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PubMed1983

[Closure of joint cartilage defects using cartilage fragments and fibrin glue].

In the knee joints of adult rabbits osteochondral defects of 4 mm in diameter were placed by a drill reaching the cancellous bone. In the first group the defects were left untreated or closed by collagen foam or by fibrin adhesive or a combination of both. In the second group the defects were closed with very small autologous cartilage fragments and fibrin adhesive. The animals were observed over up to 40 weeks. In the first group no hyaline cartilage was found histologically in any of the defects. In the second group a rapid proliferation of chondrocytes appeared with development of hyaline cartilage with alcian-blue-positive matrix. It resembled juvenile cartilage in its histologic appearance and with regard to the induction of ossification. This phenomenon is interpreted as a "second adolescence" of the adult cartilage induced by the rich nutritional and oxygen supply from the cancellous vessels, which resembles the environmental conditions before forming of subchondral cortical bone at the end of the growth period. This method enabled us to achieve a complete closure of defects by hyaline cartilage on the very level of the surrounding articular surface.

Animals↗
PubMedDate not supplied

[Use of the alar cartilage in repairing of defects of the cartilage part of the dorsum nasi].

The authors present long-term results of using costal and alar allo-cartilages for repairing defects of the cartilage part of nasal ridge. Transplantation of the costal allo-cartilage to 362 patients entailed cartilage deformations in 50, inflammation in 34 and resolution of the cartilage in 26 patients. Transplantation of alar cartilage brought resolution and deformation in 10 and 7 cases of 276 transplantations, respectively, in the absence of inflammation. Moreover, the latter material provides better cosmetic results.

Cartilage↗
PubMedDate not supplied

Abnormalities in secondary cartilages in four lines of transgenic mice harboring two different types of mutations in the cartilage-specific type II collagen gene.

A histological analysis was performed on two secondary cartilages, the mandibular condyle and the medial end of clavicle, in transgenic mice harboring two different types of mutations in the cartilage-specific type II collagen gene. Considerable differences were observed in the maturation zone of the chondrocytes and the hypertrophic cells of the growth regions of the two secondary cartilages examined between the transgenic mice and their transgene-negative littermates, which served as controls. Looseness of the perichondrium/periosteum was a distinct feature seen in both mutations. However, phenotypic consequences of the mutations in secondary cartilages were less severe than those in primary cartilages. We propose that the differences between primary and secondary cartilages are due to differences in their origin, mode of growth, architecture and behavior under extrinsic factors.

Amino Acid Sequence↗
PubMed1994

Alteration of cartilage specific proteoglycan with non-weight bearing articular cartilage.

The cartilage composed of chondrocytes and their surrounding extracellular matrix, and mechanical motion of joint may influence on the metabolism of cartilage. In order to determine whether non-weight bearing status alter the metabolism of cartilage, we made histological and biochemical analysis with incorporation of 35S and the distribution of the molecular size of proteoglycans produced in the case of disused cartilage. Histologically, there were seen no disorder in cell arrangement, but poorer in cellularity and thinner in cartilage width as compared with normal one. Biochemical analysis, however demonstrate that incorporation of 35S in newly synthesized glycosaminoglycan (GAG) was lower and the molecular size also smaller than that of control suggesting that mechanical stress is an important environmental factor in maintaining the differential function of the cartilage.

Cartilage, Articular↗
PubMed1998

[From chondrocyte culture to joint cartilage replacement. Development of de novo cartilage in vitro].

Local repair of acute or chronic cartilage lesions has not been successful so far. An attempt has been made to use synthetic materials to improve the quality of the repair tissue, but no method has achieved reliable regrowth of normal hyaline cartilage with adequate biomechanical properties and bonding to surrounding tissue. After publication of the first short-term results of chondrocyte transplantation in patients with localized cartilage lesions of the knee joints by a Swedish group in 1994 [1], the situation seems to have changed. Even though the advantages of this method of chondrocyte transplantation is a matter of controversy, the interest in the so-called "Carticel" approach has grown steadily. Indeed, the technique was recently approved by the FDA, on condition of a randomized, "placebo"-controlled trial. In view of this rapid development, we feel that independent experimental studies are urgently needed. In this article we present our own results in synthesizing de novo cartilage from cultured and phenotypically stable chondrocytes in a truly three-dimensional cartilage-like polyanionic matrix. With the experience gained in animals, we expect to set the stage for future experimental therapy in young human patients with early cartilage lesions.

Animals↗
PubMed2005

Functional significance of arytenoid adduction with the suture attaching to cricoid cartilage versus to thyroid cartilage for unilateral paralytic dysphonia.

OBJECTIVE: In the treatment of unilateral paralytic dysphonia, traditional arytenoid adduction is designed to place suture through the muscular process of the arytenoid attaching anteriorly to the thyroid ala. In contrast with the suture direction of this technique, a new paramedian approach to arytenoid adduction anchors anteroinferiorly to the cricoid cartilage, mimicking the force action of the lateral cricoarytenoid muscle (the major adductor of the larynx). This study investigated the influence of these changes in suture direction on the vocal fold level as well as the vocal outcomes in these two techniques of arytenoid adduction. STUDY DESIGN: A prospective clinical series. METHODS: Thirty patients with unilateral paralytic dysphonia underwent medialization laryngoplasty with arytenoid adduction and strap muscle transposition. Under local anesthesia, the thyroid lamina on the involved side was paramedially separated. The inner perichondrium was carefully elevated away from the overlying thyroid cartilage, carrying the dissection posteriorly to the level of the superior and inferior cornua. The lamina was retracted laterally, the inner perichondrium was opened near the midpoint, and the lateral cricoarytenoid muscle identified. Tracing the muscle fibers posterosuperiorly, the muscular process of the arytenoid was identified. A 2-0 Prolene suture was placed through the muscular process and temporarily tied to the anterolateral aspect of the thyroid ala (AA-thyroid suture). Intraoperative acoustic and perceptual assessments were performed. After releasing the tie, the suture was anchored to the cricoid cartilage at the origin of the lateral cricoarytenoid muscle (AA-cricoid suture). Voice assessments were repeated, and the outcomes of the two tests were compared. The choice of the type of arytenoid adduction suture was made intraoperatively according to which condition provided better vocal performance. After securing the suture, a bipedicled strap muscle flap was transposed into the space between the lamina and inner perichondrium and the thyroid cartilages sutured back into place. RESULTS: The intraoperative acoustic and perceptual assessments revealed the vocal performance was significantly better with AA-cricoid suture than the AA-thyroid suture in this series. No major complications occurred in the study. CONCLUSION: This study suggests that arytenoid adduction with suture attachment along the longitudinal axis of the lateral cricoarytenoid muscle to the cricoid cartilage is more physiologic and effective than that attaching the suture to the thyroid ala. A paramedian approach to arytenoid adduction with or without strap muscle transposition is a safe and effective method for treatment of unilateral paralytic dysphonia.

Adult↗
PubMed1996

[Histological study of cartilage channels in the epiphyseal cartilage of young dogs and their relationship to that of osteochondrosis dissecans in the most frequently affected locations].

Osteochondrosis is a disease occurring in many species of domestic animals. There are different factors like genetic predisposition, housing and feeding, trauma and stress, which are thought to be the causes or part of the causes of the disease. There have been studies about swine, finding a connection between cartilage channels in juvenile epiphyseal cartilage and the development of osteochondrosis. The aim of the study was to find out whether those connections exist in dogs as well. Special interest has been laid upon the localisation, the contents and the surroundings of cartilage channels as well as their relationship to the localisation of osteochondrosis. Joint surfaces, that are most often subject to osteochondrosis in the dog, have been examined macroscopically and histologically, e.g. the caput humeri, the medial part of the humeral condyle, the lateral condyle of the os femoris, the cochlea tibiae and the trochlea tali of 31 dogs at the age of three days to nine months. According to this examination cartilage channels can disturb the process of ossification of cartilage in the secondary centre of ossification, causing a thickening of cartilage layers. These changes can often be seen in locations, where osteochondrosis usually develops, especially in the caput humeri. Altogether they could be located more often in male animals and large breeds than in female animals and small breeds. To a certain degree these changes can be considered as normal in the development and growth of a young dog, but combined with other factors like trauma or stress, they may play a favoring role in the pathogenesis of osteochondrosis as well.

Animals↗
PubMed1999

Changes in serum cartilage marker levels indicate altered cartilage metabolism in families with the osteoarthritis-related type II collagen gene COL2A1 mutation.

OBJECTIVE: The Arg5l9-Cys mutation in type II collagen results in severe, precocious familial osteoarthritis (OA) in 100% of carriers within the first 3 decades of life. The carrier population provided a well-defined patient population for the study of serum markers of familial OA with respect to pathogenesis, diagnosis, and prognosis. METHODS: Serum was obtained from 31 mutation-positive individuals and 16 mutation-negative individuals. OA severity was determined by clinical and radiologic assessments. Levels of serum cartilage oligomeric matrix protein (COMP), keratan sulfate (KS) epitope, the 846 epitope of aggrecan, and the C propeptide of type II collagen (CPII) were measured and were correlated with the radiologic findings. RESULTS: COMP and KS levels, both of which have been suggested to be indicative of disturbed cartilage turnover, were significantly elevated in mutation-positive individuals and in the individuals with OA regardless of mutation status. There was no statistically significant difference between mutation-positive, mutation-negative, OA-positive, and OA-negative individuals with respect to serum concentrations of epitope 846 or CPII, both of which are putative markers of cartilage repair. CONCLUSION: Study of the macromolecular constituents of cartilage released into serum in subjects with familial OA revealed altered metabolism in OA, as demonstrated by elevated COMP and KS levels. Other constituents, the 846 epitope and CPII, were not altered, indicating dissociation of cartilage anabolism and breakdown. Future sequential studies will provide an opportunity to define biochemical changes as familial OA develops and to monitor therapeutic responses.

Adult↗
PubMed1988

Dermatan sulphate proteoglycan from human articular cartilage. Variation in its content with age and its structural comparison with a small chondroitin sulphate proteoglycan from pig laryngeal cartilage.

Low molecular mass proteoglycans (PG) were isolated from human articular cartilage and from pig laryngeal cartilage, which contained protein cores of similar size (Mr 40-44 kDa). However, the PG from human articular cartilage contained dermatan sulphate (DS) chains (50% chondroitinase AC resistant), whereas chains from pig laryngeal PG were longer and contained only chondroitin sulphate (CS). Disaccharide analysis after chondroitinase ABC digestion showed that the human DS-PG contained more 6-sulphated residues (34%) than the pig CS-PG (6%) and both contained fewer 6-sulphated residues than the corresponding high Mr aggregating CS-PGs from these tissues (86% and 20% from human and pig respectively). Cross-reaction of both proteoglycans with antibodies to bovine bone and skin DS-PG-II and human fibroblasts DS-PG suggested that the isolated proteoglycans were the humans DS-PG-II and pigs CS-PG-II homologues of the cloned and sequenced bovine proteoglycan. Polyclonal antibodies raised against the pig CS-PG-II were shown to cross-react with human DS-PG-II. SDS/polyacrylamide-gel analysis and immunoblotting of pig and human cartilage extracts showed that some free core protein was present in the tissues in addition to the intact proteoglycan. The antibodies were used in a competitive radioimmunoassay to determine the content of this low Mr proteoglycan in human cartilage extracts. Analysis of samples from 5-80 year-old humans showed highest content (approximately 4 mg/g wet wt.) in those from 15-25 year-olds and lower content (approximately 1 mg/g wet wt.) in older tissue (greater than 55 years). These changes in content may be related to the deposition and maintenance of the collagen fibre network with which this class of small proteoglycan has been shown to interact.

Age Factors↗
PubMedDate not supplied

[Biomechanical properties of cartilage repair tissue after different cartilage repair procedures in sheep].

AIM: The purpose of this study was to evaluate the biomechanical quality of cartilage and repair tissue in a sheep's knee. 4 standardized 7 mm defects were created on the medial femoral condyle and on the patellar groove (n = 22). These were treated with 4 different cartilage repair procedures and examined 1 year later. MATERIAL AND METHODS: The different groups were: (1) a cell-seeded collagen type-I/III-membrane (Chondro Gide(R)) glued into the defect; (2) a collagen type-I/III-membrane, sutured and cells injected underneath; (3) an engineered, cell-seeded collagen type-II-membrane, glued; (4) periosteum sutured and cells injected underneath; (5) CONTROLS: healthy contra-lateral knees. Indentation tests were performed to reveal the biomechanical capacity. From creep indentation over 35 s a "25-s creep index" was calculated. A high creep index means that the cartilage can undergo greater and faster compression. RESULTS: The repair tissue was significantly thinner than the normal cartilage. The mean creep index of all repair tissues was measured at 111 and 125, respectively (p < 0.05). There were no significant differences among the treated groups. CONCLUSION: In this animal study, none of the induced repair tissues was biomechanically comparable to genuine articular cartilage.

Animals↗
PubMed1980

Effect of cartilage bone marrow extract on the metabolism of collagen in osteoarthrotic cartilage.

The effect of cartilage bone marrow extract (CBME) on the metabolism of collagen and proteoglycan in crude embryo and human cartilage was investigated. While in chick embryos' articular cartilages the increased levels of radioactivity in collagen and proteoglycan were observed, in normal human cartilage only slight changes were detected. In osteoarthrotic cartilages, however, a marked increase in radioactivity was found in collagen and in the proteoglycan fraction containing the glycoprotein link. A blockade of collagenolysis by CBME treatment is suggested.

Animals↗
PubMed2025

Localisation-Dependent Variations in Articular Cartilage ECM: Implications for Tissue Engineering and Cartilage Repair.

Articular cartilage (AC) is a specialised connective tissue covering joint surfaces. It enables smooth movement, distributes mechanical loads, and protects the underlying bone. In response to loading, AC adapts by modifying both its thickness and composition. AC is organised in different zones, with low cellularity and a high abundance of extracellular matrix (ECM). Mechanical overloading or immobilisation can lead to structural changes, potentially resulting in osteoarthritis (OA), for which no causal treatment currently exists. However, smaller defects can be treated using chondrocyte/cartilage transplantation or tissue engineering. A better understanding of the molecular composition of AC at different locations is essential to improve such therapeutic approaches. For this purpose, we performed a comprehensive analysis of porcine femoral knee cartilage at eight defined anatomical sites. Cartilage thickness and proteoglycan (PG) content were analysed histologically, while specific ECM proteins were assessed by proteomics and validated by immunohistochemistry and Western blot. Significant differences were identified, particularly between medial and lateral compartments, in terms of cartilage thickness, PG abundance, and ECM composition. Some proteins also showed zone-specific localisation patterns. These structural differences likely reflect adaptation to mechanical loading and should be considered to optimise future cartilage repair and tissue engineering strategies.

Extracellular Matrix↗
PubMed2004

[Value of autologous chondrocyte transplantation in experimental cartilage defects reconstruction. Part II: Microscopic analysis of reconstructed cartilage structural integrity and surface regularity].

UNLABELLED: Experimental and clinical tests proved that cultured, autologous chondrocytes retain their properties and have ability to reconstruct hyaline-like cartilage, which represents chemical composition and biomechanical characteristics similar to normal hyaline cartilage. The aim of this part of the study was microscopic evaluation of repair tissue structural integrity and surface regularity after autologous chondrocyte transplantation. MATERIAL AND METHODS: Repair of partial thickness cartilage defect (ICRS III(o) grade) on distal femur joint surface was evaluated (25 adolescent rabbits). Procedures were performed in two groups: I--autologous chondrocyte transplantation under periosteal flap, II--periosteal graft. Chondrocytes were isolated from the cartilage specimens by enzymatic digestion and cultured in vitro. The follow-up periods were established at 4, 8, 12 weeks. Repair tissue was evaluated microscopically according to modified O'Driscoll scale. RESULTS: In group I, 4 weeks after the procedure surface of the reconstructed tissue was irregular. 8- and 12-week observation found the surface regular and plain, and repair tissue exhibited complete structural integrity. In group II, in all follow-up periods regenerate surface was irregular, there was many fissures and cracks in graft tissue, and in several cases--regenerate disintegration. CONCLUSION: Obtained results indicate, that hyaline-like cartilage reconstructed after autologous chondrocyte transplantation was characterized by regular, plain surface and complete structural integrity.

Animals↗
PubMed1989

The effects of "matrigenin" activity from bovine bone on the glycosaminoglycans of bovine articular cartilage in culture. A model for cartilage repair by bone derived factors.

A bovine articular cartilage longterm culture system was used to study proteoglycan synthesis by a pulse labeling technique. A brief preincubation of the cartilage slices with bacterial collagenase was found to be an effective method of depleting proteoglycan. The addition of a fraction from bovine bone that contained partially purified "matrigenin" activity to the cultures resulted in the stimulation of incorporation of radioactive precursors into cartilage chondroitin sulfate, suggesting increased proteoglycan synthesis. The stimulatory effect of matrigenin activity was observed earlier and was more sustained if the cartilage slices were preincubated with collagenase. The system appears to be useful for testing the hypothesis that bone derived factors stimulate the repair of damaged cartilage.

Animals↗
PubMed2000

Elastic registration of 3D cartilage surfaces from MR image data for detecting local changes in cartilage thickness.

The objective of this work was to develop and validate a computational method for the registration (matching) of 3D cartilage plates from MR image data sets. The technique tracks local cartilage thickness changes over time. A 3D elastic registration technique was applied that identifies corresponding points of the bone-cartilage interface in MR data sets of 3D-reconstructed cartilage plates. In a first rigid preregistration step, the surfaces are aligned, using the principal axes decomposition to correct for different joint positions and orientations in the MR scanner. In a second step, the surfaces are deformed elastically, based on geometric surface features, until they are sufficiently similar to identify corresponding surface points. The method was validated against artificially corrupted cartilage surfaces and MR data obtained from in vivo and in vitro compression experiments. The in vivo reproducibility was tested on patellar data sets of volunteers, with repositioning of the joint in between replicate acquisitions.

Cartilage, Articular↗
PubMedDate not supplied

Aggregation of cartilage proteoglycans. II Evidence for the presence of a hyaluronate-binding region on proteoglycans from osteoarthritic cartilage.

Proteoglycan aggregates isolated from normal bovine knee cartilage were larger than those from osteoarthritic cartilage of the same joints and appeared relatively more resistant to digestion with leech hyaluronidase. Incubation of proteoglycan subunits from the arthritic cartilage with hyaluronic acid resulted in marked aggregation, comparable in magnitude to that shown by subunits from normal cartilage. The results indicate that the hyaluronate-binding region of these proteoglycans was functionally intact and suggest that diminished aggregation of proteoglycans in osteoarthritic cartilage may be due to an abnormality in some other constituent of the aggregates.

Animals↗
PubMed1979

Articular cartilage preservation and storage. I. Application of tissue culture techniques to the storage of viable articular cartilage.

Articular cartilage slice explants were stored under various conditions, including freezing-thawing at various rates by using dimethyl sulfoxide (DMSO) as a cryoprotective agent, incubating in standard tissue culture medium (MEM Eagle:NCTC 135:15% fetal calf serum) in 5% CO2 and air at 4 degrees, 21 degrees, and 37 degrees C, and incubating in standard tissue culture medium containing 200 micrograms/ml alpha-tocopherol (vitamin E) at 37 degrees C after first ascertaining a dose-response curve of vitamin E. Results indicated that articular cartilage slice explants did not survive freezing or storage at 4 degrees and 21 degrees C as measured by 35S uptake. When stored at 37 degrees C in standard tissue culture in 5% CO2 and air, the slice explants remained viable for up to 60 days. The addition of alpha-tocopherol to the medium resulted in significantly less release of previously incorporated 35Sin stored cartilage slices and significantly less reduction of the amount of hexosamine present in the stored explants. alpha-Tocopherol in the medium also preserved safranin O staining. Thus, the application of tissue culture techniques to the storage of articular cartilage made it possible to preserve cartilage slice explants in a viable, biochemically "normal" state.

Animals↗
PubMed2006

Oncostatin M induces angiogenesis and cartilage degradation in rheumatoid arthritis synovial tissue and human cartilage cocultures.

OBJECTIVE: To investigate the role of oncostatin M (OSM) in cell adhesion, angiogenesis, and matrix degradation in rheumatoid arthritis (RA) synovial tissue and normal human cartilage. METHODS: Human dermal microvascular endothelial cell (HDMEC) and RA synovial fibroblast (RASF) proliferation and intercellular adhesion molecule 1 (ICAM-1) and vascular cell adhesion molecule 1 (VCAM-1) expression were assessed by a bromodeoxyuridine proliferation assay and flow cytometry. HDMEC tubule formation and migration were assessed by Matrigel culture and migration assay. Production of matrix metalloproteinase (MMP) and tissue inhibitor of metalloproteinases 1 (TIMP-1) in RA synovial explants, and proteoglycan/glycosaminoglycan (GAG) release, vascular endothelial growth factor (VEGF), and angiopoietin 2 production from RASF/normal cartilage cocultures were assessed by enzyme-linked immunosorbent assay and immunohistology. RESULTS: HDMEC/RASF proliferation was induced by OSM and interleukin-1beta (IL-1beta), alone and in combination. OSM enhanced cell surface expression of ICAM-1, but not VCAM-1, on endothelial cells and RASFs. OSM increased endothelial cell tubule formation and migration. In RA synovial explants, OSM induced production of MMP-1 and TIMP-1. When OSM was combined with IL-1beta, however, the MMP-1:TIMP-1 ratio was significantly increased. OSM potentiated IL-1beta-induced MMP-1 and MMP-13 expression in normal human cartilage/RASF cocultures, resulting in a significant increase in the MMP:TIMP ratio. In OSM/IL-1beta- stimulated cocultures, cartilage sections demonstrated significant proteoglycan depletion that was paralleled by a significant increase in GAG release in supernatants. Finally, compared with either cytokine alone, the combination of OSM and IL-1beta significantly induced VEGF production in RASF/cartilage cocultures. CONCLUSION: These data suggest that OSM promotes angiogenesis and endothelial cell migration and potentiates the effects of IL-1beta in promoting extracellular matrix turnover and human cartilage degradation. Furthermore, the induction of VEGF in cocultures supports the hypothesis of a link between angiogenesis and cartilage degradation.

Arthritis, Rheumatoid↗