NAADP mobilizes Ca2+ from a thapsigargin-sensitive store in the nuclear envelope by activating ryanodine receptors

Julia V. Gerasimenko, Yoshio Maruyama, Kojiro Yano, Nick J. Dolman, Alexei V. Tepikin, Ole H. Petersen, Oleg V. Gerasimenko

Research output: Contribution to journalArticle

181 Citations (Scopus)

Abstract

Ca2+ release from the envelope of isolated pancreatic acinar nuclei could be activated by nicotinic acid adenine dinucleotide phosphate (NAADP) as well as by inositol 1,4,5-trisphosphate (IP3) and cyclic ADP-ribose (cADPR). Each of these agents reduced the Ca2+ concentration inside the nuclear envelope, and this was associated with a transient rise in the nucleoplasmic Ca2+ concentration. NAADP released Ca2+ from the same thapsigargin-sensitive pool as IP 3. The NAADP action was specific because, for example, nicotineamide adenine dinucleotide phosphate was ineffective. The Ca2+ release was unaffected by procedures interfering with acidic organelles (bafilomycin, brefeldin, and nigericin). Ryanodine blocked the Ca2+-releasing effects of NAADP, cADPR, and caffeine, but not IP3. Ruthenium red also blocked the NAADP-elicited Ca2+ release. IP3 receptor blockade did not inhibit the Ca2+ release elicited by NAADP or cADPR. The nuclear envelope contains ryanodine and IP3 receptors that can be activated separately and independently; the ryanodine receptors by either NAADP or cADPR, and the IP3 receptors by IP3.

Original languageEnglish
Pages (from-to)271-282
Number of pages12
JournalJournal of Cell Biology
Volume163
Issue number2
DOIs
Publication statusPublished - 2003 Oct 27

Keywords

  • Acinar cells
  • Calcium
  • Cyclic ADP-ribose
  • IP
  • Pancreas

ASJC Scopus subject areas

  • Cell Biology

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