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Full-Text Articles in Social and Behavioral Sciences
A Glu-496 To Ala Polymorphism Leads To Loss Of Function Of The Human P2x7 Receptor, Ben J. Gu, Weiyi Zhang, Rebecca A. Worthington, Ronald Sluyter, L Phuong Dao-Ung, Stephen Petrou, J A. Barden, James Wiley
A Glu-496 To Ala Polymorphism Leads To Loss Of Function Of The Human P2x7 Receptor, Ben J. Gu, Weiyi Zhang, Rebecca A. Worthington, Ronald Sluyter, L Phuong Dao-Ung, Stephen Petrou, J A. Barden, James Wiley
Faculty of Science - Papers (Archive)
P2X(7) receptor is a ligand-gated cation-selective channel that mediates ATP-induced apoptosis of cells of the immune system. We and others have shown that P2X(7) is nonfunctional both in lymphocytes and monocytes from some subjects. To study a possible genetic basis we sequenced DNA coding for the carboxyl-terminal tail of P2X(7). In 9 of 45 normal subjects a heterozygous nucleotide substitution (1513A-->C) was found, whereas 1 subject carried the homozygous substitution that codes for glutamic acid to alanine at amino acid position 496. Surface expression of P2X(7) on lymphocytes was not affected by this E496A polymorphism, demonstrated both by confocal …
Detection Of P2x Purinergic Receptors On Human B Lymphocytes, Ronald Sluyter, J A. Barden, James Wiley
Detection Of P2x Purinergic Receptors On Human B Lymphocytes, Ronald Sluyter, J A. Barden, James Wiley
Faculty of Science - Papers (Archive)
B lymphocytes are known to synthesise the P2X(7) subtype of the P2X purinergic receptor family; however, the identification of the other six P2X subtypes on these cells has been limited by the absence of specific antibodies. In this study, we used a panel of anti-P2X polyclonal antibodies and confocal microscopy to examine the presence of each P2X receptor on human B lymphocytes. We observed that P2X(1), P2X(2), P2X(4) and P2X(7) subtypes, but not P2X(3), P2X(5) and P2X(6) subtypes, are present on B lymphocytes.