Identification and characterization of splice variants of the human P2X7 ATP channel
Identification and characterization of splice variants of the human P2X7 ATP channel
复制标题
DOI：
10.1016/j.bbrc.2005.04.087
复制
发表时间：
2005-06-24
影响因子：
3.1
通讯作者：
Greenfeder, S
中科院分区：
文献类型：
--
作者：
Cheewatrakoolpong, B;Gilchrest, H;Greenfeder, S
P2 X7通道是配体门控离子通道的P2 X家族的成员，其响应于作为内源性激动剂的ATP。研究表明，P2 X7在炎症反应中具有潜在的关键作用，主要源于其在介导响应ATP的IL-1 β释放中的作用。我们报告了由选择性剪接引起的人P2 X7的七种变体的鉴定。将这些变体中的两种（一种缺乏第一跨膜结构域，第二种缺乏整个胞质尾区）与全长通道进行比较。实时PCR分析表明，这两种变体在各种组织中表达，并且胞质尾缺失变体高度表达。第一个跨膜结构域的缺失导致无功能通道。细胞质尾部的缺失不影响离子运动，但严重影响形成大孔和诱导半胱天冬酶活化的能力。(c)2005年爱思唯尔公司All rights reserved.
The P2X7 channel is a member of the P2X family of ligand-gated ion channels which respond to ATP as the endogenous agonist. Studies suggest that P2X7 has a potentially pivotal role in inflammatory responses largely stemming from its role in mediating the release of IL-1 beta in response to ATP. We report the identification of seven variants Of human P2X7 which result from alternative splicing. Two of these variants (one lacking the first transmembrane domain, the second lacking the entire cytoplasmic tail) were compared to the full-length channel. Real-time PCR analysis demonstrated that both variants were expressed in various tissues and that the cytoplasmic tail deleted variant is highly expressed. Deletion of the first transmembrane domain resulted in a non-functional channel. Deletion of the cytoplasmic tail did not affect ion movement but severely affected the ability to form a large pore and to induce activation of caspases. (c) 2005 Elsevier Inc. All rights reserved.