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Related Experiment Videos

Complement activates phospholipases and protein kinases in glomerular epithelial cells

A V Cybulsky1, J Papillon, A J McTavish

  • 1Department of Medicine, Royal Victoria Hospital, McGill University, Montreal, Quebec, Canada. cybulsky@pathology.lan.mcgill.ca

Kidney International
|August 5, 1998
PubMed
Summary

Complement C5b-9 activates cytosolic phospholipase A2 (cPLA2) in glomerular epithelial cells (GEC) via the diacylglycerol-protein kinase C (PKC) pathway. Mitogen-activated protein kinase (MAPK) activity is secondary to PKC in this process.

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Area of Science:

  • Nephrology
  • Cell Biology
  • Molecular Biology

Background:

  • Complement C5b-9 triggers glomerular epithelial cell (GEC) injury and proteinuria in rat membranous nephropathy.
  • Eicosanoids partially mediate GEC injury, with sublytic C5b-9 activating cytosolic phospholipase A2 (cPLA2) to release arachidonic acid (AA) and eicosanoids.
  • This study investigates the role of protein kinases in C5b-9-induced cPLA2 activation.

Purpose of the Study:

  • To elucidate the role of protein kinases, specifically protein kinase C (PKC) and mitogen-activated protein kinase (MAPK), in the activation of cytosolic phospholipase A2 (cPLA2) by complement C5b-9 in rat glomerular epithelial cells (GEC).

Main Methods:

  • Glomerular epithelial cells (GEC) were stably transfected with wild-type (wt) cPLA2 or a serine505-->alanine mutant (cPLA2-SA505) lacking the MAPK phosphorylation site.

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  • Protein kinase C (PKC) activity was depleted, and p42 MAPK pathways were inhibited to assess their roles.
  • Epidermal growth factor (EGF) was used to activate p42 MAPK and stimulate PKC activity.

    • Main Results:

    • Complement C5b-9 activated p42 MAPK and protein kinase C (PKC) in GEC. Overexpression of either cPLA2-wt or cPLA2-SA505 amplified arachidonic acid (AA) release.
    • Depletion of PKC abolished complement-dependent cPLA2 activation, while p42 MAPK inhibition had no effect.
    • Epidermal growth factor (EGF) activated p42 MAPK strongly but PKC weakly. EGF-induced cPLA2 activation required PKC and was augmented by p42 MAPK.

    Conclusions:

    • Complement C5b-9-induced activation of cytosolic phospholipase A2 (cPLA2) in GEC is primarily dependent on the diacylglycerol-protein kinase C (PKC) pathway.
    • The p42 mitogen-activated protein kinase (MAPK) pathway's role in cPLA2 activation is secondary and becomes redundant when PKC activation is potent.