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CD38 : a NAADP degrading enzyme

Schmid, Frederike (author)
University Medical Centre Hamburg-Eppendorf, Germany
Bruhn, Sören, 1976- (author)
University Medical Centre Hamburg-Eppendorf, Germany
Weber, Karin (author)
University Medical Centre Hamburg-Eppendorf, Germany
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Mitrücker, Hans (author)
University Medical Centre Hamburg-Eppendorf, Germany
Guse, Andreas (author)
University Medical Centre Hamburg-Eppendorf, Germany
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 (creator_code:org_t)
2011-10-19
2011
English.
In: FEBS Letters. - : Elsevier. - 0014-5793 .- 1873-3468. ; 585:22, s. 3544-3548
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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 NAADPdegrading rather than a NAADP forming enzyme, perhaps avoiding desensitizing NAADP levels in intact cells.

Keyword

Calcium signalling; NAADP; CD38; Jurkat T lymphocyte

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