scholarly journals Osteogenic protein-1 promotes the synthesis and retention of extracellular matrix within bovine articular cartilage and chondrocyte cultures

2000 ◽  
Vol 8 (2) ◽  
pp. 127-136 ◽  
Author(s):  
Y. Nishida ◽  
C.B. Knudson ◽  
K.E. Kuettner ◽  
W. Knudson
Keyword(s):  
Extracellular Matrix ◽  
Articular Cartilage ◽  
Bovine Articular Cartilage ◽  
Chondrocyte Cultures ◽  
Osteogenic Protein

Effects of interleukin-1β on chondroblast viability and extracellular matrix changes in bovine articular cartilage explants

2003 ◽  
Vol 57 (7) ◽  
pp. 314-319 ◽  
Author(s):  
Giordano Stabellini ◽  
Monica De Mattei ◽  
Carla Calastrini ◽  
Nicoletta Gagliano ◽  
Claudia Moscheni ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Articular Cartilage ◽  
Cartilage Explants ◽  
Interleukin 1Β ◽  
Bovine Articular Cartilage

scholarly journals Release of elastase from monocytes adherent to a fibronectin-gelatin surface

Blood ◽  
1993 ◽  
Vol 81 (1) ◽  
pp. 186-192
Author(s):  
DL Xie ◽  
R Meyers ◽  
GA Homandberg
Keyword(s):  
Extracellular Matrix ◽  
Articular Cartilage ◽  
Fluid Phase ◽  
High Ratio ◽  
Blocking Effect ◽  
Bovine Articular Cartilage ◽  
Amino Terminal ◽  
Tissue Surface

Fibronectin (Fn) is a circulating and extracellular matrix glycoprotein that may serve to facilitate phagocytosis because of its ability to bind many inflammatory ligands and to a monocyte receptor. Fn fragments have been shown in many systems to have augmented properties over those of native Fn. We show in this report that although Fn fragments did not cause elastase release from monocytes in suspension, fragments did cause elastase release from monocytes that were first bound to Fn- gelatin surfaces. An amino-terminal 29-Kd and a 140-Kd integrin-binding fragment were half-maximally active at 100 nmol/L, whereas the Arg-Gly- Asp-Ser integrin-recognition peptide was half-maximally active at 100 mumol/L. Fluid-phase Fn was ineffective yet blocked the activity of the Fn fragments. Complexing of Fn with gelatin or with heparin partially removed the blocking effect of Fn. Similar results were obtained with U- 937 cells. Substitution of the Fn-gelatin surface with bovine articular cartilage also promoted elastase release. Therefore, in conditions in vivo in which monocytes bind to tissue surface, a high ratio of Fn fragments to native Fn may upregulate certain monocyte activities such as protease release.

Depth Dependent Diffusivity Profile in Bovine Articular Cartilage: Comparing Transverse and Axial Diffusivities

2007 ◽  
Author(s):  
Onyi N. Irrechukwu ◽  
Marc E. Levenston
Keyword(s):  
Extracellular Matrix ◽  
Articular Cartilage ◽  
Articular Surface ◽  
Deep Zone ◽  
Superficial Zone ◽  
Transport Pathway ◽  
Bovine Articular Cartilage ◽  
Extracellular Matrix Components ◽  
Matrix Components ◽  
Oriented Parallel

As articular cartilage is avascular, diffusion at a tissue length scale is the primary mode of solute and nutrient transport to its cells. The major extracellular matrix components are water (70–80%), chondrocytes, collagen (10–20%) and proteoglycans (5–10%) bearing sulfated glycosaminoglycans (GAG) [1]. Electron microscopy studies have shown that articular cartilage can be regarded as having three separate structural zones — superficial, middle and deep. The proportions of the various matrix components vary from the surface to the deep zone in any given joint and the greatest variations in content occur in the GAG content [2]. In addition the collagen fiber alignment varies, with fibers oriented parallel to the articular surface in the superficial zone, randomly oriented in the middle zone and oriented perpendicular to the surface in the deep zone. To a large extent, it is the spatially inhomogeneous composition of articular cartilage and microstructural orientation of its extracellular matrix components that determines the tortuosity of the transport pathway [3]. We therefore hypothesized that the diffusivity profile of a solute through the cartilage depth is inversely related to the GAG content and that the ratio between the axial and lateral diffusivities within each cartilage zone is related to the degree of anisotropy within the zone.

scholarly journals Release of elastase from monocytes adherent to a fibronectin-gelatin surface

Blood ◽  
1993 ◽  
Vol 81 (1) ◽  
pp. 186-192 ◽  
Author(s):  
DL Xie ◽  
R Meyers ◽  
GA Homandberg
Keyword(s):  
Extracellular Matrix ◽  
Articular Cartilage ◽  
Fluid Phase ◽  
High Ratio ◽  
Blocking Effect ◽  
Bovine Articular Cartilage ◽  
Amino Terminal ◽  
Tissue Surface

Abstract Fibronectin (Fn) is a circulating and extracellular matrix glycoprotein that may serve to facilitate phagocytosis because of its ability to bind many inflammatory ligands and to a monocyte receptor. Fn fragments have been shown in many systems to have augmented properties over those of native Fn. We show in this report that although Fn fragments did not cause elastase release from monocytes in suspension, fragments did cause elastase release from monocytes that were first bound to Fn- gelatin surfaces. An amino-terminal 29-Kd and a 140-Kd integrin-binding fragment were half-maximally active at 100 nmol/L, whereas the Arg-Gly- Asp-Ser integrin-recognition peptide was half-maximally active at 100 mumol/L. Fluid-phase Fn was ineffective yet blocked the activity of the Fn fragments. Complexing of Fn with gelatin or with heparin partially removed the blocking effect of Fn. Similar results were obtained with U- 937 cells. Substitution of the Fn-gelatin surface with bovine articular cartilage also promoted elastase release. Therefore, in conditions in vivo in which monocytes bind to tissue surface, a high ratio of Fn fragments to native Fn may upregulate certain monocyte activities such as protease release.

Tofacitinib and TPCA-1 exert chondroprotective effects on extracellular matrix turnover in bovine articular cartilage ex vivo

2019 ◽  
Vol 165 ◽  
pp. 91-98 ◽  
Author(s):  
Cecilie F. Kjelgaard-Petersen ◽  
Neha Sharma ◽  
Ashref Kayed ◽  
Morten A. Karsdal ◽  
Ali Mobasheri ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Articular Cartilage ◽  
Ex Vivo ◽  
Bovine Articular Cartilage
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