Oligosaccharides Derived from Bovine Articular Cartilage Keratan Sulfates after Keratanase II Digestion: Implications for Keratan Sulfate Structural Fingerprinting

Biochemistry ◽  
1994 ◽  
Vol 33 (16) ◽  
pp. 4836-4846 ◽  
Author(s):  
Gavin M. Brown ◽  
Thomas N. Huckerby ◽  
Haydn G. Morris ◽  
Beverley L. Abram ◽  
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.


1999 ◽  
Vol 274 (9) ◽  
pp. 5777-5781 ◽  
Author(s):  
Håkan Hedlund ◽  
Erik Hedbom ◽  
Dick Heinegård ◽  
Silwa Mengarelli-Widholm ◽  
Finn P. Reinholt ◽  
...  

1996 ◽  
Vol 319 (1) ◽  
pp. 137-141 ◽  
Author(s):  
Gavin M. BROWN ◽  
Thomas N. HUCKERBY ◽  
Beverley L. ABRAM ◽  
Ian A. NIEDUSZYNSKI

Alkaline-borohydride-reduced keratan sulphate chains were isolated from bovine articular cartilage (6–8-year-old animals) and digested with keratanase II, an endo-β-N-acetylglucosaminidase. The resulting oligosaccharides were borohydride-reduced and fractionated on a strong anion-exchange column. 1H-NMR spectroscopic analysis of the products revealed one containing both α(2-3)-linked sialic acid and α(1-3)-linked fucose which was shown to have the structure (I) shown. This structure is a sulphated variant of the VIM-2 epitope (CD65), a putative ligand of E-selectin. No oligosaccharide containing the sialyl-Lex structure [NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAcβ1-] was identified in this study.


2016 ◽  
Vol 202 (5-6) ◽  
pp. 382-392 ◽  
Author(s):  
Shuichi Mizuno ◽  
Eiichiro Takada ◽  
Naomi Fukai

Articular cartilage has multiple histologically distinct longitudinal depth zones. Development and pathogenesis occur throughout these zones. Cartilage explants, monolayer cell culture and reconstituted 3-dimensional cell constructs have been used for investigating mechanisms of pathophysiology in articular cartilage. Such models have been insufficient to reproduce zone-dependent cellular characteristics and extracellular matrix (ECM) upon investigation into cartilage development and pathogenesis. Therefore, we defined a chondrocyte spheroid model consistently formed with isolated chondrocytes from longitudinal depth zones without extrinsic materials. This spheroid showed zone-dependent characteristics of size, cartilage-specific ECM (collagen types I and II, aggrecan and keratan sulfate) and gene expressions of anabolic and catabolic molecules (matrix molecules and matrix metalloproteinase-13). In addition, the spheroid model is small enough to maintain the viability of cells and point symmetry to analyze the gradient of diffusive molecules. This spheroid organoid model will be useful to elucidate the mechanism of histogenesis and pathogenesis in articular cartilage.


Sign in / Sign up

Export Citation Format

Share Document