The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
A Functional P2X7 Splice Variant with an Alternative Transmembrane Domain 1 Escapes Gene Inactivation in P2X7 Knock-out Mice
Open accessAbstract
The ATP-activated P2X7 receptor channel is involved in immune function and inflammatory pain and represents an important drug target. Here we describe a new P2X7 splice variant (P2X7(k)), containing an alternative intracellular N terminus and first transmembrane domain encoded by a novel exon 1 in the rodent P2rx7 gene. Whole cell patch clamp recordings of the rat isoform expressed in HEK293 cells revealed an 8-fold higher sensitivity to the agonist Bz-ATP and much slower deactivation kinetics when compared with the P2X7(a) receptor. Permeability measurements in Xenopus oocytes show a high permeability for N-methyl-D-glucamine immediately upon activation, suggesting that the P2X7(k) channel is constitutively dilated upon opening. The rates of agonist-induced dye uptake and membrane blebbing in HEK cells were also increased. PCR analyses and biochemical analysis by SDS-PAGE and BN-PAGE indicate that the P2X7(k) variant escapes gene deletion in one of the available P2X7(-/-) mice strains and is strongly expressed in the spleen. Taken together, we describe a novel P2X7 isoform with distinct functional properties that contributes to the diversity of P2X7 receptor signaling. Its presence in one of the P2X7(-/-) strains has important implications for our understanding of the role of this receptor in health and disease.
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Cites
Molecular Physiology of P2X Receptors
North, R. A. (2002) · Physiological Reviews · doi:10.1152/physrev.00015.2002 · Cited by 2,919
Reanalysis of P2X7Receptor Expression in Rodent Brain
Sim, J. A., Young, M. T., Sung, H.-Y., North, R. A., & Surprenant, A. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.1469-04.2004 · Cited by 264
Lucae, S., Salyakina, D., Barden, N., Harvey, M., Gagné, B., Labbé, M., Binder, E. B., Uhr, M., Paez-Pereda, M., Sillaber, I., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl166 · Cited by 261
Cited by
The P2X7 Receptor in Infection and Inflammation
Di Virgilio, F., Dal Ben, D., Sarti, A. C., Giuliani, A. L., & Falzoni, S. (2017) · Immunity · doi:10.1016/j.immuni.2017.06.020 · Cited by 1,267
Pathological pain and the neuroimmune interface
Grace, P. M., Hutchinson, M. R., Maier, S. F., & Watkins, L. R. (2014) · Nature Reviews Immunology · doi:10.1038/nri3621 · Cited by 932
Neutrophil P2X7 receptors mediate NLRP3 inflammasome-dependent IL-1β secretion in response to ATP
Karmakar, M., Katsnelson, M. A., Dubyak, G. R., & Pearlman, E. (2016) · Nature Communications · doi:10.1038/ncomms10555 · Cited by 450
P2X7 receptor: an emerging target in central nervous system diseases
Sperlágh, B., & Illes, P. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2014.08.002 · Cited by 390
Extracellular ATP mediates mast cell-dependent intestinal inflammation through P2X7 purinoceptors
Kurashima, Y., Amiya, T., Nochi, T., Fujisawa, K., Haraguchi, T., Iba, H., Tsutsui, H., Sato, S., Nakajima, S., Iijima, H., et al. (2012) · Nature Communications · doi:10.1038/ncomms2023 · Cited by 286
Metadata
- Authors
- Nicke, A., Kuan, Y.-H., Masin, M., Rettinger, J., Marquez-Klaka, B., Bender, O., Górecki, D. C., Murrell-Lagnado, R. D., & Soto, F.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-09
- Volume
- 284
- Issue
- 38
- Pages
- 25813-25822
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2022291383
- Cited by
- 187
- References
- 3
- FWCI
- 8.91
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Nicke, A., Kuan, Y.-H., Masin, M., Rettinger, J., Marquez-Klaka, B., Bender, O., Górecki, D. C., Murrell-Lagnado, R. D., & Soto, F. (2009). A Functional P2X7 Splice Variant with an Alternative Transmembrane Domain 1 Escapes Gene Inactivation in P2X7 Knock-out Mice. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m109.033134
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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