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A decrease in all major gangliosides, contrasting with a marked increase in the GM3 third band (3B-GM3), has been demonstrated in osteoarthritic fibrillated cartilage. We found the 3B-GM3 in osteoarthritic fibrillated, grossly intact and osteophytic human cartilage, but it was undetectable in pig and bovine cartilage, bone, synovium, synovial fluid white cells, erythrocytes, and various extracellular tissues. We made a similar finding with lactosyl ceramide, the GM3 neutral glycolipid precursor. The search for an antibody against the 3B-GM3, as a possible specific antigenic marker of osteoarthritis (OA), was unsuccessful. However, an antibody against a molecule very close to 3B-GM3 on high performance thin layer chromatography, which will probably be identified as a glycosylphosphatidylinositol, was found in the serum of some patients with OA.

Objective: Glycosphingolipids (GSLs) are biologically active molecules in the physiology and pathology of cells. Since changes in GSLs might be associated with the impaired metabolism of articular cartilage in osteoarthritis (OA), we investigated gangliosides from normal and OA human cartilage., Methods: OA and control cartilage was obtained from patients with hip OA and femoral neck fracture, respectively. Gangliosides were extracted and quantified by determining their lipid-bound sialic acid concentration. Major gangliosides were identified by immuno-detection on thin-layer plates, purified by high performance liquid chromatography, and analyzed for their carbohydrate, fatty acid, and long-chain base composition., Results: The total ganglioside content of OA cartilage was decreased by 40% (per mg of DNA). Major gangliosides, GM3 and GD3, separated into 3 on thin-layer chromatography bands. All were decreased except for the lowest migrating band of GM3, which was increased 5-fold. This ganglioside had the same carbohydrate moiety and fatty acids as the other two, but differed by a long-chain base composed mainly of C20-sphingosine., Conclusion: OA cartilage is characterized by a decrease in all gangliosides except GM3, which demonstrates a large increase in the lowest band. These results indicate that there are changes in the biochemical composition of chondrocyte membranes in OA. The causes and roles of these changes remain to be determined.

The effect of non-steroidal anti-inflammatory drugs (NSAIDs) on the activity of glycosyltransferases required for the synthesis of the polysaccharide chains of proteoglycans, was studied in human osteoarthritic cartilage in vitro. Using exogenous acceptors, salicylate and indomethacin suppressed the activity of glucuronyl- and xylosyltransferases in a concentration-dependent manner, but had little effect on N-acetylgalactosaminyl- and galactosyltransferases. When used at a concentration derived from the values found in the synovial fluid, salicylate, indomethacin and chloroquine significantly suppressed the activity of glucuronyl- and xylosyltransferases, while tiaprofenic acid, paracetamol (acetaminophen), floctafenine, ketoprofen, ibuprofen and tenoxicam had no effect on the enzymes. An alteration of some glycosyltransferases could explain the reported suppressive effect of some NSAIDs on cartilage proteoglycan synthesis.