Hyaluronate in articular cartilage: Age-related changes

1978 ◽  
Vol 26 (1) ◽  
pp. 19-21 ◽  
Author(s):  
E. J. -M. A. Thonar ◽  
M. B. E. Sweet ◽  
A. R. Immelman ◽  
G. Lyons
2014 ◽  
Vol 75 (2) ◽  
pp. 449-458 ◽  
Author(s):  
Wang Hui ◽  
David A Young ◽  
Andrew D Rowan ◽  
Xin Xu ◽  
Tim E Cawston ◽  
...  

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

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.


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

2001 ◽  
Vol 358 (2) ◽  
pp. 523 ◽  
Author(s):  
Robert M. LAUDER ◽  
Thomas N. HUCKERBY ◽  
Gavin M. BROWN ◽  
Michael T. BAYLISS ◽  
Ian A. NIEDUSZYNSKI

1998 ◽  
Vol 330 (2) ◽  
pp. 753-757 ◽  
Author(s):  
M. Robert LAUDER ◽  
N. Thomas HUCKERBY ◽  
A. Ian NIEDUSZYNSKI ◽  
H. K. Anna PLAAS

Bovine articular cartilage fibromodulin has been isolated from animals aged 3 months to 8 years, and the attached keratan sulphate (KS) chains digested with keratanase II. The oligosaccharides generated have been reduced, examined by high-pH anion-exchange chromatography and their structures identified by comparison with standards. It has been shown that in fibromodulin from young articular cartilage, the KS chains do not possess either non-reducing terminal (α2-6)-linked N-acetylneuraminic acid or fucose (α1-3)-linked to sulphated N-acetylglucosamine residues. However, an age-related increase has been observed in the abundance of both (α2-6)-linked N-acetylneuraminic acid and (α1-3)-linked fucose, neither of which is found in KS isolated from non-articular cartilage, irrespective of the age of the source. Interestingly, the KS chain length remains constant as a function of age, which possibly relates to a role in collagen fibril assembly. In addition, no significant age-related changes were identified in levels of galactose sulphation.


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