Photolysis of intracellular caged sphingosine-1-phosphate causes Ca 2+ mobilization independently of G-protein-coupled receptors

Dagmar Meyer Zu Heringdorf, K. Liliom, Michael Schaefer, Kerstin Danneberg, Jonathan H. Jaggar, Gabor Tigyi, Karl H. Jakobs

Research output: Contribution to journalArticle

81 Citations (Scopus)

Abstract

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 Ca2+ in intact cells independently of S1P-GPCR. Within seconds, S1P generated by the photolysis of caged S1P raised the intracellular free Ca2+ concentration in HEK-293, SKNMC and HepG2 cells, in which the response to extracellularly applied S1P was either blocked or absent. Ca2+ transients induced by photolysis of caged S1P were caused by Ca2+ mobilization from thapsigargin-sensitive stores. These results provide direct evidence for a true intracellular action of S1P.

Original languageEnglish
Pages (from-to)443-449
Number of pages7
JournalFEBS Letters
Volume554
Issue number3
DOIs
Publication statusPublished - Nov 20 2003

Fingerprint

Photolysis
G-Protein-Coupled Receptors
Thapsigargin
HEK293 Cells
Hep G2 Cells
Second Messenger Systems
sphingosine 1-phosphate
caged sphingosine 1-phosphate

Keywords

  • Ca mobilization
  • Photolysis
  • Sphingosine-1-phosphate
  • Thapsigargin-sensitive Ca store

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Photolysis of intracellular caged sphingosine-1-phosphate causes Ca 2+ mobilization independently of G-protein-coupled receptors. / Meyer Zu Heringdorf, Dagmar; Liliom, K.; Schaefer, Michael; Danneberg, Kerstin; Jaggar, Jonathan H.; Tigyi, Gabor; Jakobs, Karl H.

In: FEBS Letters, Vol. 554, No. 3, 20.11.2003, p. 443-449.

Research output: Contribution to journalArticle

Meyer Zu Heringdorf, Dagmar ; Liliom, K. ; Schaefer, Michael ; Danneberg, Kerstin ; Jaggar, Jonathan H. ; Tigyi, Gabor ; Jakobs, Karl H. / Photolysis of intracellular caged sphingosine-1-phosphate causes Ca 2+ mobilization independently of G-protein-coupled receptors. In: FEBS Letters. 2003 ; Vol. 554, No. 3. pp. 443-449.
@article{6d5b3a61ea6e408db611697268bf7752,
title = "Photolysis of intracellular caged sphingosine-1-phosphate causes Ca 2+ mobilization independently of G-protein-coupled receptors",
abstract = "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 Ca2+ in intact cells independently of S1P-GPCR. Within seconds, S1P generated by the photolysis of caged S1P raised the intracellular free Ca2+ concentration in HEK-293, SKNMC and HepG2 cells, in which the response to extracellularly applied S1P was either blocked or absent. Ca2+ transients induced by photolysis of caged S1P were caused by Ca2+ mobilization from thapsigargin-sensitive stores. These results provide direct evidence for a true intracellular action of S1P.",
keywords = "Ca mobilization, Photolysis, Sphingosine-1-phosphate, Thapsigargin-sensitive Ca store",
author = "{Meyer Zu Heringdorf}, Dagmar and K. Liliom and Michael Schaefer and Kerstin Danneberg and Jaggar, {Jonathan H.} and Gabor Tigyi and Jakobs, {Karl H.}",
year = "2003",
month = "11",
day = "20",
doi = "10.1016/S0014-5793(03)01219-5",
language = "English",
volume = "554",
pages = "443--449",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "3",

}

TY - JOUR

T1 - Photolysis of intracellular caged sphingosine-1-phosphate causes Ca 2+ mobilization independently of G-protein-coupled receptors

AU - Meyer Zu Heringdorf, Dagmar

AU - Liliom, K.

AU - Schaefer, Michael

AU - Danneberg, Kerstin

AU - Jaggar, Jonathan H.

AU - Tigyi, Gabor

AU - Jakobs, Karl H.

PY - 2003/11/20

Y1 - 2003/11/20

N2 - 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 Ca2+ in intact cells independently of S1P-GPCR. Within seconds, S1P generated by the photolysis of caged S1P raised the intracellular free Ca2+ concentration in HEK-293, SKNMC and HepG2 cells, in which the response to extracellularly applied S1P was either blocked or absent. Ca2+ transients induced by photolysis of caged S1P were caused by Ca2+ mobilization from thapsigargin-sensitive stores. These results provide direct evidence for a true intracellular action of S1P.

AB - 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 Ca2+ in intact cells independently of S1P-GPCR. Within seconds, S1P generated by the photolysis of caged S1P raised the intracellular free Ca2+ concentration in HEK-293, SKNMC and HepG2 cells, in which the response to extracellularly applied S1P was either blocked or absent. Ca2+ transients induced by photolysis of caged S1P were caused by Ca2+ mobilization from thapsigargin-sensitive stores. These results provide direct evidence for a true intracellular action of S1P.

KW - Ca mobilization

KW - Photolysis

KW - Sphingosine-1-phosphate

KW - Thapsigargin-sensitive Ca store

UR - http://www.scopus.com/inward/record.url?scp=0242710592&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0242710592&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(03)01219-5

DO - 10.1016/S0014-5793(03)01219-5

M3 - Article

VL - 554

SP - 443

EP - 449

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 3

ER -