کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2048709 | 1074093 | 2011 | 5 صفحه PDF | دانلود رایگان |
The role of the multifunctional enzyme CD38 in formation of the Ca2+-mobilizing second messenger nicotinic acid adenine dinucleotide phosphate (NAADP) was investigated. Gene silencing of CD38 did neither inhibit NAADP synthesis in intact Jurkat T cells nor in thymus or spleen obtained from CD38 knock out mice. In vitro, both NAADP formation by base-exchange and degradation to 2-phospho adenosine diphosphoribose were efficiently decreased. Thus in vivo CD38 appears to be a NAADP degrading rather than a NAADP forming enzyme, perhaps avoiding desensitizing NAADP levels in intact cells.
► We studied the role of CD38 in formation of the second messenger NAADP.
► We used gene silencing and CD38 KO mice to show a lack of inhibition of NAADP synthesis.
► We conclude that CD38 appears to be a NAADP degrading enzyme in intact cells.
Journal: FEBS Letters - Volume 585, Issue 22, 16 November 2011, Pages 3544–3548