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Papers In Press, published online ahead of print February 20, 2002
J. Biol. Chem, 10.1074/jbc.M110944200
Submitted on November 15, 2001
Revised on February 18, 2002
Accepted on February 20, 2002

Dichotomy of Ca2+ signals triggered by different phospholipid pathways in antigen stimulation of human mast cells

Alirio J. Melendez and Aik K. Khaw

Physiology, National University of Singapore, Singapore 117597

Corresponding Author: phsmraj{at}nus.edu.sg

Mast cell activation triggers Ca2+ signals and the release of enzyme containing granules, events that play a major role in allergic/hypersensitivity reactions. However, the precise molecular mechanisms that regulate antigen triggered degranulation and Ca2+ fluxes, in human mast cells, are still poorly understood. Here we show, for the first time, that a receptor can trigger Ca2+ via two separate molecular mechanisms. Using an antisense approach, we show that IgE-antigen stimulation, of human bone marrow-derived mast cells, triggers a sphingosine kinase 1 (SPHK1)-mediated fast and transient Ca2+ release from intracellular stores. However, PLCg1 triggers a second (slower) wave of calcium release from intracellular stores, and it this PLCg1 generated signal that is responsible for Ca2+ entry. Surprisingly, FceRI triggered mast cell degranulation depends on the first, sphingosine kinase-mediated, Ca2+ signal. These two pathways act independently, since antisense knock down of either enzyme does not interfere with the activity of the other. Of interest, similarly to PLCg1, SPHK1 rapidly translocates to the membrane, after FceRI crosslinking. Here we also show that SPHK1 activity depends on phospholipase D1 (PLD1), and that, FceRI-triggered mast cells degranulation depends primarily on the activation of both PLD1 and SPHK1.


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