scholarly journals An Assay to Quantify Chemotactic Properties of Degradation Products from Extracellular Matrix

2013 ◽  
pp. 103-110 ◽  
Author(s):  
Brian M. Sicari ◽  
Li Zhang ◽  
Ricardo Londono ◽  
Stephen F. Badylak
Keyword(s):  
Extracellular Matrix ◽  
Degradation Products

scholarly journals Degradation of glomerular basement membrane by purified mammalian metalloproteinases

1988 ◽  
Vol 254 (2) ◽  
pp. 609-612 ◽  
Author(s):  
W H Baricos ◽  
G Murphy ◽  
Y W Zhou ◽  
H H Nguyen ◽  
S V Shah
Keyword(s):  
Extracellular Matrix ◽  
Basement Membrane ◽  
Glomerular Basement Membrane ◽  
Degradation Products ◽  
Gel Chromatography ◽  
Collagen Types ◽  
Percentage Release ◽  
Dose Dependent

Neutral metalloproteinases degrade components of the extracellular matrix, including collagen types I-V, fibronectin, laminin and proteoglycan. However, their ability to degrade intact glomerular basement membrane (GBM) has not previously been investigated. Incubation of [3H]GBM (50,000 c.p.m.; pH 7.5; 24 h at 37 degrees C) with purified gelatinase or stromelysin (2 units) resulted in significant GBM degradation: gelatinase, 46 +/- 2.2; stromelysin, 59 +/- 5.8 (means +/- S.E.M.; percentage release of non-sedimentable radioactivity; n = 4). In contrast, 2 units of collagenase released only 5.6 +/- 0.52% (n = 3) of the [3H]GBM radioactivity compared with 2.0 +/- 0.15% (n = 7) released from [3H]GBM incubated alone. Sephadex G-200 gel chromatography of supernatants obtained from incubations of [3H]GBM with either gelatinase or stromelysin confirmed the ability of these enzymes to degrade GBM and revealed both high-(800,000) and relatively low-(less than 20,000) Mr degradation products for both enzymes. GBM degradation by gelatinase and stromelysin was dose-dependent (range 0.02-2.0 units), near maximal between pH 6.0 and 8.6, and was completely inhibited (greater than 95%) by 2 mM-o-phenanthroline. Collagenase (2 units) did not enhance the degradation of GBM by either gelatinase (0.02 or 0.2 unit) or stromelysin (0.02 or 0.2 unit). Our results indicate that metalloproteinase-mediated GBM degradation by neutrophils and glomeruli may be attributable to gelatinase (neutrophils) and/or stromelysin (glomeruli) and suggest an important role for these proteinases in glomerular pathophysiology.

scholarly journals Extracellular Matrix Degradation Products and Low-Oxygen Conditions Enhance the Regenerative Potential of Perivascular Stem Cells

2011 ◽  
Vol 17 (1-2) ◽  
pp. 37-44 ◽  
Author(s):  
Stephen Tottey ◽  
Mirko Corselli ◽  
Eric M. Jeffries ◽  
Ricardo Londono ◽  
Bruno Peault ◽  
...  
Keyword(s):  
Stem Cells ◽  
Extracellular Matrix ◽  
Degradation Products ◽  
Matrix Degradation ◽  
Low Oxygen ◽  
Extracellular Matrix Degradation ◽  
Oxygen Conditions ◽  
Perivascular Stem Cells

Antibacterial Activity within Degradation Products of Biological Scaffolds Composed of Extracellular Matrix

2006 ◽  
Vol 0 (0) ◽  
pp. 060928131519006
Author(s):  
Ellen P. Brennan ◽  
Janet Reing ◽  
Douglas Chew ◽  
Julie M. Myers-Irvin ◽  
E.J. Young ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Antibacterial Activity ◽  
Degradation Products ◽  
Biological Scaffolds

scholarly journals Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression.

1989 ◽  
Vol 109 (2) ◽  
pp. 877-889 ◽  
Author(s):  
Z Werb ◽  
P M Tremble ◽  
O Behrendtsen ◽  
E Crowley ◽  
C H Damsky
Keyword(s):  
Gene Expression ◽  
Extracellular Matrix ◽  
Monoclonal Antibodies ◽  
Cell Shape ◽  
Degradation Products ◽  
Direct Consequence ◽  
Synovial Fibroblasts ◽  
Fibronectin Receptor ◽  
Expression Of Genes ◽  
Initial Adhesion

We have investigated the effects of ligation of the fibronectin receptor (FnR) on gene expression in rabbit synovial fibroblasts. Monoclonal antibodies to the FnR that block initial adhesion of fibroblasts to fibronectin induced the expression of genes encoding the secreted extracellular matrix-degrading metalloproteinases collagenase and stromelysin. That induction was a direct consequence of interaction with the FnR was shown by the accumulation of mRNA for stromelysin and collagenase. Monoclonal antibodies to several other membrane glycoprotein receptors had no effect on metalloproteinase gene expression. Less than 2 h of treatment of the fibroblasts with anti-FnR in solution was sufficient to trigger the change in gene expression, and induction was blocked by dexamethasone. Unlike other inducers of metalloproteinase expression, including phorbol diesters and growth factors, addition of the anti-FnR in solution to cells adherent to serum-derived adhesion proteins or collagen produced no detectable change in cell shape or actin microfilament organization. Inductive effects were potentiated by cross-linking of the ligand. Fab fragments of anti-FnR were ineffective unless cross-linked or immobilized on the substrate. Adhesion of fibroblasts to native fibronectin did not induce metallo-proteinases. However, adhesion to covalently immobilized peptides containing the arg-gly-asp sequence that were derived from fibronectin, varying in size from hexapeptides up to 120 kD, induced collagenase and stromelysin gene expression. This suggests that degradation products of fibronectin are the natural inductive ligands for the FnR. These data demonstrate that signals leading to changes in gene expression are transduced by the FnR, a member of the integrin family of extracellular matrix receptors. The signaling of changes in gene expression by the FnR is distinct from signaling involving cell shape and actin cytoarchitecture. At least two distinct signals are generated: the binding of fibronectin-derived fragments and adhesion-blocking antibodies to the FnR triggers events different from those triggered by binding of the native fibronectin ligand. Because the genes regulated by this integrin are for enzymes that degrade the extracellular matrix, these results suggest that information transduced by the binding of various ligands to integrins may orchestrate the expression of genes regulating cell behavior in the extracellular environment.

scholarly journals A rapid quantitative assay for the detection of mammalian heparanase activity

1997 ◽  
Vol 325 (1) ◽  
pp. 229-237 ◽  
Author(s):  
Craig FREEMAN ◽  
Christopher R. PARISH
Keyword(s):  
Extracellular Matrix ◽  
Cell Lines ◽  
Degradation Products ◽  
Human Cancer ◽  
Umbilical Vein ◽  
Heparan Sulphate ◽  
Metastatic Potential ◽  
Mammary Adenocarcinoma ◽  
Quantitative Assay

Heparan sulphate (HS) is an important component of the extracellular matrix and the vasculature basal laminar which functions as a barrier to the extravasation of metastatic and inflammatory cells. Cleavage of HS by endoglycosidase or heparanase activity produced by invading cells may assist in the disassembly of the extracellular matrix and basal laminar, and thereby facilitate cell migration. Heparanase activity has previously been shown to be related to the metastatic potential of murine and human melanoma cell lines [Nakajima, Irimura and Nicolson (1988) J. Cell. Biochem. 36, 157–167]. To determine heparanase activity, porcine mucosal HS was partially de-N-acetylated and re-N-acetylated with [3H]acetic anhydride to yield a radiolabelled substrate. This procedure prevented the masking of, or possible formation of, new heparanase-sensitive cleavage sites as has been observed with previous methods of radiolabelling. Heparanase activity in a variety of tissues and cell homogenates including human platelets, colonic carcinoma cells, umbilical vein endothelial cells and rat mammary adenocarcinoma cells (both metastatic and non-metastatic variants) and liver homogenates all degraded the substrate in a stepwise fashion from 18.5 to approximately 13, 8 and finally to 4.5 kDa fragments, as assessed by gel-filtration analysis, confirming the substrate as suitable for the detection of heparanase activity present in a variety of cells and tissues. A rapid quantitative assay was developed with the HS substrate using a novel method for separating degradation products from the substrate by taking advantage of the decreased affinity of the heparanase-cleaved products for the HS-binding plasma protein chicken histidine-rich glycoprotein (cHRG). Incubation mixtures were applied to cHRG–Sepharose columns, with unbound material corresponding to heparanase-degradation products. Heparanase activity was determined for a variety of human, rat and murine cell and tissue homogenates. The highly metastatic rat mammary adenocarcinoma and murine lung carcinoma cell lines had four to ten times the heparanase activity of non-metastatic variants, confirming the correlation of heparanase activity with metastatic potential. Human cancer patients had twice the serum heparanase levels of normal healthy adults. The assay will be valuable for the determination of heparanase activity from a variety of tissue and cell sources, as a diagnostic tool for the determination of heparanase potential, and for the development of specific inhibitors of heparanase activity and metastasis.

scholarly journals Chemoattractant activity of degradation products of fetal and adult skin extracellular matrix for keratinocyte progenitor cells

2008 ◽  
Vol 2 (8) ◽  
pp. 491-498 ◽  
Author(s):  
Ellen P. Brennan ◽  
Xiao-Han Tang ◽  
Ann M. Stewart-Akers ◽  
Lorraine J. Gudas ◽  
Stephen F. Badylak
Keyword(s):  
Extracellular Matrix ◽  
Progenitor Cells ◽  
Degradation Products ◽  
Adult Skin

scholarly journals Degradation products of extracellular matrix bioscaffolds derived from diverse source tissues differentially influence macrophage phenotype

2016 ◽  
Vol 4 ◽  
Author(s):  
Dziki Jenna ◽  
Wang Derek ◽  
Pineda Catalina ◽  
Sicari Brian ◽  
Badylak Stephen
Keyword(s):  
Extracellular Matrix ◽  
Degradation Products ◽  
Macrophage Phenotype ◽  
Diverse Source

scholarly journals How does the Extracellular Matrix Change in the Setting of Heart Failure?

2018 ◽  
Vol 6 (3) ◽  
pp. 102-109
Author(s):  
Amerikos Argyriou
Keyword(s):  
Heart Failure ◽  
Extracellular Matrix ◽  
Degradation Products ◽  
Internal Communication ◽  
Matrix Proteins ◽  
Reduced Ejection Fraction ◽  
Functional Changes ◽  
Metalloproteinase Inhibitors

The Extracellular Matrix is a dynamic entity, showing constant degradation and deposition while providing the framework for the cardiomyocytes and interstitial proteins to lie on. Its function is important for the proper myocyte alignment within the heart and for internal communication from cell to matrix. Dysregulation of the remodeling process resulting in the breakdown of collagen by matrix metalloproteinases is a hallmark of heart failure pathophysiology and produces functional changes encompassing all matrix proteins. Several etiologies with distinct mechanisms ultimately bring about signs of heart exhaustion such as reduced ejection fraction, reduced compliance and ventricular dilatation. Discussed in this paper is the role of inflammation, collagen cross-linking and of myofibroblasts in matrix dysfunction and the mechanisms with which these changes occur in heart failure. Understanding extracellular protein roles within this context would allow for specific drug targeting and thus prevention of heart failure in the early stages of the disease. More studies must be conducted to discover the specific matrix proteins and cytokines that modulate the pathological remodeling process. Serum biomarkers of extracellular degradation products, selective metalloproteinase inhibitors and a personalized treatment approach with a revisal of the current classification of heart failure are topics requiring further exploration.

Degradation Products of Extracellular Matrix Affect Cell Migration and Proliferation

2009 ◽  
Vol 15 (3) ◽  
pp. 605-614 ◽  
Author(s):  
Janet E. Reing ◽  
Li Zhang ◽  
Julie Myers-Irvin ◽  
Kevin E. Cordero ◽  
Donald O. Freytes ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Migration ◽  
Degradation Products ◽  
Cell Migration And Proliferation

scholarly journals Antibacterial Activity within Degradation Products of Biological Scaffolds Composed of Extracellular Matrix

2006 ◽  
Vol 12 (10) ◽  
pp. 2949-2955 ◽  
Author(s):  
Ellen P. Brennan ◽  
Janet Reing ◽  
Douglas Chew ◽  
Julie M. Myers-Irvin ◽  
E.J. Young ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Antibacterial Activity ◽  
Degradation Products ◽  
Biological Scaffolds
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