Expression and characterization of a carbohydrate-binding fragment of rat aggrecan

• Published in: Glycobiology (Oxford) Vol. 3; no. 2; p. 185
• Main Authors: Saleque, S, Ruiz, N, Drickamer, K
• Format: Journal Article
• Language: English
• Published: England 01-04-1993
• Subjects: Aggrecans; Amino Acid Sequence; Animals; Bacteria - genetics; Binding Sites; Carbohydrate Metabolism; DNA - genetics; Extracellular Matrix Proteins; Gene Expression; Humans; Lectins, C-Type; Molecular Sequence Data; Peptide Fragments - chemistry; Peptide Fragments - genetics; Protein Biosynthesis; Proteoglycans - chemistry; Proteoglycans - genetics; Proteoglycans - metabolism; Rats; Sequence Homology, Amino Acid; Transcription, Genetic
• ISSN: 0959-6658
• DOI: 10.1093/glycob/3.2.185

The COOH-terminal portion of cartilage proteoglycan core protein, aggrecan, expressed by in vitro translation, binds carbohydrate-containing affinity columns. The in vitro expression approach has been used to define the sugar-binding portion of the core protein. The active fragment, which corresponds closely to the carbohydrate-recognition domains in the family of Ca(2+)-dependent (C-type) animal lectins, has been expressed in bacteria and characterized. The CD spectrum of the domain is very similar to the spectrum of the binding domain of serum mannose-binding protein, suggesting that its overall structure probably resembles the known three-dimensional structure of the mannose-binding domain. The binding specificity of the core protein fragment has been characterized using a solid-phase assay. The results suggest that the monosaccharide-binding site is also similar to that in other C-type carbohydrate-recognition domains.