scholarly journals Degradation of Type IV Collagen by Matrix Metalloproteinases Is an Important Step in the Epithelial-Mesenchymal Transformation of the Endocardial Cushions

2000 ◽  
Vol 227 (2) ◽  
pp. 606-617 ◽  
Author(s):  
Wanmin Song ◽  
Kathy Jackson ◽  
Paul G. McGuire
Keyword(s):  
Matrix Metalloproteinases ◽  
Type Iv Collagen ◽  
Endocardial Cushions ◽  
Type Iv ◽  
Mesenchymal Transformation

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

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.

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 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.

scholarly journals Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan. A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and -2 and punctuated metalloproteinase (PUMP)

1991 ◽  
Vol 277 (1) ◽  
pp. 277-279 ◽  
Author(s):  
G Murphy ◽  
M I Cockett ◽  
R V Ward ◽  
A J P Docherty
Keyword(s):  
Matrix Metalloproteinases ◽  
Connective Tissue ◽  
Matrix Metalloproteinase ◽  
Quantitative Data ◽  
Type Iv Collagen ◽  
Quantitative Comparison ◽  
Degrading Enzymes ◽  
Type Iv ◽  
The Matrix

The abilities of the matrix metalloproteinases 95 kDa and 72 kDa gelatinases (type IV collagenases), stromelysins-1 and -2 and punctuated metalloproteinase (PUMP) to degrade insoluble elastin, type IV collagen films and proteoglycan have been compared. The gelatinases and PUMP were markedly more active in the degradation of elastin than were the stromelysins. PUMP and the stromelysins were more potent proteoglycan-degrading enzymes. All of the enzymes studied degraded soluble native type IV collagen, but the gelatinases were more effective at higher temperatures. These quantitative data allow an analysis of the potential relative roles of these metalloproteinases in the breakdown of the key components of connective tissue matrices.

Malignant Mixed Müllerian Tumor of the Uterus. Features Favoring its Origin from a Common Cell Clone and an Epithelial-to-Mesenchymal Transformation Mechanism of Histogenesis

1998 ◽  
Vol 84 (3) ◽  
pp. 391-397 ◽  
Author(s):  
Marcello Guarino ◽  
Ferdinando Giordano ◽  
Francesco Pallotti ◽  
Giulio Polizzotti ◽  
Paolo Tricomi ◽  
...  
Keyword(s):  
Basement Membrane ◽  
Type Iv Collagen ◽  
Cell Clone ◽  
Sarcomatoid Carcinoma ◽  
Muscle Actin ◽  
Transformation Mechanism ◽  
Epithelial Markers ◽  
Type Iv ◽  
Mesenchymal Transformation ◽  
P53 Immunoreactivity

Aims and background Various histogenetic mechanisms have been postulated to explain the biphasic carcinomatous-sarcomatous appearance of malignant mixed müllerian tumors (MMMTs), but the nature of these uncommon neoplasms is still unclear. Some evidence would suggest that MMMT displays similarities with sarcomatoid carcinoma, a tumor arising in extragenital sites that also features a mixed appearance. To gain further insight into the histogenesis of this tumor, we have studied by immunohistochemistry a case of uterine MMMT showing an extensive rhabdomyosarcomatous component. Methods A panel of antibodies including reactivity for p53, cytokeratin, vimentin, desmin, muscle actin, epithelial membrane antigen (EMA), myoglobin, type IV collagen, laminin, and tenascin was applied to paraffin tumor sections by means of the avidin-biotin complex technique. Results p53 immunoreactivity was observed in approximately the same number of cells in carcinomatous and sarcomatous tissue. The former stained for vimentin, cytokeratin and EMA, while the latter, in addition to expressing vimentin, desmin, muscle actin and myoglobin, also exhibited immunoreactivity for epithelial markers such as cytokeratin and EMA. At the borders between carcinoma and sarcoma the basement membrane pattern, as seen by staining for type IV collagen and laminin, showed interruptions in correspondence with areas of transition between the two tissues. Antibody to tenascin strongly labeled the sarcomatous tissue immediately around carcinomatous elements. Conclusions A similar immunoreactivity for p53 in both carcinomatous and sarcomatous components, expression of epithelial markers in the sarcomatous cells, and disruption of the basement membrane profile in areas of transition between carcinomatous and sarcomatous tissue, would all suggest, as has been postulated for extragenital sarcomatoid carcinomas, an origin from a common epithelial clone and an epithelial-to-mesenchymal transformation-based mechanism of development for this MMMT. In addition, these findings provide further analogies between these categories of tumors, supporting a unifying nosological concept for MMMTs and sarcomatoid carcinomas of non-genital tract origin.

The use of 1nm silver enhanced gold probes for the detection of skin antigens

1990 ◽  
Vol 48 (3) ◽  
pp. 902-903
Author(s):  
J.P Cassella ◽  
H. Shimizu ◽  
A. Ishida-Yamamoto ◽  
R.A.J. Eady
Keyword(s):  
Type Iv Collagen ◽  
Freeze Substitution ◽  
Collagen Type Iv ◽  
Electron Microscopic ◽  
Normal Human Skin ◽  
Type Iv ◽  
Type Vii Collagen ◽  
Keratin Filaments ◽  
Normal Human ◽  
Phosphate Buffered Saline

1nm colloidal gold with silver enhancement has been used in conjunction with a low-temperature post-embedding (post-E) technique for the demonstration of skin antigens at both the light microscopic (LM) and electron microscopic (EM) levels.Keratin filaments and basement membrane zone (BMZ) associated antigens in normal human skin (NHS) were immunolabelled using antibodies against keratin 14, 10, and 1, the carboxy-terminus and collagenous portion of type VII collagen, type IV collagen and bullous pemphigoid antigen (BP-Ag).Fresh samples of NHS were cryoprotected in 15% glycerol, cryofixed in propane at -190°C, subjected to freeze substitution in methanol at -80°C and embedded in Lowicryl K11M at -60°C. Polymerisation of the resin was initiated under UVR at - 60°C for 48 hours and continued at room temperature for a further 48 hours. Semith in sections were air dried onto slides coated with 3-aminopropyltriethoxysilane. The following immunolabelling protocol was adopted: Primary antibody was applied for 2 hours at 37°C or overnight at 4°C. Following washing in Dulbecco’s phosphate buffered saline (PBSA) a biotinylated secondary antibody was applied for 2 hours at 37°C. The sections were further washed in PBSA and 1nm gold avidin was applied. Sections were finally washed in PBSA and silver enhanced.

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