BIOMAT Database Logo BIOMAT Database Logo

Structure determination for octasaccharides derived from the carbohydrate-protein linkage region of chondroitin sulphate chains in the proteoglycan aggrecan from bovine articular cartilage. 1998

T N Huckerby, and R M Lauder, and I A Nieduszynski
The Polymer Centre, School of Physics and Chemistry, Lancaster University, Bailrigg, England.

Five octasaccharides derived from the protein carbohydrate linkage region of chondroitin sulphate (CS) have been isolated from the large aggregating proteoglycan (aggrecan) extracted from the bovine articular cartilage of 6-year-old to 8-year-old animals. Following the purification of aggrecan the attached CS chains were digested with CS ABC endolyase and subsequently released from the protein core by beta-elimination. The individual oligosaccharides were purified by strong anion-exchange chromatography and their structures determined by very high-field one-dimensional and two-dimensional 1H-NMR spectroscopy. They were found to be octasaccharides, comprised of tetrasaccharide repeat-region extensions to the core tetrasaccharide linkage region structure. They have the following structures: deltaUA(beta1-3)GalNAc(beta1-4)GlcA(beta1-3)GalNAc(beta1-4)+ ++GlcA(beta1-3)Gal(beta1-3)Gal(beta1-4)Xyl-ol, deltaUA(beta1-3)GalNAc(beta1-4)GlcA(beta1-3)GalNAc6S(b eta1-4)GlcA(beta1-3)Gal(beta1-3)Gal(beta1-4)Xyl-ol, deltaUA(beta1-3)GalNAc6S(beta1-4)GlcA(beta1-3)GalNAc(b eta1-4)GlcA(beta1-3)Gal(beta1-3)Gal(beta1-4)Xyl-ol, deltaUA(beta1-3)GalNAc6S(beta1-4)GlcA(beta1-3)GalNA c6S(beta1-4)GlcA(beta1-3)Gal(beta1-3)Gal(beta1-4)Xyl-ol and deltaUA(beta1-3)GalNAc4S(beta1-4)GlcA(beta1-3)GalNA c6S(beta1-4)GlcA(beta1-3)Gal(beta1-3)Gal(beta1-4)Xyl-ol. They differ only in the nature of the sulphation of the GalNAc residues of the tetrasaccharide-repeat-region extension, which forms the first two disaccharides of the repeat region. No sulphation of any of the uronic acid residues has been identified and in one oligosaccharide neither of the GalNAc residues were sulphated. The majority of the linkage regions contained GalNAc residues which were fully 6-sulphated. However, in a significant amount, only one of the residues was 6-sulphated while the other was either unsulphated or 4-sulphated. There was no evidence either for sulphation of the linkage region galactose residues or for phosphorylation of the xylose residue, through which the chain is attached to the core protein.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009682 Magnetic Resonance Spectroscopy Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING). In Vivo NMR Spectroscopy,MR Spectroscopy,Magnetic Resonance,NMR Spectroscopy,NMR Spectroscopy, In Vivo,Nuclear Magnetic Resonance,Spectroscopy, Magnetic Resonance,Spectroscopy, NMR,Spectroscopy, Nuclear Magnetic Resonance,Magnetic Resonance Spectroscopies,Magnetic Resonance, Nuclear,NMR Spectroscopies,Resonance Spectroscopy, Magnetic,Resonance, Magnetic,Resonance, Nuclear Magnetic,Spectroscopies, NMR,Spectroscopy, MR
D009844 Oligosaccharides Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form. Oligosaccharide
D011509 Proteoglycans Glycoproteins which have a very high polysaccharide content. Proteoglycan,Proteoglycan Type H
D002236 Carbohydrate Conformation The characteristic 3-dimensional shape of a carbohydrate. Carbohydrate Linkage,Carbohydrate Conformations,Carbohydrate Linkages,Conformation, Carbohydrate,Conformations, Carbohydrate,Linkage, Carbohydrate,Linkages, Carbohydrate
D002240 Carbohydrate Sequence The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS. Carbohydrate Sequences,Sequence, Carbohydrate,Sequences, Carbohydrate
D002358 Cartilage, Articular A protective layer of firm, flexible cartilage over the articulating ends of bones. It provides a smooth surface for joint movement, protecting the ends of long bones from wear at points of contact. Articular Cartilage,Articular Cartilages,Cartilages, Articular
D002417 Cattle Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor. Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
D002809 Chondroitin Sulfates Derivatives of chondroitin which have a sulfate moiety esterified to the galactosamine moiety of chondroitin. Chondroitin sulfate A, or chondroitin 4-sulfate, and chondroitin sulfate C, or chondroitin 6-sulfate, have the sulfate esterified in the 4- and 6-positions, respectively. Chondroitin sulfate B (beta heparin; DERMATAN SULFATE) is a misnomer and this compound is not a true chondroitin sulfate. Chondroitin 4-Sulfate,Chondroitin 6-Sulfate,Chondroitin Sulfate A,Chondroitin Sulfate C,Blutal,Chondroitin 4-Sulfate, Aluminum Salt,Chondroitin 4-Sulfate, Potassium Salt,Chondroitin 6-Sulfate, Potassium Salt,Chondroitin 6-Sulfate, Sodium Salt,Chondroitin Sulfate,Chondroitin Sulfate 4-Sulfate, Sodium Salt,Chondroitin Sulfate, Calcium Salt,Chondroitin Sulfate, Iron (+3) Salt,Chondroitin Sulfate, Iron Salt,Chondroitin Sulfate, Potassium Salt,Chondroitin Sulfate, Sodium Salt,Chondroitin Sulfate, Zinc Salt,Chonsurid,Sodium Chondroitin Sulfate,Translagen,Chondroitin 4 Sulfate,Chondroitin 4 Sulfate, Aluminum Salt,Chondroitin 4 Sulfate, Potassium Salt,Chondroitin 6 Sulfate,Chondroitin 6 Sulfate, Potassium Salt,Chondroitin 6 Sulfate, Sodium Salt,Chondroitin Sulfate 4 Sulfate, Sodium Salt,Chondroitin Sulfate, Sodium,Sulfate, Chondroitin,Sulfate, Sodium Chondroitin,Sulfates, Chondroitin
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

T N Huckerby, and R M Lauder, and I A Nieduszynski
Gene structure of chick cartilage chondroitin sulfate proteoglycan (aggrecan) core protein.
December 1995, Journal of molecular evolution,
T N Huckerby, and R M Lauder, and I A Nieduszynski
The sulphated carbohydrate-protein linkage region isolated from chondroitin 4-sulphate chains of inter-alpha-trypsin inhibitor in human plasma.
May 1995, Glycobiology,
T N Huckerby, and R M Lauder, and I A Nieduszynski
Structural studies on sulfated oligosaccharides derived from the carbohydrate-protein linkage region of chondroitin sulfate proteoglycans of whale cartilage.
December 1991, European journal of biochemistry,
T N Huckerby, and R M Lauder, and I A Nieduszynski
Roles of aggrecan, a large chondroitin sulfate proteoglycan, in cartilage structure and function.
October 1998, Journal of biochemistry,
T N Huckerby, and R M Lauder, and I A Nieduszynski
Degradation of chondroitin 4-sulphate by tri-fluoroacetolysis: isolation of oligosaccharides from the carbohydrate-protein linkage region.
October 1984, Carbohydrate research,
T N Huckerby, and R M Lauder, and I A Nieduszynski
Dermatan sulphate proteoglycan from human articular cartilage. Variation in its content with age and its structural comparison with a small chondroitin sulphate proteoglycan from pig laryngeal cartilage.
September 1988, The Biochemical journal,
T N Huckerby, and R M Lauder, and I A Nieduszynski
The carbohydrate-protein linkage region of chondroitin 6-sulfate.
December 1968, Biochimica et biophysica acta,
T N Huckerby, and R M Lauder, and I A Nieduszynski
Variations in the chondroitin sulfate-protein linkage region of aggrecans from bovine nasal and human articular cartilages.
November 1996, The Journal of biological chemistry,
T N Huckerby, and R M Lauder, and I A Nieduszynski
Structural studies of two populations of keratan sulphate chains from mature bovine articular cartilage.
January 1989, Glycoconjugate journal,
T N Huckerby, and R M Lauder, and I A Nieduszynski
Formation of chondroitin sulphate proteoglycan in cartilage regenerated from free perichondrial graft.
January 1989, Scandinavian journal of plastic and reconstructive surgery and hand surgery,
Copied contents to your clipboard!