دورية أكاديمية
Rectification of ATP-gated current of rat P2X2 and P2X7 receptors depends on the cytoplasmic N-terminus.
| العنوان: | Rectification of ATP-gated current of rat P2X2 and P2X7 receptors depends on the cytoplasmic N-terminus. |
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| المؤلفون: | Migita K; Department of Drug Informatics, Faculty of Pharmaceutical Sciences, Fukuoka University, Fukuoka, 814-0180, Japan. Electronic address: migitak@fukuoka-u.ac.jp., Oyabu K; Department of Drug Informatics, Faculty of Pharmaceutical Sciences, Fukuoka University, Fukuoka, 814-0180, Japan., Terada K; Division of Pharmacotherapeutics, Faculty of Pharmaceutical Sciences, Himeji Dokkyo University, Himeji, 670-8524, Japan. |
| المصدر: | Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2023 Dec 25; Vol. 688, pp. 149213. Date of Electronic Publication: 2023 Nov 07. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Country of Publication: United States NLM ID: 0372516 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1090-2104 (Electronic) Linking ISSN: 0006291X NLM ISO Abbreviation: Biochem Biophys Res Commun Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: <2002- >: San Diego, CA : Elsevier Original Publication: New York, Academic Press. |
| مواضيع طبية MeSH: | Receptors, Purinergic P2X7*/genetics , Adenosine Triphosphate*, Rats ; Animals ; Cytoplasm ; Cytosol ; Receptors, Purinergic P2X2/genetics |
| مستخلص: | The phenotypes of ATP-gated currents thought ionotropic P2X channels depend on the composition of the oligomeric receptor. We constructed chimeric P2X2/P2X7 receptors to study the effect of cytoplasmic domains on rectification of current flow through the open channel. We found that the identity of the N-terminus determines the pattern of rectification, with chimeric receptors containing the N-terminus of the P2X2 receptor displaying inward rectification, and chimeric receptors containing the N-terminus of the P2X7 receptor displaying slightly outward rectification. In contrast, rectification of current through chimeric receptors with swapped C-termini always mimicked the wild-type receptor. Thus, our findings suggest that the N-terminus of P2X receptors regulate ion flow through the channel pore and are responsible in part for determining current rectification. Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. (Copyright © 2023 Elsevier Inc. All rights reserved.) |
| فهرسة مساهمة: | Keywords: N-terminus; P2X2 receptor; P2X7 receptor; Rectification |
| المشرفين على المادة: | 0 (Receptors, Purinergic P2X7) 8L70Q75FXE (Adenosine Triphosphate) 0 (Receptors, Purinergic P2X2) |
| تواريخ الأحداث: | Date Created: 20231117 Date Completed: 20231127 Latest Revision: 20231228 |
| رمز التحديث: | 20231229 |
| DOI: | 10.1016/j.bbrc.2023.149213 |
| PMID: | 37976814 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1090-2104 |
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| DOI: | 10.1016/j.bbrc.2023.149213 |