Ion channels activated by inositol 1,4,5-trisphosphate in plasma membrane of human T-lymphocytes

Nature ◽  
1987 ◽  
Vol 326 (6110) ◽  
pp. 301-304 ◽  
Author(s):  
Miyuki Kuno ◽  
Phyllis Gardner
1995 ◽  
Vol 38 (11) ◽  
pp. 1877-1883 ◽  
Author(s):  
William F. Michne ◽  
Joseph W. Guiles ◽  
Adi M. Treasurywala ◽  
Laurie A. Castonguay ◽  
Carolyn A. Weigelt ◽  
...  

2004 ◽  
Vol 67 (4) ◽  
pp. 1034-1044 ◽  
Author(s):  
Miklós Bagdáany ◽  
Cesar V. F. Batista ◽  
Norma A. Valdez-Cruz ◽  
Sándor Somodi ◽  
Ricardo C. Rodriguez de la Vega ◽  
...  

2008 ◽  
Vol 183 (6) ◽  
pp. i15-i15
Author(s):  
Olga Antón ◽  
Alicia Batista ◽  
Jaime Millán ◽  
Laura Andrés-Delgado ◽  
Rosa Puertollano ◽  
...  

2010 ◽  
Vol 88 (4) ◽  
pp. 487-496 ◽  
Author(s):  
Claudine Irles ◽  
Joel Arias-Martinez ◽  
José Guzmán-Bárcenas ◽  
Alicia Ortega

Uncovering the plasma membrane distribution of tyrosine kinase Lck is crucial to understanding T lymphocyte triggering. Several studies of Lck species partitioning have given contradictory results. We decided to re-address this point by using phospho-specific antibodies to characterize active and inactive Lck partitioning in raft and non-raft membranes from primary human peripheral blood T lymphocytes. We show that most inactive Lck was localized in rafts and was associated with nearly all CD4 coreceptors and its negative regulator Csk in resting cells, while T cell receptor (TCR) engagement promoted a sustained dephosphorylation of inactive Lck. In contrast, active Lck had a more discrete distribution interacting with only a small number of CD4 coreceptors, and the kinase showed a rapid and short phosphorylation after TCR triggering. The differences in distribution and kinetics may be related to T lymphocyte signalling threshold modulation by Lck species and suggest how TCR triggering is first initiated. This study furthers our knowledge of the TCR activation model in primary human T lymphocytes.


Blood ◽  
1996 ◽  
Vol 87 (2) ◽  
pp. 682-690 ◽  
Author(s):  
OR Baricordi ◽  
D Ferrari ◽  
L Melchiorri ◽  
P Chiozzi ◽  
S Hanau ◽  
...  

We investigated the effect of pharmacologic modulation of the ATP receptor on intracellular ion changes and proliferative response of human peripheral blood lymphocytes (PBLs) and purified T lymphocytes. Extracellular ATP (ATPe) triggered in these cells an increase in the cytoplasmic Ca2+ concentration ([Ca2+]i) and plasma membrane depolarization. Whereas both Ca2+ release from intracellular stores and influx across the plasma membrane were detected in the whole PBL population, only Ca2+ influx was observed in T cells. In the presence of near physiologic extracellular Na+ concentrations (125 mmol/L), Ca2+ permeability through the ATPe-gated channel was very low, suggesting a higher selectivity for monovalent over divalent cations. The selective P2Z agonist benzoylbenzoic ATP (BzATP) increased [Ca2+]i in the presence but not the absence of extracellular Ca2+ and also caused plasma membrane depolarization. The covalent blocker oxidized ATP (oATP), an inhibitor of P2X and P2Z receptors, prevented Ca2+ influx and plasma membrane depolarization, but had no effect on Ca2+ release from stores. Stimulation with ATPe alone had no significant effects on PBL 3H-thymidine incorporation. On the contrary, ATPe or BzATP had a synergistic effect on DNA synthesis stimulated by selective T-cell mitogens such as phytohemagglutinin, anti-CD3 monoclonal antibody, or allogenic PBLs (mixed lymphocyte cultures). Treatment with oATP inhibited mitogenic stimulation by these receptor-directed agents but not by the combined application of the Ca2+ ionophore ionomycin and phorbol myristate acetate. Interleukin-2 partially relieved inhibition by oATP. These results suggest that human T lymphocytes express a plasma membrane channel gated by ATPe that is involved in mitogenic stimulation.


2016 ◽  
Vol 32 (7) ◽  
pp. 658-659
Author(s):  
Charlotte Mariani-Floderer ◽  
Jean-Baptiste Sibarita ◽  
Cyril Favard ◽  
Delphine M. Muriaux

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