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- W2085333846 abstract "Abstract Extracellular ATP has been shown to induce apoptotic death of many cell types of hematopoietic origin. This action of ATP is mediated via activation of P2X 7 purinergic receptors, which show the unusual property of time‐dependent channel dilation to accept permeants as large as ethidium cation (314 Da). P2X 7 function, measured by area under the ATP‐induced ethidium uptake curve, was 5‐fold greater for monocytes than lymphocytes, while polymorphs and platelets showed no ethidium uptake. Expression of P2X 7 receptor, measured by the binding of a monoclonal antibody, was also 5‐fold greater on monocytes than lymphocytes. However, in some subjects, both normal and with chronic lymphocytic leukemia, the P2X 7 receptor was nonfunctional despite good expression of P2X 7 protein. Three single nucleotide polymorphisms were found in the P2X 7 cDNA coding region, one of which correlated with P2X 7 function. Thus, the homozygous substitution of alanine for glutamic acid at amino acid 496 led to complete loss of function of the P2X 7 receptor, while the heterozygous polymorphism gave function half that of the germline P2X 7 receptor. Drug Dev. Res. 53:72–76, 2001. © 2001 Wiley‐Liss, Inc." @default.
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- W2085333846 date "2001-06-01" @default.
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- W2085333846 title "Genetic polymorphisms of the human P2X<sub>7</sub> receptor and relationship to function" @default.
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- W2085333846 doi "https://doi.org/10.1002/ddr.1173" @default.
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