Structure of the keratan sulphate chains attached to fibromodulin isolated from bovine tracheal cartilage. Oligosaccharides generated by keratanase digestion

Huckerby

Nieduszynski

et al. 1998

Biochemical Journal

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.

“…A single peak of fibromodulin eluted at approx. 32 min, identical with that reported previously for fibromodulin [14].…”

Section: Isolation Of Fibromodulin From Bovine Articular Cartilagesupporting

confidence: 90%

Section: Digestion and Examination Of Ksmentioning

confidence: 97%

Section: Isolation Of Oligosaccharidesmentioning

confidence: 99%

Section: Isolation Of Fibromodulinmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Age-related changes in the structure of the keratan sulphate chains attached to fibromodulin isolated from articular cartilage

Huckerby

Nieduszynski

et al. 1998

Biochemical Journal

Proteoglycan and Acidic Polysaccharide Analysis

Encyclopedia of Analytical Chemistry

2000

The isolation and analysis of proteoglycans (PGs) and the acidic polysaccharide glycosaminoglycan (GAG) chains attached to them is an area of increasing importance. PGs are a structurally diverse group of complex macromolecules comprising a core protein, varying in size from 11 to 400 kDa, to which are attached one or more GAG chains of the same or a different type. These chains carry a negative charge derived mainly from sulfate groups and are composed of a repeating disaccharide, a hexosamine and either a hexuronic acid or, in keratan sulfate (KS), galactose.

Proteoglycans and Acidic Polysaccharides Analysis

Encyclopedia of Analytical Chemistry

2015

The study of the structure and function of proteoglycans (PGs) and glycosaminoglycans (GAGs) has assumed an increasing significance as the wide range of important biological processes in which they play central roles has been elucidated. As studies of GAG structure expand in scope, and detail, the full structural diversity of these polymers is being uncovered. Significant heterogeneity can be seen but relationships with development, age, and pathology are being uncovered, which place these macromolecules centrally in these processes. Available methodologies allow detailed analysis of GAGs, but careful attention to the sample requirements of these methods and to their limitations is required to ensure the quality and reliability of the data derived is assured. Important developments, including mass spectrometry approaches, will take the field forward but well‐established methods for the isolation and characterization of these complex molecules continue to have a hugely important role to play in structural and functional studies. This article examines a wide range of methodologies for the isolation and characterization of the PGs and GAGs in which recent developments in the field are reported along with well‐established methods for the characterization of entire GAG chains or discrete features within those.