CHANGES IN SWINE KNEE ARTICULAR CARTILAGE DURING GROWTH

1979 ◽  
Vol 59 (1) ◽  
pp. 167-179 ◽  
Author(s):  
T. NAKANO ◽  
F. X. AHERNE ◽  
J. R. THOMPSON

Twenty-five crossbred boars reared under normal conditions were serially slaughtered at the age of 3 days, and 5, 10, 20 and 30 wk. Five boars were slaughtered at each age and morphological, histochemical and biochemical age-related changes in femoral condylar articular cartilage were studied. No osteochondrotic joints were found in pigs 10 wk of age or younger, while 7 of the 10 boars slaughtered at 20 and 30 wk of age were osteochondrotic. Cartilage thickness increased (P < 0.05) until the age of 5 wk and decreased (P < 0.05) thereafter. Cell density decreased (P < 0.05) as age advanced. Age-associated changes found in the chemical composition of the cartilage were an increase in the concentration of dry matter and hydroxyproline and a decrease in the concentration of glycosaminoglycans (GAG) including chondroitin sulfate (ChS), keratan sulfate and hyaluronic acid. The proportions of soluble proteoglycan and 4-sulfated disaccharide from the ChS fraction decreased (P < 0.05) while the proportion of 6-sulfated disaccharide from ChS increased (P < 0.05). Osteochondrosis was observed as a disturbed endochondral ossification, and softening and fracture of the cartilage. The former was accompanied by a loss of intercellular GAG and cell necrosis, and the latter by local losses of GAG and cells. Osteochondrotic cartilage also contained higher proportions of soluble proteoglycan and 6-sulfated disaccharide, and lower proportions of 4-sulfated disaccharide than did the visually normal cartilage.

1995 ◽  
Vol 75 (3) ◽  
pp. 433-437 ◽  
Author(s):  
T. Nakano ◽  
J. S. Sim

Chemical composition of the proximal tibial articular cartilage and growth plate of broiler chickens from seven age groups (1, 8, 14, 22, 29, 36, and 43 d old) was studied. In the articular cartilage, the contents of dry matter, collagen measured as hydroxyproline, and keratan sulfate increased (P < 0.05), and the content of sialic acid decreased (P < 0.05) as age advanced. The content of chondroitin sulfate measured as uronic acid and the proportion of hyaluronic acid in total glycosaminoglycan (GAG) were relatively constant (P > 0.05) among the age groups. In the growth plate, the contents of chondroitin sulfate and keratan sulfate increased (P < 0.05) with age, while the contents of dry matter, sialic acid, and collagen were similar among the age groups. The proportion of hyaluronic acid in total GAG decreased at the age of 8 d, and remained relatively constant thereafter. The growth dependent changes observed in the concentration of chondroitin sulfate in the broiler chicken cartilage were different from those in other species which have been reported to show a decrease during early postnatal growth. Key words: Tibia, epiphyseal cartilage, growth plate, broiler chicken, age


1978 ◽  
Vol 176 (3) ◽  
pp. 683-693 ◽  
Author(s):  
M T Bayliss ◽  
S Y Ali

1. Analysis of the purified proteoglycans extracted from normal human articular cartilage with 4M-guanidinium chloride showed that there was an age-related increase in their content of protein and keratan sulphate. 2. The hydrodynamic size of the dissociated proteoglycans also decreased with advancing age, but there was little change in the proportion that could aggregate. 3. Results suggested that some extracts of aged-human cartilage had an increased content of hyaluronic acid compared with specimens from younger patients. 4. Dissociated proteoglycans, from cartilage of all age groups, bind to hyaluronic acid and form aggregates in direct proportion to the hyaluronic acid concentration. 5. Electrophoretic heterogeneity of the dissociated proteoglycans was demonstrated on polyacrylamide/agarose gels. The number of proteoglycan species observed was also dependent on the age of the patient.


2014 ◽  
Vol 75 (2) ◽  
pp. 449-458 ◽  
Author(s):  
Wang Hui ◽  
David A Young ◽  
Andrew D Rowan ◽  
Xin Xu ◽  
Tim E Cawston ◽  
...  

1994 ◽  
Vol 42 (4) ◽  
pp. 513-522 ◽  
Author(s):  
A Asari ◽  
S Miyauchi ◽  
S Kuriyama ◽  
A Machida ◽  
K Kohno ◽  
...  

To demonstrate localization of hyaluronic acid (HA) in articular cartilage of the human femur, biotinylated HA-binding region, which specifically binds HA molecules, was applied to the tissue. In sections fixed by 2% paraformaldehyde-2% glutaraldehyde, HA staining was detected in lamina splendens and chondrocytes in the middle zone. By pretreatment with trypsin, intense HA staining appeared in the extracellular matrix of the deep zone and weak staining in the superficial and middle zones. Moreover, pre-treatment with chondroitinase ABC (CHase ABC) intensely enhanced the stainability for HA in the superficial and middle zones and weakly in the deeper zone. Combined pre-treatment of trypsin with CHase ABC abolished intra- and extracellular staining for HA in all zones. By microbiochemical study, the concentrations of HA and dermatan sulfate were high in the middle zone, whereas those of chondroitin sulfate and keratan sulfate were high in the deep zone. These results suggest that HA is abundantly synthesized in and secreted from the chondrocytes, particularly in the middle zone, whereas it is largely masked by proteoglycan constituents in the extracellular matrix.


1989 ◽  
Vol 19 (2-4) ◽  
pp. 121-133 ◽  
Author(s):  
Philippe Front ◽  
France Aprile ◽  
Dragoslav R. Mitrovic ◽  
David A. Swann

1978 ◽  
Vol 171 (1) ◽  
pp. 149-154 ◽  
Author(s):  
M T Bayliss ◽  
S Y Ali

The thiol proteinase cathepsin B (EC 3.4.22.1), previously called cathepsin B1, was assayed in human articular cartilage by its hydrolysis of the synthetic substrate alpha-N-benzoyl-DL-arginine 2-naphthylamide. The enzyme was activated by cysteine and EDTA and completely inhibited by iodoacetamide and HgCl2. It was also partially inhibited by whole human serum. Human osteoarthrotic cartilage had increased activity when compared with normal cartilage. Cathepsin B activity of normal cartilage was age-related, being high in juveniles and declining to low values in adult and elderly individuals. Cathepsin D and cathepsin B both exhibited a zonal variation through the cartilage depth; the surface cells appeared to contain more activity than those close to the subchondral bone.


1978 ◽  
Vol 26 (1) ◽  
pp. 19-21 ◽  
Author(s):  
E. J. -M. A. Thonar ◽  
M. B. E. Sweet ◽  
A. R. Immelman ◽  
G. Lyons

1982 ◽  
Vol 2 (1) ◽  
pp. 45-60 ◽  
Author(s):  
Brian R. Champion ◽  
Agnes Reiner ◽  
Peter J. Roughley ◽  
A. Robin Poole

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