Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10759513 | Biochemical and Biophysical Research Communications | 2013 | 6 Pages |
Abstract
Recent evidences indicating that cellular kinase signaling cascades are triggered by oligomers of N-acetylglucosamine (ChOS) and that condrocytes of human osteoarthritic cartilage secrete the inflammation associated chitolectin YKL-40, prompted us to study the binding affinity of partially acetylated ChOS to YKL-40 and their effect on primary chondrocytes in culture. Extensive chitinase digestion and filtration of partially deacetylated chitin yielded a mixture of ChOS (Oligominâ¢) and further ultrafiltration produced T-ChOSâ¢, with substantially smaller fraction of the smallest sugars. YKL-40 binding affinity was determined for the different sized homologues, revealing micromolar affinities of the larger homologues to YKL-40. The response of osteoarthritic chondrocytes to Oligomin⢠and T-ChOS⢠was determined, revealing 2- to 3-fold increases in cell number. About 500 μg/ml was needed for Oligomin⢠and around five times lower concentration for T-ChOSâ¢, higher concentrations abolished this effect for both products. Addition of chitotriose inhibited cellular responses mediated by larger oligosaccharides. These results, and the fact that the partially acetylated T-ChOS⢠homologues should resist hydrolysis, point towards a new therapeutic concept for treating inflammatory joint diseases.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Jon M. Einarsson, Sven Bahrke, Bjarni Thor Sigurdsson, Chuen-How Ng, Petur Henry Petersen, Olafur E. Sigurjonsson, Halldor Jr., Johannes Gislason, Finnbogi R. Thormodsson, Martin G. Peter,