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 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

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.

Scaffolds in tissue engineering of blood vessels

2010 ◽  
Vol 88 (9) ◽  
pp. 855-873 ◽  
Author(s):  
Divya Pankajakshan ◽  
Devendra K. Agrawal
Keyword(s):  
Tissue Engineering ◽  
Extracellular Matrix ◽  
Blood Vessels ◽  
Vascular Tissue ◽  
Small Diameter ◽  
Biological Scaffolds ◽  
Hemodynamic Forces ◽  
Biodegradable Scaffolds

Tissue engineering of small diameter (<5 mm) blood vessels is a promising approach for developing viable alternatives to autologous vascular grafts. It involves in vitro seeding of cells onto a scaffold on which the cells attach, proliferate, and differentiate while secreting the components of extracellular matrix that are required for creating the tissue. The scaffold should provide the initial requisite mechanical strength to withstand in vivo hemodynamic forces until vascular smooth muscle cells and fibroblasts reinforce the extracellular matrix of the vessel wall. Hence, the choice of scaffold is crucial for providing guidance cues to the cells to behave in the required manner to produce tissues and organs of the desired shape and size. Several types of scaffolds have been used for the reconstruction of blood vessels. They can be broadly classified as biological scaffolds, decellularized matrices, and polymeric biodegradable scaffolds. This review focuses on the different types of scaffolds that have been designed, developed, and tested for tissue engineering of blood vessels, including use of stem cells in vascular tissue engineering.

scholarly journals Chemical modification of erythromycins. VI. Structure and antibacterial activity of acid degradation products of 6-O-methylerythromycins A.

1990 ◽  
Vol 43 (5) ◽  
pp. 570-573 ◽  
Author(s):  
SHIGEO MORIMOTO ◽  
YOKO MISAWA ◽  
TOSHIFUMI ASAKA ◽  
HLDEAKI KONDOH ◽  
YOSHIAKI WATANABE
Keyword(s):  
Antibacterial Activity ◽  
Chemical Modification ◽  
Degradation Products ◽  
Acid Degradation

scholarly journals Comparison of two methods for prolong storage of decellularized mouse whole testis for tissue engineering application: An experimental study

2021 ◽  
Author(s):  
Nasrin Majidi Gharenaz ◽  
Mansoureh Movahedin ◽  
Zohreh Mazaheri
Keyword(s):  
Tissue Engineering ◽  
Experimental Study ◽  
Extracellular Matrix ◽  
Mouse Embryonic Fibroblast ◽  
Slow Freezing ◽  
Histological Evaluation ◽  
Biological Scaffolds ◽  
Extracellular Matrix Components ◽  
Matrix Components ◽  
Embryonic Fibroblast

Background: Biological scaffolds are derived by the decellularization of tissues or organs. Various biological scaffolds, such as scaffolds for the liver, lung, esophagus, dermis, and human testicles, have been produced. Their application in tissue engineering has created the need for cryopreservation processes to store these scaffolds. Objective: The aim was to compare the two methods for prolong storage testicular scaffolds. Materials and Methods: In this experimental study, 20 male NMRI mice (8 wk) were sacrificed and their testes were removed and treated with 0.5% sodium dodecyl sulfate followed by Triton X-100 0.5%. The efficiency of decellularization was determined by histology and DNA quantification. Testicular scaffolds were stored in phosphate-buffered saline solution at 4ºC or cryopreserved by programmed slow freezing followed by storage in liquid nitrogen. Masson’s trichrome staining, Alcian blue staining and immunohistochemistry, collagen assay, and glycosaminoglycan assay were done prior to and after six months of storage under each condition. Results: Hematoxylin-eosin staining showed no remnant cells after the completion of decellularization. DNA content analysis indicated that approximately 98% of the DNA was removed from the tissue (p = 0.02). Histological evaluation confirmed the preservation of extracellular matrix components in the fresh and frozen-thawed scaffolds. Extracellular matrix components were decreased by 4ºC-stored scaffolds. Cytotoxicity tests with mouse embryonic fibroblast showed that the scaffolds were biocompatible and did not have a harmful effect on the proliferation of mouse embryonic fibroblast cells. Conclusion: Our results demonstrated the superiority of the slow freezing method for prolong storage of testicular scaffolds. Key words: Cryopreservation, Testis, Scaffold, Mouse. 

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 Stability and Antibacterial Activity of Cefepime during Continuous Infusion

2003 ◽  
Vol 47 (6) ◽  
pp. 1991-1994 ◽  
Author(s):  
Pål F. Sprauten ◽  
Paul M. Beringer ◽  
Stan G. Louie ◽  
Timothy W. Synold ◽  
Mark A. Gill
Keyword(s):  
Antibacterial Activity ◽  
Continuous Infusion ◽  
Susceptibility Testing ◽  
Degradation Products ◽  
Infusion Pump ◽  
The Stability ◽  
Over Time

ABSTRACT The stability of cefepime during simulated continuous infusion was determined with a motorized portable infusion pump worn over a period of 24 to 36 h. Susceptibility testing on cefepime solutions over time indicates that the degradation products do not exhibit antibacterial activity. Cefepime stability at 24 h following continuous infusion was 94.3% ± 1.0%, which supports the use of continuous infusion.

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