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PubMed1985

Effects of varying intensities of laser energy on articular cartilage: a preliminary study.

The effects of laser energy on articular cartilage were studied utilizing the neodymium YAG laser. Partial-thickness cartilage defects were surgically attempted in the femoral condyles of knee joints in guinea pigs. The defects were exposed to laser energy of varying intensities [group I, 25 J (5 W X 5 sec); group II, 75 J (15 W X 5 sec); group III, 125 J (25 W X 5 sec)]. A fourth group was studied, in which the defect was not lased. Animals were killed at weekly intervals from 1 to 6 weeks and the knee joints were subjected to histological analysis. At 5 weeks, the knees exposed to 25 and 75 J demonstrated a reparative process with chondral proliferation. The knees exposed to 125 J demonstrated fibrotic tissue and tissue necrosis that resulted in fibrosis. In the knees not exposed to laser energy, numerous foci of granulation tissue were present at all stages with the end point of healing being one of fibrosis with disorganized patchy cartilage islands.

Animals↗
PubMed2004

T2 of articular cartilage in the presence of Gd-DTPA2-.

T(2) information and delayed gadolinium-enhanced MRI of cartilage (dGEMRIC) are both used to characterize articular cartilage. They are currently obtained in separate studies because Gd-DTPA(2-) (which is needed for dGEMRIC) affects the inherent T(2) information. In this study, T(2) was simulated and then measured at 8.45 T in 20 sections from two human osteochondral samples equilibrated with and without Gd-DTPA(2-). Both the simulations and data demonstrated that Gd-DTPA(2-) provides a non-negligible mechanism for relaxation, especially with higher (1 mM) equilibrating Gd-DTPA(2-) concentrations, and in areas of tissue with high T(2) (due to weak inherent T(2) mechanisms) and high tissue Gd-DTPA(2-) (due to a low glycosaminoglycan concentration). Nonetheless, T(2)-weighted images of cartilage equilibrated in 1 mM Gd-DTPA(2-) showed similar T(2) contrast with and without Gd-DTPA(2-), demonstrating that the impact on T(2) was not great enough to affect identification of T(2) lesions. However, T(2) maps of the same samples showed loss of conspicuity of T(2) abnormalities. We back-calculated inherent T(2)'s (T(2,bc)) using a T(2)-relaxivity value from a 20% protein phantom (r(2) = 9.27 +/- 0.09 mM(-1)s(-1)) and the Gd-DTPA(2-) concentration calculated from T(1,Gd). The back-calculation restored the inherent T(2) conspicuity, and a correlation between T(2) and T(2,bc) of r = 0.934 (P < 0.0001) was found for 80 regions of interest (ROIs) in the sections. Back-calculation of T(2) is therefore a viable technique for obtaining T(2) maps at high equilibrating Gd-DTPA(2-) concentrations. With T(2)-weighted images and/or low equilibrating Gd-DTPA(2-) concentrations, it may be feasible to obtain both T(2) and dGEMRIC information in the presence of Gd-DTPA(2-) without such corrections. These conditions can be designed into ex vivo studies of cartilage. They appear to be applicable for clinical T(2) studies, since pilot clinical data at 1.5 T from three volunteers demonstrated that calculated T(2) maps are comparable before and after "double dose" Gd-DTPA(2-) (as utilized in clinical dGEMRIC studies). Therefore, it may be possible to perform a comprehensive clinical examination of dGEMRIC, T(2), and cartilage volume in one scanning session without T(2) data correction.

Cartilage, Articular↗
PubMed2000

Age-related effects of TGF-beta on proteoglycan synthesis in equine articular cartilage.

The synthesis of proteoglycans was measured in normal equine articular cartilage of ages 9 months to 20 years and the effect of TGF-beta1 on this activity was investigated. The rate of incorporation of [(35)S]Na(2)SO(4) decreased with age as did the responsiveness of the tissue to the growth factor. The enhanced synthesis of proteoglycan induced at all ages by TGF-beta1 was down-regulated by IL-1 beta and retinoic acid. The expression of mRNA for TGF-beta1, 2, and 3 was also measured, and although the level of TGF-beta1 was highest at all ages, the expression of each growth factor decreased with age.

Age Factors↗
PubMed2000

Cryobiology of articular cartilage: ice morphology and recovery of chondrocytes.

The cryopreservation of articular cartilage chondrocytes has been achieved with cells isolated from the cartilage matrix but has found only limited success when the tissue is left intact. Previous work with ovine cartilage has shown that cryopreservation of the chondrocytes of the superficial and deep zones is possible, but the cells of the intermediate zone have not been successfully cryopreserved. This finding led to the suggestion that there might be biological differences between chondrocytes of the different morphological zones that were responsible for this differential recovery. This study investigates the hypothesis that the cells of the intermediate zone are more sensitive to cryoinjury by introducing cuts in the cartilage so that cells of the intermediate zone have the same proximity to the outer surface of the tissue as the cells of the superficial zone. When this was done, it was found that cells of the intermediate zone could survive cryopreservation as well as the cells of the superficial zone when they were near a surface, but not when they were embedded deep within the tissue. Thus the hypothesis of a biological difference between the cells of the two zones being responsible for the differential recovery is disproved. It is further hypothesized that physical proximity to a surface leads to higher recovery as a result of planar ice growth into the cartilage.

Animals↗
PubMed1985

Ascorbic acid stimulates the resorption of canine articular cartilage induced by a factor derived from activated rabbit macrophages.

Articular cartilage explants from the knees of mongrel dogs release 5-10% of their proteoglycan content spontaneously when cultured for 4 days in serum-free modified Bigger's medium. A factor synthesized and secreted by lipopolysaccharide-stimulated rabbit macrophages can stimulate this release of proteoglycan by 2 to 3-fold. The release of proteoglycan in response to macrophage factor is maximal in the presence of 1.5-50 micrograms/ml L-ascorbic acid. In the absence of ascorbate, or with high levels of ascorbate (150 micrograms/ml), the effect of the factor is diminished by 50%. D-isoascorbate, reduced glutathione, or dithiothreitol cannot substitute for L-ascorbate in producing this effect, while dehydroascorbate can.

Animals↗
PubMed1981

Identification of two further collagenous fractions from articular cartilage.

Salt fractionation of pepsin-solubilized human and porcine articular cartilage has revealed the presence of two further collagenous fractions, CF1 and CF2, at high salt concentration following the precipitation of Type-II, 1 alpha, 2 alpha, 3 alpha, and Type-M collagens. Both fractions precipitate at 2.0 M NaCl, but higher yields of CF1 are obtained at 3.0 M NaCl. CF1 and CF2 can be separated in the native form using carboxymethyl-cellulose chromatography. Under denaturing conditions, CF1 has an apparent molecular weight of 25 000 and is unaffected by mercaptoethanol, whereas CF2 has a molecular weight of 35 000 before and 12 000 after reduction by mercaptoethanol. These fractions are probably fragments derived from larger collagen molecules, although the cyanogen bromide digest studies suggest that they are derived from a collagenous type other than one of those previously identified in cartilage.

Amino Acids↗
PubMed2005

Material properties of articular cartilage in the rabbit tibial plateau.

The material properties of articular cartilage in the rabbit tibial plateau were determined using biphasic indentation creep tests. Cartilage specimens from matched-pair hind limbs of rabbits approximately 4 months of age and greater than 12 months of age were tested on two locations within each compartment using a custom built materials testing apparatus. A three-way ANOVA was used to determine the effect of leg, compartment, and test location on the material properties (aggregate modulus, permeability, and Poisson's ratio) and thickness of the cartilage for each set of specimens. While no differences were observed in cartilage properties between the left and right legs, differences between compartments were found in each set of specimens. For cartilage from the adolescent group, values for aggregate modulus were 40% less in the medial compartment compared to the lateral compartment, while values for permeability and thickness were greater in the medial compartment compared to the lateral compartment (57% and 30%, respectively). Values for Poisson's ratio were 19% less in the medial compartment compared to the lateral compartment. There was also a strong trend for thickness to differ between test locations. Similar findings were observed for cartilage from the mature group with values for permeability and thickness being greater in the medial compartment compared to the lateral compartment (66% and 34%, respectively). Values for Poisson's ratio were 22% less in the medial compartment compared to the lateral compartment.

Animals↗
PubMed2001

[Structure and regulation of articular cartilage proteoglycan expression].

Beyond aggrecan, the major proteoglycan present in articular cartilage that confers resistance to compressive load and viscoelasticity to the tissue, other proteoglycan families have been described in cartilage. Among them, decorin, biglycan and fibromodulin which belong to the small leucine-rich proteoglycans family bind to matrix components, specially to collagen fibrils and thus regulate fibrillogenesis in cartilage and matrix integrity. These small proteoglycans can also interact with TGF-beta and modulate its bioavailability and stability. The third family is composed by cell surface proteoglycans as syndecans, glypican-1 and betaglycan. These molecules interact with various components of cell environment (growth factors, proteases, matrix components, etc.) and mediate numerous cell functions. Some modifications of one of these proteoglycan expression occur during degenerative pathologies and may lead to alteration of the functional properties of the tissue as well as variations in growth factor bioavailability. These factors are involved in the attempt of cartilage repair initiated by chondrocytes in the early stages of osteoarthritis.

Aggrecans↗
PubMed1981

Oscillatory compressional behavior of articular cartilage and its associated electromechanical properties.

The compressive stiffness of articular cartilage was examined in oscillatory confined compression over a wide frequency range including high frequencies relevant to impact loading. Nonlinear behavior was found when the imposed sinusoidal compression amplitude exceeded a threshold value that depended on frequency. Linear behavior was attained only by suitable control of the compression amplitude. This was enabled by real time Fourier analysis of data which provided an accurate assessment of the extent of nonlinearity. For linear viscoelastic behavior, a stiffness could be defined in the usual sense. The dependence of the stiffness on ionic strength and proteoglycan content showed that electrostatic forces between matrix charge groups contribute significantly to cartilage's compressive stiffness over the 0.001 to 20 Hz frequency range. Sinusoidal streaming potentials were also generated by oscillatory compression. A theory relating the streaming potential field to the fluid velocity field is derived and used to interpret the data. The observed magnitude of the streaming potential suggests that interstitial fluid flow is significant to cartilage behavior over the entire frequency range. The use of simultaneous streaming potential and stiffness data with an appropriate theory appears to be an important tool for assessing the relative contribution of fluid flow, intrinsic matrix viscoelasticity, or other molecular mechanisms to energy dissipation in cartilage. This method is applicable in general to hydrated, charged polymers.

Action Potentials↗
PubMed1974

Neutral proteases and cathepsin D in human articular cartilage.

Proteolytic enzymes have been studied in extracts of human articular cartilage by the use of micromethods. The digestion of hemoglobin at pH 3.2 and of cartilage proteoglycan at pH 5 was shown to be due chiefly to cathepsin D. Cathepsin D was purified 900-fold from human patellar cartilage. Its identity was established by its specific cleavage of the B chain of insulin. At least six multiple forms of cathepsin D are present in cartilage; these corresponded to bovine forms 4-9. Cathepsin D had no action on proteins at pH 7.4. However, cartilage extracts digested proteoglycan, casein, and histone at this pH. The proteolytic activities against these three substrates were purified about 170-, 160-, and 70-fold, respectively. Each activity appeared in multiple forms on DEAE-Sephadex chromatography. The three activities appear to be different since cysteine inhibited casein digestion, aurothiomalate inhibited histone digestion, and neither inhibited proteoglycan digestion. Tests with a wide range of inhibitors and activators suggest that these three activities differ from other neutral proteases described in the literature.

Aged↗
PubMed1976

Metalloproteases of human articular cartilage that digest cartilage proteoglycan at neutral and acid pH.

Extracts of human articular cartilage contain proteases capable of degrading the proteoglycan component of cartilage matrix at neutral and acid pH. These enzymes have been partially purified by ion exchange chromotography and characterized by disc electrophoresis, inhibition patterns, and action of proteoglycan. Three distinct metalloproteases are described. A neutral protease that digests proteoglycan subunit optimally at pH 7.25 has been purified up to 900-fold. It is strongly inhibited by o-phenanthroline, alpha-2-macroglobulin, and egg white, and to a lesser extent by D-penicillamine and EDTA. Inhibition by chelating agents is reversed by cobalt, zinc, and ferrous ions. Two acid metalloproteases, distinct from cathespins B1, D, and F, digest proteoglycan subunit at pH 4.5 and 5.5. Both are inhibited by o-phenanthroline and activity is restored by cobalt, zinc, or ferrous ions. With electron microscopy, it was found that cartilage slices were depleted of ruthenium red-staining matrix proteoglycan after incubation in vitro with a partially purified cartilage extract at neutral pH. Sedimentation, gel chromatography, sodium dodecyl sulfate-gel electrophoresis, and immuno-diffusion studies of digests of isolated proteoglycan fraction produced by the partially purified cartilage extract at neutral and acid pH confirmed that the cartilage enzymes act only on the protein component of proteoglycan subunit, producing fragments with 5 to 12 chondroitin sulfate chains. The link proteins were not digested.

Cartilage, Articular↗
PubMed1997

Unweighting accelerates tidemark advancement in articular cartilage at the knee joint of rats.

Morphologic development of articular cartilage is influenced by biologic adaptation to functional demands. It has been theorized that intermittent stresses generated by load bearing and motion determine cartilage thickness by controlling advancement of the subchondral mineralization front. The mineralization front is comprised of two interfaces, the tidemark and chondroosseus junction, each of which advances through a different biologic process. This study was designed to evaluate the influence of one month of hind limb unweighting, with and without concurrent restriction of joint motion, on mineral apposition at the tidemark and vascular invasion at the chondroosseus junction in the knee joints of young adult rats. In mobile joints, hind limb unweighting induced a 2-fold increase in the tidemark mineral apposition rate (p = 0.0001) at the primary weight bearing region, resulting in a thinning of the uncalcified cartilage layer and a concurrent thickening of the calcified layer. Cast immobilization negated the effect of unweighting at the tidemark while it activated subchondral vascular encroachment into the calcified cartilage (p = 0.001). These findings suggest that cartilage thinning associated with the elimination of weight bearing is mediated through a different biological mechanism than cartilage loss associated with restriction of joint motion.

Adaptation, Physiological↗
PubMed2005

Distribution of small proteoglycans and glycosaminoglycans in humerus-related articular cartilage of chickens.

The expression of components present in the cartilaginous extracellular matrix is related to development, gender, and genotype, as well as to the biomechanical properties of each type of cartilage. In the present study, we analyzed small proteoglycans and glycosaminoglycans present in different cartilages of the chicken wing after extraction with guanidine hydrochloride or papain. Quantitative analysis of glycosaminoglycans showed a larger amount in humeral cartilage (around 200 mg/g tissue) than in articular cartilage of the radius and ulna, with 138 and 80 mg/g tissue, respectively. Non-collagenous proteins isolated were predominantly from cartilage in the proximal regions of the humerus and radius. D4 fractions obtained by ultracentrifugation were separated by DEAE-Sephacel and Octyl-Sepharose chromatography and analyzed by SDS-PAGE. Two bands of 57 and 70-90 kDa were observed for all samples treated with beta-mercaptoethanol. Immunoblotting of these proteins was positive for the small proteoglycans fibromodulin and decorin, respectively. Apparently, the 57-kDa protein is present in macromolecular complexes of 160 and 200 kDa. Chondroitin sulfate was detected in all regions. HPLC analysis of the products formed by chondroitinase AC and ABC digestion mainly revealed beta-D-glucuronic acid and N-acetyl beta-D-galactosamine residues. The 4-sulfation/6-sulfation ratio was close to 3, except for the proximal cartilage of the radius (2.5). These results suggest functional differences between the scapula-humerus, humerus-ulna, and humerus-radius joints of the chicken wing. This study contributes to the understanding of the physiology of cartilage and joints of birds under different types of mechanical stress.

Animals↗
PubMed2005

Desmin-positive and alpha-smooth muscle actin positive chondrocytes in human defective articular cartilage--preliminary report.

We studied the results of immunostaining for S-100 protein, alpha-smooth muscle actin, muscle specific actin and desmin in articular cartilage specimens obtained during an arthroscopy from eight patients with different degrees of osteoarthritis of the knee joint. In all cases, most of the cartilage cells were strongly positive for S-100 protein. Actin positive chondrocytes were present in four samples showing repair cartilage changes with occurrence of fibrocartilage tissue. Moreover, in one case, we observed typical desmin-positive chondrocytes in the layer of cartilage filling the defect of the articular cartilage surface. The expression of desmin can be regarded as a reaction to trauma or the indication of an inherent abnormality. The chondrocytes probably switched on smooth muscle features during the healing process, because desmin is to a great extent a typical muscle cell marker. This fact could probably support our previous supposition that cartilage cells expressing muscle markers could be designated as myochondroblasts and myochondrocytes analogously to the terminology of myofibroblasts. It is possible that during the healing of the cartilage defects, such a transformation of the immunophenotype of the cartilage cells is quite frequent, but it could also be only transient nature only.

Actins↗
PubMed1985

Comparison of spontaneous and retinoic acid stimulated rabbit articular cartilage degradation in vitro.

The in vitro degradation of rabbit articular cartilage explants was evaluated with and without the addition of retinoic acid under various experimental conditions. Retinoic acid at nontoxic concentrations ranging from 1 X 10(-7) to 1 X 10(-5) M significantly increased cartilage degradation. The addition of phenanthroline or cycloheximide, but not pepstatin, significantly inhibited spontaneous and retinoic-acid-stimulated cartilage degradation at pH 7. When the pH was reduced to 5, only pepstatin inhibited spontaneous and retinoic-acid-stimulated cartilage degradation. No chondroitin sulphate release was observed when the temperature was reduced to 4 degrees C. The different inhibitory profiles observed at pH 7 and pH 5 suggest that cartilage degradation at pH 7 is associated with the presence and synthesis of a neutral metalloproteinase.

Animals↗
PubMed1983

Studies on the repair tissue of injured articular cartilage--biochemical and biomechanical properties.

The repair tissue of the articular cartilage of a rabbit was investigated biochemically and biomechanically. An analysis of the proteoglycan demonstrated the synthesis of heavy proteoglycan component as in hyaline cartilage, but its average size was slightly smaller than normal hyaline cartilage. The collagen changed its molecular type from type I to type II at the surface of the repair tissue simultaneously up to 7 weeks after the operation. The lack of normal mucoelasticity was found in the repair tissue by the static compression test, and this may be related to the abnormalities of the proteoglycan.

Animals↗