The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
A Glu-496 to Ala Polymorphism Leads to Loss of Function of the Human P2X7 Receptor
Open accessAbstract
The 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 microscopy and immunofluorescent staining. Monocytes and lymphocytes from the E496A homozygote subject expressed nonfunctional receptor, whereas heterozygotes showed P2X(7) function that was half that of germline P2X(7). Results of transfection experiments showed that the mutant P2X(7) receptor was nonfunctional when expressed at low receptor density but regained function at a high receptor density. This density dependence of mutant P2X(7) function was also seen on differentiation of fresh monocytes to macrophages with interferon-gamma, which up-regulated mutant P2X(7) and partially restored its function. P2X(7)-mediated apoptosis of lymphocytes was impaired in homozygous mutant P2X(7) compared with germline (8.6 versus 35.2%). The data suggest that the glutamic acid at position 496 is required for optimal assembly of the P2X(7) receptor.
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Cites
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Cited by
Molecular Physiology of P2X Receptors
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The P2X7 Receptor in Infection and Inflammation
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The P2X7 Receptor: A Key Player in IL-1 Processing and Release
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Neutrophil P2X7 receptors mediate NLRP3 inflammasome-dependent IL-1β secretion in response to ATP
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Metadata
- Authors
- Gu, B. J., Zhang, W., Worthington, R. A., Sluyter, R., Dao-Ung, P., Petrou, S., Barden, J. A., & Wiley, J. S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-04
- Volume
- 276
- Issue
- 14
- Pages
- 11135-11142
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2126695278
- Cited by
- 313
- References
- 39
- FWCI
- 6.61
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Gu, B. J., Zhang, W., Worthington, R. A., Sluyter, R., Dao-Ung, P., Petrou, S., Barden, J. A., & Wiley, J. S. (2001). A Glu-496 to Ala Polymorphism Leads to Loss of Function of the Human P2X7 Receptor. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m010353200
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