A truncation variant of the cation channel P2RX5 is upregulated during T cell activation
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A truncation variant of the cation channel P2RX5 is upregulated during T cell activation. / Abramowski, Pierre; Ogrodowczyk, Christoph; Martin, Roland; Pongs, Olaf.
In: PLOS ONE, Vol. 9, No. 9, 02.09.2014, p. e104692.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - A truncation variant of the cation channel P2RX5 is upregulated during T cell activation
AU - Abramowski, Pierre
AU - Ogrodowczyk, Christoph
AU - Martin, Roland
AU - Pongs, Olaf
PY - 2014/9/2
Y1 - 2014/9/2
N2 - Members of the P2X family of ligand-gated cation channels (P2RX) are expressed by various cell types including neurons, smooth- and cardiac muscle cells, and leukocytes. The channels mediate signalling in response to extracellular ATP. Seven subunit isoforms (P2RX1-P2RX7) have been identified and these can assemble as homo- and heterotrimeric molecules. In humans, P2RX5 exists as a natural deletion mutant lacking amino acids 328-349 of exon 10, which are part of transmembrane (TM) 2 and pre-TM2 regions in other organisms like rat, chicken and zebrafish. We show that P2RX5 gene expression of human T lymphocytes is upregulated during activation. P2RX5 is recruited to the cell surface. P2RX5-siRNA-transfected CD4+ T cells produced twofold more IL-10 than controls. Surface and intracellular P2RX5 expression was upregulated in activated antigen-specific CD4+ T cell clones. These data indicate a functional role of the human P2RX5 splice variant in T cell activation and immunoregulation.
AB - Members of the P2X family of ligand-gated cation channels (P2RX) are expressed by various cell types including neurons, smooth- and cardiac muscle cells, and leukocytes. The channels mediate signalling in response to extracellular ATP. Seven subunit isoforms (P2RX1-P2RX7) have been identified and these can assemble as homo- and heterotrimeric molecules. In humans, P2RX5 exists as a natural deletion mutant lacking amino acids 328-349 of exon 10, which are part of transmembrane (TM) 2 and pre-TM2 regions in other organisms like rat, chicken and zebrafish. We show that P2RX5 gene expression of human T lymphocytes is upregulated during activation. P2RX5 is recruited to the cell surface. P2RX5-siRNA-transfected CD4+ T cells produced twofold more IL-10 than controls. Surface and intracellular P2RX5 expression was upregulated in activated antigen-specific CD4+ T cell clones. These data indicate a functional role of the human P2RX5 splice variant in T cell activation and immunoregulation.
U2 - 10.1371/journal.pone.0104692
DO - 10.1371/journal.pone.0104692
M3 - SCORING: Journal article
C2 - 25181038
VL - 9
SP - e104692
JO - PLOS ONE
JF - PLOS ONE
SN - 1932-6203
IS - 9
ER -
