◽  
Type Iv Collagen ◽  
Dermal Fibroblasts ◽  
Type Iv

scholarly journals New insights about myofibrillar myopathies: the role of metalloproteinases 2 and 9 in the pathogenesis

2020 ◽  
Author(s):  
Alzira Alves de Siqueira Carvalho ◽  
Vinicius Gomes Silva ◽  
Roseli Corazzini ◽  
Alan Patricio Silva ◽  
Emmanuelle Lacene
Keyword(s):  
Gene Expression ◽  
Matrix Metalloproteinases ◽  
Type Iv Collagen ◽  
Statistical Significance ◽  
Protein Aggregates ◽  
Myofibrillar Myopathy ◽  
Type Iv

Abstract Background There are few reports suggesting that gene expression and activation of various matrix metalloproteinases (MMPs) are deregulated. MMP-2 and MMP-9 represent the two MMPs, which degrade type IV collagen, the component of basement membrane.Methods We analyzed the involvement of gelatinases, MMP-2 and MMP-9, in the pathogenesis of myofibrillar myopathy (MFM). Muscle specimens from 23 patients well diagnosed with MFM, were immunostained by MMP-2 and MMP-9. We analyzed qualitatively the immunoexpression in three compartments: subsarcolemmal (SSC), intracytoplasmic (ICC) and perinuclear (PNC).Results 95,7% and 100% samples showed MMP-2 and MMP-9 upregulation ICC, respectively. PNC showed MMP-2 (82,6%) and MMP-9 (8,7%) regulation (p<0.001). SSC and ICC did not present statistical significance. There was no correlation between mutated gene and immunohistochemical pattern distribution.Conclusion Our results suggest that MMP-2 and/or MMP-9 could participate in the pathomechanism of MFM, causing damage of sarcomere and deposition of protein aggregates.

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