期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 457, 期 1, 页码 7-15出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2006.10.013
关键词
nucleoside triphosphate diphosphohydrolase 3 (NTPDase3); alternative splicing; biosynthetic processing; cellular trafficking; expression modulation; CD39L3
资金
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL059915, R01HL072382] Funding Source: NIH RePORTER
- NHLBI NIH HHS [R01 HL059915, R01 HL072382, HL59915, HL72882] Funding Source: Medline
Nucleoside triphosphate diphosphohydrolase 3 (NTPDase3) is a cell surface, membrane-bound enzyme that hydrolyzes extracellular nucleotides, thereby modulating purinergic signaling. An alternatively spliced variant of NTPDase3 was obtained and analyzed. This alternatively spliced variant, termed NTPDase3 beta, is produced through the use of an alternative terminal exon (exon 11) in place of the terminal exon (exon 12) in the full-length NTPDase3, now termed NTPDase3 alpha. This results in an expressed protein lacking the C-terminal cytoplasmic sequence, the C-terminal transmembrane helix, and apyrase conserved region 5. The cDNA encoding this truncated splice variant was detected in a human lung library by PCR. Like the full-length NTPDase3 alpha, the alternatively spliced NTPDase3 beta was expressed in COS cells after transfection, but only the full-length NTPDase3 alpha is enzymatically active and properly trafficked to the plasma membrane. However, when the truncated NTPDase3 beta was co-transfected with full-length NTPDase3 alpha, there was a significant reduction in the amount of NTPDase3 alpha that was properly processed and trafficked to the plasma membrane as active enzyme, indicating that the truncated form interferes with normal biosynthetic processing of the full-length enzyme. This suggests a role for the NTPDase3 beta variant in the regulation of NTPDase3 nucleotidase activity, and therefore the control of purinergic signaling, in those cells and tissues expressing both NTPDase3 alpha and NTPDase3 beta. (c) 2006 Elsevier Inc. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据