Protein Kinase C Signaling in Leukocyte Activation
Summary
Protein kinase C (PKC) enzymes form a versatile family of serine/threonine kinases that translate membrane lipid signals into functional responses in leukocytes. Upon engagement of cell-surface receptors by chemoattractants, immunoglobulins or cytokines, phospholipase C is activated to generate inositol trisphosphate and diacylglycerol (DAG). Inositol trisphosphate mobilises intracellular Ca2+, while DAG recruits and activates conventional and novel PKC isoforms at the plasma membrane. Once activated, PKC phosphorylates a spectrum of substrates that regulate cytoskeletal rearrangement, degranulation, reactive oxygen species production and transcriptional programmes. Distinct PKC isoforms (for example PKC-β in neutrophils and PKC-δ in macrophages) orchestrate discrete phases of leukocyte activation, from chemotaxis to pathogen clearance. Tight regulation of PKC signalling is critical: insufficient activity impairs host defence, whereas excessive or prolonged activation contributes to inflammatory pathology. Consequently, PKC remains a focal point for therapeutic modulation in autoimmunity, infection and inflammatory disorders.
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Protein Kinase C Signaling in Leukocyte Activation publication trend
The graph below shows the total number of articles in protein kinase c signaling in leukocyte activation across all publications each year (not limited to Nature Index journals).
Technical terms
Protein kinase C (PKC): A family of enzymes that phosphorylate serine and threonine residues in target proteins upon activation by lipid second messengers and Ca2+.
Diacylglycerol (DAG): A lipid second messenger generated by phospholipase C or phosphatidate dephosphorylation that binds and activates PKC isoforms.
Respiratory burst: The rapid assembly and activation of NADPH oxidase in phagocytes, leading to production of reactive oxygen species for microbial killing.
Phospholipase D (PLD): An enzyme that hydrolyses phosphatidylcholine to phosphatidate, facilitating subsequent DAG formation and PKC recruitment.
Phorbol 12-myristate 13-acetate (PMA): A pharmacological mimic of DAG used to activate PKC experimentally in immune cells.
References
- Effect of phorbol 12-myristate 13-acetate and its analogue 4 alpha-phorbol 12,13-didecanoate on protein phosphorylation and lysosomal enzyme release in rabbit neutrophils.. Journal of Biological Chemistry (1984).
- Phorbol myristate acetate (PMA) augments chemoattractant-induced diglyceride generation in human neutrophils but inhibits phosphoinositide hydrolysis. Implications for the mechanism of PMA priming of the respiratory burst.. Journal of Biological Chemistry (1988).
- Phospholipase D catalyzes phospholipid metabolism in chemotactic peptide-stimulated HL-60 granulocytes.. Journal of Biological Chemistry (1988).
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