Inhibition of Sphingosine Kinase Activity Enhances Immunogenic Cell Surface Exposure of Calreticulin Induced by the Synthetic Cannabinoid 5-epi-CP-55,940

2021 ◽  
Author(s):  
Jeremy A. Hengst ◽  
Asvelt J. Nduwumwami ◽  
Wesley M. Raup-Konsavage ◽  
Kent E. Vrana ◽  
Jong K. Yun
Keyword(s):  
Cell Surface ◽  
Kinase Activity ◽  
Sphingosine Kinase ◽  
Synthetic Cannabinoid ◽  
Cp 55,940

Essential requirement for sphingosine kinase activity in eNOS‐dependent NO release and vasorelaxation

2005 ◽  
Vol 20 (2) ◽  
pp. 340-342 ◽  
Author(s):  
Fiorentina Roviezzo ◽  
Mariarosaria Bucci ◽  
Chantal Delisle ◽  
Vincenzo Brancaleone ◽  
Annarita Di Lorenzo ◽  
...  
Keyword(s):  
Kinase Activity ◽  
Sphingosine Kinase ◽  
Essential Requirement ◽  
No Release

scholarly journals Broad and Region-Specific Impacts of the Synthetic Cannabinoid CP 55,940 in Adolescent and Adult Female Mouse Brains

2018 ◽  
Vol 11 ◽  
Author(s):  
Emma Leishman ◽  
Michelle N. Murphy ◽  
Michelle I. Murphy ◽  
Ken Mackie ◽  
Heather B. Bradshaw
Keyword(s):  
Adult Female ◽  
Female Mouse ◽  
Synthetic Cannabinoid ◽  
Cp 55,940

scholarly journals Association of phosphatidylinositol 3-kinase with the insulin receptor: compartmentation in rat liver

2000 ◽  
Vol 279 (2) ◽  
pp. E266-E274 ◽  
Author(s):  
Paul G. Drake ◽  
Alejandro Balbis ◽  
Jiong Wu ◽  
John J. M. Bergeron ◽  
Barry I. Posner
Keyword(s):  
Plasma Membrane ◽  
Cell Surface ◽  
Insulin Receptor ◽  
Rat Liver ◽  
Intracellular Signaling ◽  
Kinase Activity ◽  
Glycogen Synthase ◽  
Metabolic Effects ◽  
Phosphatidylinositol 3 Kinase ◽  
Phosphatidylinositol 3

Phosphatidylinositol 3-kinase (PI 3-kinase) plays an important role in a variety of hormone and growth factor-mediated intracellular signaling cascades and has been implicated in the regulation of a number of metabolic effects of insulin, including glucose transport and glycogen synthase activation. In the present study we have examined 1) the association of PI 3-kinase with the insulin receptor kinase (IRK) in rat liver and 2) the subcellular distribution of PI 3-kinase-IRK interaction. Insulin treatment promoted a rapid and pronounced recruitment of PI 3-kinase to IRKs located at the plasma membrane, whereas no increase in association with endosomal IRKs was observed. In contrast to IRS-1-associated PI 3-kinase activity, association of PI 3-kinase with the plasma membrane IRK did not augment the specific activity of the lipid kinase. With use of the selective PI 3-kinase inhibitor wortmannin, our data suggest that the cell surface IRK β-subunit is not a substrate for the serine kinase activity of PI 3-kinase. The functional significance for the insulin-stimulated selective recruitment of PI 3-kinase to cell surface IRKs remains to be elucidated.

scholarly journals Single-cell sphingosine kinase activity measurements in primary leukemia

2014 ◽  
Vol 406 (27) ◽  
pp. 7027-7036 ◽  
Author(s):  
Alexandra J. Dickinson ◽  
Sally A. Hunsucker ◽  
Paul M. Armistead ◽  
Nancy L. Allbritton
Keyword(s):  
Single Cell ◽  
Kinase Activity ◽  
Sphingosine Kinase ◽  
Activity Measurements ◽  
Primary Leukemia

Characterization of sphingolipid long-chain base kinase in Arabidopsis thaliana

2000 ◽  
Vol 28 (6) ◽  
pp. 747-748 ◽  
Author(s):  
H. Nishiura ◽  
K. Tamura ◽  
Y. Morimoto ◽  
H. Imai
Keyword(s):  
Arabidopsis Thaliana ◽  
Kinase Activity ◽  
Sphingosine Kinase ◽  
Functional Identification ◽  
Chain Base ◽  
Sequence Identity ◽  
Gene Coding ◽  
Long Chain Base ◽  
Long Chain

Sphingolipid long-chain base (LCB) kinase catalyses the phosphorylation of sphingolipid LCB to form LCB 1-phosphate. Based on sequence identity to a murine sphingosine kinase (murine SPHK1a), we isolated and characterized a LCB kinase-like cDNA in Arabidopsis thaliana. The deduced amino acid sequence of the homologous cDNA shows several regions that are highly conserved in LCB kinases from mouse, yeast, human and Caenorhabditis elegans. These regions are not similar to those of other known kinase families. For a functional identification, the homologous cDNA from A. thaliana was expressed in Escherichia coli and LCB kinase activity was measured. The recombinant AtLcbk1 protein was found to utilize ATP and sphinganine. These results indicate the first identification of a gene coding for a LCB kinase in plants.

scholarly journals Early Activation of Sphingosine Kinase in Mast Cells and Recruitment to FcεRI Are Mediated by Its Interaction with Lyn Kinase

2004 ◽  
Vol 24 (19) ◽  
pp. 8765-8777 ◽  
Author(s):  
Nicole Urtz ◽  
Ana Olivera ◽  
Elisa Bofill-Cardona ◽  
Robert Csonga ◽  
Andreas Billich ◽  
...  
Keyword(s):  
Mast Cells ◽  
Tyrosine Kinase ◽  
Kinase Activity ◽  
Immunoglobulin E ◽  
Sphingosine Kinase ◽  
Lipid Kinase ◽  
Lyn Kinase ◽  
Sphingosine 1 Phosphate ◽  
High Affinity Receptor

ABSTRACT Sphingosine kinase has been recognized as an essential signaling molecule that mediates the intracellular conversion of sphingosine to sphingosine-1-phosphate. In mast cells, induction of sphingosine kinase and generation of sphingosine-1-phosphate have been linked to the initial rise in Ca2+, released from internal stores, and to degranulation. These events either precede or are concomitant with the activation of phospholipase C-γ and the generation of inositol trisphosphate. Here we show that sphingosine kinase type 1 (SPHK1) interacts directly with the tyrosine kinase Lyn and that this interaction leads to the recruitment of this lipid kinase to the high-affinity receptor for immunoglobulin E (FcεRI). The interaction of SPHK1 with Lyn caused enhanced lipid and tyrosine kinase activity. After FcεRI triggering, enhanced sphingosine kinase activity was associated with FcεRI in sphingolipid-enriched rafts of mast cells. Bone marrow-derived mast cells from Lyn−/ − mice, compared to syngeneic wild-type cells, were defective in the initial induction of SPHK1 activity, and the defect was overcome by retroviral Lyn expression. These findings position the activation of SPHK1 as an FcεRI proximal event.

scholarly journals The Human Semaphorin-like Leukocyte Cell Surface Molecule CD100 Associates with a Serine Kinase Activity

1997 ◽  
Vol 272 (38) ◽  
pp. 23515-23520 ◽  
Author(s):  
Abdellah Elhabazi ◽  
Valérie Lang ◽  
Cécile Hérold ◽  
Gordon J. Freeman ◽  
Armand Bensussan ◽  
...  
Keyword(s):  
Cell Surface ◽  
Kinase Activity ◽  
Surface Molecule ◽  
Serine Kinase ◽  
Cell Surface Molecule

scholarly journals Epithelial cell extrusion requires the sphingosine-1-phosphate receptor 2 pathway

2011 ◽  
Vol 193 (4) ◽  
pp. 667-676 ◽  
Author(s):  
Yapeng Gu ◽  
Tetyana Forostyan ◽  
Roger Sabbadini ◽  
Jody Rosenblatt
Keyword(s):  
Stem Cells ◽  
Epithelial Cell ◽  
Kinase Activity ◽  
Apoptotic Cell ◽  
Sphingosine Kinase ◽  
Live Cells ◽  
Sphingosine 1 Phosphate ◽  
A Cell ◽  
Dying Cells ◽  
Cell Extrusion

To maintain an intact barrier, epithelia eliminate dying cells by extrusion. During extrusion, a cell destined for apoptosis signals its neighboring cells to form and contract a ring of actin and myosin, which squeezes the dying cell out of the epithelium. Here, we demonstrate that the signal produced by dying cells to initiate this process is sphingosine-1-phosphate (S1P). Decreasing S1P synthesis by inhibiting sphingosine kinase activity or by blocking extracellular S1P access to its receptor prevented apoptotic cell extrusion. Extracellular S1P activates extrusion by binding the S1P2 receptor in the cells neighboring a dying cell, as S1P2 knockdown in these cells or its loss in a zebrafish mutant disrupted cell extrusion. Because live cells can also be extruded, we predict that this S1P pathway may also be important for driving delamination of stem cells during differentiation or invasion of cancer cells.

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