Nicotinamide phosphoribosyltransferase regulates cell survival through autophagy in cardiomyocytes

Chiao Po Hsu, Nirmala Hariharan, Ralph R. Alcendor, Shinichi Oka, Junichi Sadoshima

Research output: Contribution to journalArticle

31 Scopus citations

Abstract

Nicotinamide adenine dinucleotide (NAD+) acts as a transfer molecule for electrons, thereby acting as a key cofactor for energy production. NAD+ also serves as a substrate for cellular enzymes, including poly (ADPribose) polymerase (PARP)-1 and Sirt1. Activation of PARP-1 by DNA damage depletes the cellular pool of NAD+, leading to necrotic cell death. NAD+ in the nucleus enhances the activity of Sirt1, thereby modulating transcription. NAD+ is either synthesized de novo from amino acids, namely tryptophan and aspartic acid, or resynthesized from NAD + metabolites, such as nicotinamide (NAM), through the salvage pathway. NAM phosphoribosyltransferase (Nampt) is a rate-limiting enzyme in the NAD+ salvage pathway. We have recently demonstrated that Nampt is an important regulator of NAD+ and autophagy in cardiomyocytes. Here we discuss the role of Nampt in regulating autophagy and potential mechanisms by which NAD+ regulates autophagy in the heart.

Original languageEnglish (US)
Pages (from-to)1229-1231
Number of pages3
JournalAutophagy
Volume5
Issue number8
DOIs
StatePublished - Nov 16 2009
Externally publishedYes

Keywords

  • Autophagy
  • Ischemia
  • Longevity factor
  • Nampt
  • Sirt1

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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