scholarly journals The chemical composition of bovine vitreous-humour collagen fibres

1980 ◽  
Vol 185 (3) ◽  
pp. 545-554 ◽  
Author(s):  
D A Swann ◽  
S S Sotman
Keyword(s):  
Articular Cartilage ◽  
Chemical Composition ◽  
Distinct Type ◽  
Type Ii Collagen ◽  
Vitreous Humour ◽  
Gel Chromatography ◽  
Type Ii ◽  
Glucose Content ◽  
Chain Component ◽  
Alpha Chain

The insoluble protein fraction was prepared from the central and posterior peripheral fraction of bovine vitreous humour. The collagen present in this fraction was solubilized by pepsin and fractionated by gel chromatography. Analysis of the solubilized collagen fractions showed that the alpha-chain component had an amino acid composition and yielded a series of CNBr-cleavage peptides that showed it was very similar to type II collagen obtained from articular cartilage. Bovine vitreous-humour collagen alpha-chains differed, however, from those of cartilage collagen in that they had a lower alanine content and differed in their susceptibility to cleavage by CNBr. Satisfactory cleavage was obtained after two CNBr treatments involving reduction and alkylation. In addition, significant quantities of other peptides constituents were present in the vitreous-humour collagen fractions, and the galactose and glucose content of the alpha-chain fraction was more than double that of the same fraction obtained from articular cartilage. Although the origin of the additional peptide constituents in the vitreous-humour collagen preparations is not known, the results obtained indicate that they are probably not derived from a distinct type of alpha-chain component but may be terminal peptides covalently linked to the alpha 1 type-II helical portions of the collagen. The differences in the chemical composition of the vitreous-humour collagen indicate that vitreous-humour fibres are composed of a special type-II collagen.

scholarly journals Boosting the Intra-Articular Efficacy of Low Dose Corticosteroid through a Biopolymeric Matrix: An In Vivo Model of Osteoarthritis

Cells ◽  
2020 ◽  
Vol 9 (7) ◽  
pp. 1571
Author(s):  
Matilde Tschon ◽  
Francesca Salamanna ◽  
Lucia Martini ◽  
Gianluca Giavaresi ◽  
Luca Lorenzini ◽  
...  
Keyword(s):  
Articular Cartilage ◽  
Pain Sensitivity ◽  
Type Ii Collagen ◽  
Male Rats ◽  
In Vivo Model ◽  
Type Ii ◽  
Chemical Induction ◽  
Local Pain ◽  
Gait Parameters

The purpose of this study was to verify the efficacy of a single intra-articular (i.a.) injection of a hyaluronic acid-chitlac (HY-CTL) enriched with two low dosages of triamcinolone acetonide (TA, 2.0 mg/mL and 4.5 mg/mL), in comparison with HY-CTL alone, with a clinical control (TA 40 mg/mL) and with saline solution (NaCl) in an in vivo osteoarthritis (OA) model. Seven days after chemical induction of OA, 80 Sprague Dawley male rats were grouped into five arms (n = 16) and received a single i.a. injection of: 40 mg/mL TA, HY-CTL alone, HY-CTL with 2.0 mg/mL TA (RV2), HY-CTL with 4.5 mg/mL TA (RV4.5) and 0.9% NaCl. Pain sensitivity and Catwalk were performed at baseline and at 7, 14 and 21 days after the i.a. treatments. The histopathology of the joint, meniscus and synovial reaction, type II collagen expression and aggrecan expression were assessed 21 days after treatments. RV4.5 improved the local pain sensitivity in comparison with TA and NaCl. RV4.5 and TA exerted similar beneficial effects in all gait parameters. Histopathological analyses, measured by Osteoarthritis Research Society International (OARSI) and Kumar scores and by immunohistochemistry, evidenced that RV4.5 and TA reduced OA features in the same manner and showed a stronger type II collagen and aggrecan expression; both treatments reduced synovitis, as measured by Krenn score and, at the meniscus level, RV4.5 improved degenerative signs as evaluated by Pauli score. TA or RV4.5 treatments limited the local articular cartilage deterioration in knee OA with an improvement of the physical structure of articular cartilage, gait parameters, the sensitivity to local pain and a reduction of the synovial inflammation.

Finite Element Modeling of Osmotic Swelling in Tissue-Engineered Cartilage

2008 ◽  
Author(s):  
Liming Bian ◽  
Terri Ann N. Kelly ◽  
Eric G. Lima ◽  
Gerard A. Ateshian ◽  
Clark T. Hung
Keyword(s):  
Articular Cartilage ◽  
Potential Role ◽  
Swelling Pressure ◽  
Type Ii Collagen ◽  
Type Ii ◽  
Osmotic Swelling ◽  
Fixed Charges ◽  
Central Regions ◽  
Significant Research ◽  
Engineered Cartilage

Proteoglycans and Type II collagen represent the two major biochemical constituents of articular cartilage. Collagen fibrils in cartilage resist the swelling pressure that arises from the fixed charges of the glycosaminoglycans (GAGs), and together they give rise to the tissue’s unique load bearing properties. As articular cartilage exhibits a poor intrinsic healing capacity, there is significant research in the development of cell-based therapies for cartilage repair. In some of our tissue engineering studies, we have observed a phenomenon where chondrocyte-seeded hydrogel constructs display cracking in their central regions after significant GAG content has been elaborated in culture. A theoretical analysis was performed to gain greater insights into the potential role that the spatial distribution of proteoglycan and collagen may play in this observed response.

scholarly journals The Effects of Proteoglycan and Type II Collagen on T1ρ Relaxation Time of Articular Cartilage

2015 ◽  
Vol 72 (2) ◽  
pp. 108
Author(s):  
Won Seok Choi ◽  
Hye Jin Yoo ◽  
Sung Hwan Hong ◽  
Ja-Young Choi
Keyword(s):  
Relaxation Time ◽  
Articular Cartilage ◽  
Type Ii Collagen ◽  
Type Ii

Theory of the Short Time Mechanical Relaxation in Articular Cartilage

2011 ◽  
Vol 133 (10) ◽  
Author(s):  
J. W. Ruberti ◽  
J. B. Sokoloff
Keyword(s):  
Hyaluronic Acid ◽  
Articular Cartilage ◽  
Chondroitin Sulfate ◽  
Relaxation Times ◽  
Type Ii Collagen ◽  
Mechanical Relaxation ◽  
Side Chains ◽  
Type Ii ◽  
Interface Area ◽  
Short Time

Articular cartilage is comprised of macromolecules, proteoglycans, with (charged) chondroitin sulfate side-chains attached to them. The proteoglycans are attached to longer hyaluronic acid chains, trapped within a network of type II collagen fibrils. As a consequence of their relatively long persistence lengths, the number of persistence lengths along the chondroitin sulfate and proteoglycan chains is relatively small, and consequently, the retraction times for these side chains are also quite short. We argue that, as a consequence of this, they will not significantly inhibit the reptation of the hyaluronic acid chains. Scaling arguments applied to this model allow us to show that the shortest of the mechanical relaxation times of cartilage, that have been determined by Fyhrie and Barone to be due to reptation of the hyaluronic acid polymers, should have a dependence on the load, i.e., force per unit interface area P, carried by the cartilage, proportional to P3/2.

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.

scholarly journals Excessive degradation of type II collagen in articular cartilage in equine osteochondrosis

2002 ◽  
Vol 20 (6) ◽  
pp. 1282-1289 ◽  
Author(s):  
S. Laverty ◽  
S. O'Kouneff ◽  
M. Ionescu ◽  
A. Reiner ◽  
I. Pidoux ◽  
...  
Keyword(s):  
Articular Cartilage ◽  
Type Ii Collagen ◽  
Type Ii ◽  
Equine Osteochondrosis

Type II Collagen Peptide Release from Rabbit Articular Cartilage

1999 ◽  
Vol 878 (1 INHIBITION OF) ◽  
pp. 590-593 ◽  
Author(s):  
B. R. FELICE ◽  
C. O. CHICHESTER ◽  
H.-J. BARRACH
Keyword(s):  
Articular Cartilage ◽  
Type Ii Collagen ◽  
Type Ii ◽  
Collagen Peptide ◽  
Peptide Release ◽  
Rabbit Articular Cartilage
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