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N-acetylglucosamine prevents IL-1 beta-mediated activation of human chondrocytes.
It is shown that both glucosamine and N-acetylglucosamine inhibit IL-1beta- and TNF-alpha-induced NO production in normal human articular chondrocytes and identifies a novel mechanism for the inhibition of inflammatory processes. Expand
Profile of glycosaminoglycan-degrading glycosidases and glycoside sulfatases secreted by human articular chondrocytes in homeostasis and inflammation.
The concept that lysosomal glycosidases, in particular hexosaminidase, represent a distinct subset of cartilage matrix-degrading enzymes that are activated by proinflammatory stimuli is supported. Expand
N-Acetylglucosamine Prevents IL-1β-Mediated Activation of Human Chondrocytes1
It is shown that both glucosamine and N-acetylglucosamine inhibit IL-1β- and TNF-α-induced NO production in normal human articular chondrocytes and identifies a novel mechanism for the inhibition of inflammatory processes. Expand
Cytokine Regulation of Facilitated Glucose Transport in Human Articular Chondrocytes1
- A. Shikhman, D. Brinson, J. Valbracht, M. Lotz
- Biology, Medicine
- The Journal of Immunology
- 15 December 2001
Results demonstrate that stimulation of glucose transport represents a component of the chondrocyte response to IL-1β, and does not require phosphoinositide 3-kinase, extracellular signal-related kinase, or c-Jun N-terminal kinase activation. Expand
The osteoprotegerin/receptor activator of nuclear factor kappaB/receptor activator of nuclear factor kappaB ligand system in cartilage.
Examination of human articular cartilage for the expression of RANK, RANKL, and OPG molecules and the role of RankL in the regulation of chondrocyte function demonstrates theexpression of OPG, Ranks, and RanksL in cartilage. Expand
Role of heavy chain constant domains in antibody-antigen interaction. Apparent specificity differences among streptococcal IgG antibodies expressing identical variable domains.
- L. J. Cooper, A. Shikhman, D. Glass, D. Kangisser, M. Cunningham, N. Greenspan
- Biology, Medicine
- Journal of immunology
- 15 March 1993
The results suggest that epitope density can significantly influence the magnitude of IgG subclass-associated binding differences, and that structural differences in the CH regions, particularly the CH2 and CH3 domains, can influence the apparent specificities of Igg molecules for multivalent Ag. Expand
Immunological mimicry between N-acetyl-beta-D-glucosamine and cytokeratin peptides. Evidence for a microbially driven anti-keratin antibody response.
It is demonstrated that Abs to keratin and synthetic keratin decapeptides were induced in BALB/c mice immunized with GlcNAc-BSA but not with BSA, suggesting that the anti-keratin Ab response in vivo may be driven by nonkeratin Ags containing terminal O-linked Glc NAc. Expand
Cytokeratin peptide SFGSGFGGGY mimics N-acetyl-beta-D-glucosamine in reaction with antibodies and lectins, and induces in vivo anti-carbohydrate antibody response.
Results of the experiments indicated that certain peptides may express functional activity similar to GlcNAc and induce in vivo anti-carbohydrate Ab responses. Expand
A subset of mouse monoclonal antibodies cross-reactive with cytoskeletal proteins and group A streptococcal M proteins recognizes N-acetyl-beta-D-glucosamine.
A new group of multireactive autoantibodies that recognize GlcNAc and cytoskeletal proteins, as well as defined peptide epitopes are identified and previously shown to neutralize coxsackie viruses. Expand
Chondroprotective activity of N-acetylglucosamine in rabbits with experimental osteoarthritis.
Intra-articular GlcNAc has chondroprotective and anti-inflammatory activity in experimental OA and was better than that of viscosupplementation treatment with hyaluronan. Expand