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.

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.

Facilitating In Vivo Articular Cartilage Repair by Tissue-Engineered Cartilage Grafts Produced From Auricular Chondrocytes

2017 ◽  
Vol 46 (3) ◽  
pp. 713-727 ◽  
Author(s):  
Chin-Chean Wong ◽  
Chih-Hwa Chen ◽  
Li-Hsuan Chiu ◽  
Yang-Hwei Tsuang ◽  
Meng-Yi Bai ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Articular Cartilage ◽  
Cartilage Repair ◽  
Articular Chondrocytes ◽  
Type Ii Collagen ◽  
Type Ii ◽  
Articular Cartilage Repair ◽  
3 Dimensional ◽  
Cell Conversion

Background: Insufficient cell numbers still present a challenge for articular cartilage repair. Converting heterotopic auricular chondrocytes by extracellular matrix may be the solution. Hypothesis: Specific extracellular matrix may convert the phenotype of auricular chondrocytes toward articular cartilage for repair. Study Design: Controlled laboratory study. Methods: For in vitro study, rabbit auricular chondrocytes were cultured in monolayer for several passages until reaching status of dedifferentiation. Later, they were transferred to chondrogenic type II collagen (Col II)–coated plates for further cell conversion. Articular chondrogenic profiles, such as glycosaminoglycan deposition, articular chondrogenic gene, and protein expression, were evaluated after 14-day cultivation. Furthermore, 3-dimensional constructs were fabricated using Col II hydrogel-associated auricular chondrocytes, and their histological and biomechanical properties were analyzed. For in vivo study, focal osteochondral defects were created in the rabbit knee joints, and auricular Col II constructs were implanted for repair. Results: The auricular chondrocytes converted by a 2-step protocol expressed specific profiles of chondrogenic molecules associated with articular chondrocytes. The histological and biomechanical features of converted auricular chondrocytes became similar to those of articular chondrocytes when cultivated with Col II 3-dimensional scaffolds. In an in vivo animal model of osteochondral defects, the treated group (auricular Col II) showed better cartilage repair than did the control groups (sham, auricular cells, and Col II). Histological analyses revealed that cartilage repair was achieved in the treated groups with abundant type II collagen and glycosaminoglycans syntheses rather than elastin expression. Conclusion: The study confirmed the feasibility of applying heterotopic chondrocytes for cartilage repair via extracellular matrix–induced cell conversion. Clinical Relevance: This study proposes a feasible methodology to convert heterotopic auricular chondrocytes for articular cartilage repair, which may serve as potential alternative sources for cartilage repair.

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 T1ρ and T2 mapping reveal the in vivo extracellular matrix of articular cartilage

2011 ◽  
Vol 35 (1) ◽  
pp. 147-155 ◽  
Author(s):  
Hiroaki Nishioka ◽  
Jun Hirose ◽  
Eiichi Nakamura ◽  
Yasunari Oniki ◽  
Koji Takada ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Articular Cartilage ◽  
T2 Mapping

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 Synthesis of cartilage matrix by mammalian chondrocytes in vitro. I. Isolation, culture characteristics, and morphology.

1982 ◽  
Vol 93 (3) ◽  
pp. 743-750 ◽  
Author(s):  
K E Kuettner ◽  
B U Pauli ◽  
G Gall ◽  
V A Memoli ◽  
R K Schenk
Keyword(s):  
Articular Cartilage ◽  
Articular Chondrocytes ◽  
Ruthenium Red ◽  
Bovine Articular Cartilage ◽  
Culture Characteristics ◽  
Bovine Articular Chondrocytes ◽  
Fetal Bovine ◽  
Roller Bottles

We describe the isolation and the ultrastructural characteristics of adult bovine articular chondrocytes in vitro. Slices of bovine articular cartilage undergo sequential digestions with pronase and collagenase in order to release cells. Chondrocytes are plated at high density (1 x 10(5) cells/cm2) in culture dishes or roller bottles with Ham's F-12 medium, supplemented with 10% fetal bovine serum. Before culture, chondrocytes are freed of surrounding territorial matrix. Within the first few days of culture they re-establish a territorial matrix. As time progresses, chondrocytes synthesize both territorial and extraterritorial matrices. The matrices are rich in collagen fibrils and ruthenium red-positive proteoglycans. These features are most apparent in mass roller cultures in which aggregates of cells and matrix appear as long streaks and nodules. This morphology reveals an organization of chondrocytes and their matrices that is similar to that of the parent articular cartilage in vivo.

The compressive strength of articular cartilage

1998 ◽  
Vol 212 (4) ◽  
pp. 273-280 ◽  
Author(s):  
A J Kerin ◽  
M R Wisnom ◽  
M A Adams
Keyword(s):  
Mechanical Properties ◽  
Compressive Strength ◽  
Articular Cartilage ◽  
Testing Machine ◽  
Mechanical Damage ◽  
Materials Testing ◽  
Bovine Articular Cartilage ◽  
Creep Loading ◽  
Force Displacement

Articular cartilage provides the smooth bearing surfaces in freely moving (synovial) joints. Its mechanical properties are important because structural failure of cartilage is closely associated with joint disorders, including osteoarthritis. Some mechanical properties of cartilage are well characterized, but little is known about its compressive strength. A technique for measuring cartilage compressive strength is evaluated, and an overview of experiments which relate strength to stiffness and tissue hydration is given. Specimens of bovine articular cartilage-on-bone, approximately 15 mm square, were loaded on a hydraulic materials testing machine using flat impermeable indentors. Linear-ramp loading/unloading cycles of 1 s duration, and of increasing severity, were applied until failure was evident on force-displacement graphs. Some specimens were tested following a 30 min period of creep loading. Inkstaining and histology were used to locate the site of initial damage to each specimen. Specimen failure occurred first in the cartilage surface layer at a nominal applied stress of 14–59 MPa (mean 35.7 MPa). Mechanical properties were little affected by specimen or indentor size, provided both remained within defined limits, and compressive strength could be measured to an accuracy of approximately ±5 per cent. Compressive stiffness was a significant predictor of strength, but only if it was measured at high levels of stress. Strength increased following creep-induced water loss, and initial mechanical damage could propagate under moderate cyclic loading. This technique for measuring cartilage compressive strength has potential for investigating the causes of cartilage failure in vivo

The Frictional Coefficient of Bovine Articular Cartilage Correlates With Interstitial Fluid Load Support in Creep

2002 ◽  
Author(s):  
Ramaswamy Krishnan ◽  
Gerard A. Ateshian
Keyword(s):  
Articular Cartilage ◽  
Friction And Wear ◽  
Interstitial Fluid ◽  
Load Transfer ◽  
Frictional Coefficient ◽  
Fluid Phase ◽  
Constant Load ◽  
Low Friction ◽  
Bovine Articular Cartilage ◽  
Fluid Load

Articular cartilage functions as the bearing material in joints and provides low friction and wear over a lifetime. The cartilage lubrication mechanism has not yet been fully characterized though several theories have been proposed. In previous studies [1–3] it was hypothesized that interstitial fluid load support contributes significantly to the reduction of the frictional coefficient due to load transfer from the solid to the fluid phase of the tissue. This study provides experimental verification for a theoretical model based on this hypothesis [1,4]. The specific aim of this study is to experimentally investigate the correlation between the frictional response of bovine articular cartilage, and its interstitial fluid load support during sliding against glass under a constant load.

scholarly journals Mature bovine articular cartilage contains abundant aggrecan that is C-terminally truncated at Ala719-Ala720, a site which is readily cleaved by m-calpain

2004 ◽  
Vol 382 (1) ◽  
pp. 253-259 ◽  
Author(s):  
Hidefumi OSHITA ◽  
John D. SANDY ◽  
Kiichi SUZUKI ◽  
Atsushi AKAIKE ◽  
Yun BAI ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Articular Cartilage ◽  
Chondroitin Sulphate ◽  
Globular Domain ◽  
Cleavage Sites ◽  
Keratan Sulphate ◽  
Bovine Articular Cartilage ◽  
The Matrix ◽  
A Site

Extracts of normal mature articular cartilage contain aggrecan molecules which bear the G1 domain (the N-terminal globular domain of aggrecan) and are C-terminally truncated by proteolysis at a number of sites. A proportion of these molecules are generated by an aggrecanase and/or matrix-metalloproteinase-mediated cleavage in the IGD (interglobular domain between the G1 and G2 domains of aggrecan). However, the proteinase(s) responsible for formation of the majority of the larger G1-G2 and glycosaminoglycan-bearing truncated species is (are) unknown. N-terminal sequencing of aggrecan core fragments generated by m-calpain digestion of bovine aggrecan has identified four novel cleavage sites: one within the CS (chondroitin sulphate)-1 domain (at one or more of the bonds Ser1229–Val1230, Ser1249–Val1250, Ser1287–Val1288, Gly1307–Val1308 and Ser1346–Val1347), two within the IGD (at bonds Ala474–Ala475 and Gly365–Gly366) and one within the KS (keratan sulphate) domain (at Ala719–Ala720). A new monoclonal antibody (SK-28) to the C-terminal neoepitope at M710VTQVGPGVA719 showed that aggrecan products generated by this cleavage are present in high abundance in mature bovine articular cartilage extracts. We conclude that m-calpain, or an unidentified proteinase with the capacity to cleave at the same site, is active during aggrecan biosynthesis/secretion by mature chondrocytes or in the matrix of mature bovine articular cartilage in vivo.

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