A truncation variant of the cation channel P2RX5 is upregulated during T cell activation.
PLoS One, 2014;9(9):e104692.
Abramowski P[1], Ogrodowczyk C[2], Martin R[3], Pongs O[4]
Affiliations
PMID: 25181038DOI: 10.1371/journal.pone.0104692
Impact factor: 3.752
Abstract
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.
MeSH terms
Alternative Splicing; Animals; CD4-Positive T-Lymphocytes; Cell Membrane; Cell Polarity; Clone Cells; Gene Expression Profiling; Gene Knockdown Techniques; HEK293 Cells; Humans; Interleukin-10; Lymphocyte Activation; Lymphocyte Subsets; Mutant Proteins; Protein Subunits; Protein Transport; RNA, Messenger; Receptors, Purinergic P2X5; Up-Regulation
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