Salivary type I collagen degradation end-products and related matrix metalloproteinases in periodontitis

2012 ◽  
Vol 40 (1) ◽  
pp. 18-25 ◽  
Author(s):  
Ulvi K. Gursoy ◽  
Eija Könönen ◽  
Sisko Huumonen ◽  
Taina Tervahartiala ◽  
Pirkko J. Pussinen ◽  
...  
Keyword(s):  
Matrix Metalloproteinases ◽  
Type I Collagen ◽  
Collagen Degradation ◽  
Type I ◽  
End Products

Zinc Inhibits Collagenolysis by Cathepsin K and Matrix Metalloproteinases in Demineralized Dentin Matrix

2017 ◽  
Vol 51 (6) ◽  
pp. 576-581 ◽  
Author(s):  
Pinar Altinci ◽  
Roda Seseogullari-Dirihan ◽  
Gulsen Can ◽  
David Pashley ◽  
Arzu Tezvergil-Mutluay
Keyword(s):  
Matrix Metalloproteinases ◽  
Mass Loss ◽  
Type I Collagen ◽  
Cathepsin K ◽  
Collagen Degradation ◽  
Type I ◽  
Level Control ◽  
Physiological Level ◽  
Cysteine Cathepsins ◽  
Demineralized Dentin

The enzymatic degradation of dentin organic matrix occurs via both the action of matrix metalloproteinases (MMPs) and cysteine cathepsins (CCs). Zinc can prevent collagen hydrolysis by MMPs. However, its effect on the activity of dentin-bound CCs is not known. The aim of this study was to investigate the effect of zinc on matrix-bound cathepsin K and MMP activity in dentin. Completely demineralized dentin beams were divided into test groups (n = 9) and incubated at 37°C in an incubation media (1 mL) containing ZnCl2 of 0.02 (physiological level, control), 0.2, 0.5, 1, 5, 10, 20, 30, or 40 mM. The dry mass changes of the beams were determined, and incubation media were analyzed for cathepsin K- and MMP-specific collagen degradation end products - CTX (C-terminal cross-linked telopeptide of type I collagen) and ICTP (cross-linked carboxy-terminal telopeptide of type I collagen) - at 1, 3, and 7 days of incubation. The mass loss of the beams decreased when the zinc level in the incubation media was ≥5 mM (p < 0.05). The release of liberated collagen degradation telopeptides decreased in accordance with the decrease in the mass loss rates of the beams. Cathepsin K-induced dentin collagen degradation can be strongly inhibited by zinc. Zinc levels of ≥5 mM can be considered as a reliable threshold for the stabilization of dentin matrices.

1. Type I collagen degradation by murine osteoblasts stimulated with 1,25(OH)2-vitamin D3: evidence for a plasminogen activator—plasmin—metalloproteinase cascade

Bone ◽  
1989 ◽  
Vol 10 (6) ◽  
pp. 471 ◽  
Author(s):  
BM Thomson ◽  
SJ Atkinson ◽  
AM McGarrity ◽  
RM Hembry ◽  
JJ Reynolds ◽  
...  
Keyword(s):  
Plasminogen Activator ◽  
Vitamin D3 ◽  
Type I Collagen ◽  
Collagen Degradation ◽  
Type I

Tissue inhibitor of metalloproteinases (TIMP) regulates extracellular type I collagen degradation by chondrocytes and endothelial cells

1987 ◽  
Vol 87 (2) ◽  
pp. 357-362
Author(s):  
J. Gavrilovic ◽  
R.M. Hembry ◽  
J.J. Reynolds ◽  
G. Murphy
Keyword(s):  
Endothelial Cells ◽  
Type I Collagen ◽  
Model System ◽  
Collagen Degradation ◽  
Type I ◽  
Tissue Inhibitor Of Metalloproteinases ◽  
Regulatory Factor ◽  
Tissue Inhibitor ◽  
Cells Cultured

A specific antiserum to purified rabbit tissue inhibitor of metalloproteinases (TIMP) was raised in sheep, characterized and used to investigate the role of TIMP in a model system. Chondrocytes and endothelial cells cultured on 14C-labelled type I collagen films and stimulated to produce collagenase were unable to degrade the films unless the anti-TIMP antibody was added. The degradation induced was inhibited by a specific anti-rabbit collagenase antibody. It was concluded that TIMP is a major regulatory factor in cell-mediated collagen degradation.

Abstract P383: 3D-collagen Matrix Enhanced Integrins And Matrix Metalloproteinases Expression In Cardiac Mesenchymal Cells

2021 ◽  
Vol 129 (Suppl_1) ◽  
Author(s):  
Senthilkumar Muthusamy ◽  
Asha V Nath ◽  
Shilpa Ajit ◽  
Anil K PR
Keyword(s):  
Matrix Metalloproteinases ◽  
Adhesion Molecules ◽  
Type I Collagen ◽  
Collagen Matrix ◽  
Mesenchymal Cells ◽  
Pcr Analysis ◽  
Type I ◽  
Culture Dish ◽  
Tissue Culture Dish ◽  
3D Collagen

Introduction: Use of cardiac mesenchymal cells (CMCs) has been shown to improve cardiac function following myocardial infarction. Main drawback in cardiac cell therapy is the major loss of injected cells within few hours. Increase the retention of these injected cells could increase their efficacy, where cardiac patches with various cell types showed better outcome. Among, collagen patch plays lead role as a cell-laden matrix in cardiac tissue engineering. Creating a detailed understanding of how collagen matrix changes the cellular phenotype could provide seminal insights to regeneration therapy. Hypothesis: Growing CMCs in three dimensional (3D) collagen matrix could alter the expression of extracellular matrix (ECM) and adhesion molecules, which may enhance their efficacy. Methods: The bovine type I collagen was chemically modified and solubilized in culture medium with photo-initiator. The mouse CMCs were isolated and resuspended in collagen solution, printed using 3D bioprinter and UV-crosslinked to form 3D-CMC construct. The 3D-CMC construct was submerged in growth medium and cultured for 48h and analyzed for the expression of ECM and adhesion molecules (n=5/group). CMCs cultured in regular plastic tissue culture dish was used as control. Results: RT profiler array showed changes in the ECM and adhesion molecules expression, specifically certain integrins and matrix metalloproteinases (MMPs) in CMCs cultured 3D collagen construct compared to 2D monolayer. Subsequent qRT-PCR analysis revealed significant (p<0.01) upregulation of integrins such as Itga2 (2.96±0.13), Itgb1 (3.18±0.2) and Itgb3 (2.4±0.27) and MMPs such as MMP13 (37.2±3.36), MMP9 (5.23±1.06) and MMP3 (7.14±2.07). Western blot analysis further confirmed significant elevation of these integrins and matrix metalloproteinases at protein level. Collagen encapsulation did not alter the expression of N-cadherin in CMCs, which is a potential mesenchymal cadherin adhesion molecule. Conclusion: Integrin αβ heterodimers transduce signals that facilitate cell homing, migration, survival and differentiation. Similarly, MMPs plays vital role in cell migration and proliferation. Our results demonstrate that the 3D-collagen Niche enhances the expression of certain integrins and MMPs in CMCs. This suggest that the efficacy of CMCs could be magnified by providing 3D architecture with collagen matrix and further in vivo experiments would reveal functional benefits from CMCs for clinical use.

scholarly journals Matrix Metalloproteinase Mediated Type I Collagen Degradation — An Independent Risk Factor for Mortality in Women

EBioMedicine ◽  
2015 ◽  
Vol 2 (7) ◽  
pp. 723-729 ◽  
Author(s):  
K. Dragsbæk ◽  
J.S. Neergaard ◽  
H.B. Hansen ◽  
I. Byrjalsen ◽  
P. Alexandersen ◽  
...  
Keyword(s):  
Risk Factor ◽  
Matrix Metalloproteinase ◽  
Independent Risk Factor ◽  
Type I Collagen ◽  
Collagen Degradation ◽  
Type I

Urinary markers of type I collagen degradation in the dog

2000 ◽  
Vol 69 (2) ◽  
pp. 123-127 ◽  
Author(s):  
M.J ALLEN ◽  
L.C.V ALLEN ◽  
W.E HOFFMANN ◽  
D.C RICHARDSON ◽  
G.J BREUR
Keyword(s):  
Type I Collagen ◽  
Collagen Degradation ◽  
Type I ◽  
Urinary Markers
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