Agents and Actions

, Volume 27, Issue 3–4, pp 385–387 | Cite as

Phospholipase A2 (PLA2) activity in rabbit chondrocytes

  • T. M. Stevens
  • J. E. Chin
  • M. McGowan
  • J. Giannaras
  • J. S. Kerr
Eicosanoids

Abstract

The effects of recombinant interleukin-1β (rIL-1β), recombinant tumor necrosis factor (rTNFα) and two growth factors, basic fibroblast growth factor (bFGF) and epidermal growth factor (EGF) on PLA2 activity and prostaglandin E2 (PGE2) release were investigated using rabbit chondrocytes. Cellular PLA2 activity increased 2–10×above controls in the presence of 8×10−12M (5 U) rIL-1β or 5×10−9M rTNFα after 20 hr incubation. PLA2 activity remained constant with 1–50 ng/ml of either growth factor. PGE2 release significantly increased (p<0.05) when the chondrocytes were incubated with rIL-1β, bFGF and EGF alone, but not with rTNFα above. These data suggest PLA2 activity and PGE2 release are not coordinately regulated in rabbit chondrocytes.

Keywords

Growth Factor Tumor Necrosis Tumor Necrosis Factor Prostaglandin Epidermal Growth Factor 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. [1]
    S. C. Gilman, P. R. Berner and J. Chang,Phospholipase A 2 activation by interleukin-1: release and metabolism of arachidonic acid by IL-1-stimulated chondrocytes. Agents and Actions21, 345–347 (1987).Google Scholar
  2. [2]
    J. Chang, S. C. Gilman and A. J. Lewis,Interleukin-1 activates phospholipase A 2 in rabbit chondrocytes: A possible signal for IL-1 action. J. Immunol.136, 1283–1287 (1986).Google Scholar
  3. [3]
    R. W. Godfrey, W. J. Johnson, T. Newman and S. T. Hoffstein,Interleukin-1 and tumor necrosis factor are not synergistic for human synovial fibroblast PLA 2 activation and PGE 2 production. Prostaglandins35, 107–114 (1988).Google Scholar
  4. [4]
    V. Evequoz, F. Bettens, F. Kristensen, U. Trachsel, B. M. Stadler and J.-M. Dayer,Interleukin-2-independent stimulation of rabbit chondrocyte collagenase and prostaglandin E 2 production by an interleukin-1-like factor. Eur. J. Immunol.14, 490–495 (1984).Google Scholar
  5. [5]
    P. Patriarca, S. Beckerdite and P. Elsbach,Phospholipases and phospholipid turnover in Escherichia coli spheroplasts. Biochem. Biophys. Acta260, 593–600 (1972).Google Scholar
  6. [6]
    F. F. Davidson, E. A. Dennis, M. Powell and J. R. Glenney Jr.,Inhibition of phospholipase A 2 by “lipocortins” and calpactins. An effect of binding to substrate phospholipids. J. Biol. Chem.262, 1698–1705 (1987).Google Scholar
  7. [7]
    M. M. Bradford,A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem.72, 248–254 (1976).Google Scholar
  8. [8]
    S. C. Gilman,Activation of rabbit articular chondrocytes by recombinant human cytokines. J. Rheumatol.14, 1002–1007 (1987).Google Scholar

Copyright information

© Birkhäuser Verlag 1989

Authors and Affiliations

  • T. M. Stevens
    • 1
  • J. E. Chin
    • 1
  • M. McGowan
    • 1
  • J. Giannaras
    • 1
  • J. S. Kerr
    • 1
  1. 1.Medical Products DepartmentE. I. Du Pont de Nemours & Co., Inc., Experimental Station, E400/4223WilmingtonUSA

Personalised recommendations