Effect of recombinant cytokines on glycolysis and fructose 2,6-bisphosphate in rheumatoid synovial cells in vitro.

Journal article

Recombinant-derived human interleukin 1 (IL1) alpha and beta and interferon gamma (IFN-gamma) each produced similar increases in rheumatoid synovial cell (RSC) glycolysis, as judged by increased values for glucose uptake, lactate production and cellular fructose 2,6-bisphosphate [Fru(2,6)P2]. Measurement of Fru(2,6)P2 proved to be the most sensitive parameter for an assessment of glycolysis: IL1 alpha, IL1 beta and IFN-gamma all produced a 3-6-fold increase in this metabolite whereas tumour necrosis factor (TNF alpha) was far less effective. Prostaglandin E production was stimulated predominantly by IL1 alpha and IL1 beta rather than by IFN-gamma or TNF alpha. When combinations of cytokines were examined the addition of IFN-gamma with either IL1 alpha, IL1 beta or murine IL1 produced a synergistic increase in cellular Fru(2,6)P2. The three forms of IL1 increased Fru(2,6)P2 via the same pathway, whereas IFN-gamma acted via a different mechanism. The increase in Fru(2,6)P2 in subcultured RSC produced by addition of medium from a primary culture exceeded the maximal effects of any of the single cytokines studied, suggesting the presence of a mixture of cytokines in the primary RSC culture medium.

Authors: Taylor, D; Whitehead, R; Evanson, J; Westmacott, D; Feldmann, M

• Publication status: Published
• Journal: Biochemical journal
• Volume: 250
• Issue: 1
• Pages: 111-115
• Publication date: 1988-02-01
• EISSN: 1470-8728
• ISSN: 0264-6021
• Language: English
• Keywords: Hexosediphosphates; Cells, Cultured; Humans; Interleukin-1; Recombinant Proteins; Fructosediphosphates; Arthritis, Rheumatoid; Prostaglandins E; Synovial Membrane; Interferon-gamma; Glycolysis