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Photolysis of intracellular caged sphingosine‐1‐phosphate causes Ca 2+ mobilization independently of G‐protein‐coupled receptors
Author(s) -
Meyer zu Heringdorf Dagmar,
Liliom Karoly,
Schaefer Michael,
Danneberg Kerstin,
Jaggar Jonathan H.,
Tigyi Gabor,
Jakobs Karl H.
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01219-5
Subject(s) - sphingosine , intracellular , g protein coupled receptor , sphingosine 1 phosphate , second messenger system , chemistry , thapsigargin , receptor , sphingosine kinase , biophysics , photodissociation , microbiology and biotechnology , biochemistry , biology , photochemistry
Sphingosine‐1‐phosphate (S1P), the product of sphingosine kinase, activates several widely expressed G‐protein‐coupled receptors (GPCR). S1P might also play a role as second messenger, but this hypothesis has been challenged by recent findings. Here we demonstrate that intracellular S1P can mobilize Ca 2+ in intact cells independently of S1P‐GPCR. Within seconds, S1P generated by the photolysis of caged S1P raised the intracellular free Ca 2+ concentration in HEK‐293, SKNMC and HepG2 cells, in which the response to extracellularly applied S1P was either blocked or absent. Ca 2+ transients induced by photolysis of caged S1P were caused by Ca 2+ mobilization from thapsigargin‐sensitive stores. These results provide direct evidence for a true intracellular action of S1P.