Coffee Induces Autophagy in Vivo

Cell Cycle. 2014;13(12):1987-94. doi: 10.4161/cc.28929. Epub 2014 Apr 25.

Abstract

Epidemiological studies and clinical trials revealed that chronic consumption coffee is associated with the inhibition of several metabolic diseases as well as reduction in overall and cause-specific mortality. We show that both natural and decaffeinated brands of coffee similarly rapidly trigger autophagy in mice. One to 4 h after coffee consumption, we observed an increase in autophagic flux in all investigated organs (liver, muscle, heart) in vivo, as indicated by the increased lipidation of LC3B and the reduction of the abundance of the autophagic substrate sequestosome 1 (p62/SQSTM1). These changes were accompanied by the inhibition of the enzymatic activity of mammalian target of rapamycin complex 1 (mTORC1), leading to the reduced phosphorylation of p70(S6K), as well as by the global deacetylation of cellular proteins detectable by immunoblot. Immunohistochemical analyses of transgenic mice expressing a GFP-LC3B fusion protein confirmed the coffee-induced relocation of LC3B to autophagosomes, as well as general protein deacetylation. Altogether, these results indicate that coffee triggers 2 phenomena that are also induced by nutrient depletion, namely a reduction of protein acetylation coupled to an increase in autophagy. We speculate that polyphenols contained in coffee promote health by stimulating autophagy.

Keywords: acetyl-coenzyme A; acetylation; mTOR; macroautophagy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Adaptor Proteins, Signal Transducing / metabolism
  • Animals
  • Autophagy*
  • Coffee / metabolism*
  • Female
  • Liver / metabolism
  • Mechanistic Target of Rapamycin Complex 1
  • Mice, Inbred C57BL
  • Multiprotein Complexes / metabolism
  • Muscle, Skeletal / metabolism
  • Myocardium / metabolism
  • Phagosomes / metabolism
  • TOR Serine-Threonine Kinases / metabolism
  • Transcription Factors / metabolism

Substances

  • Adaptor Proteins, Signal Transducing
  • Coffee
  • Gtf2h1 protein, mouse
  • Multiprotein Complexes
  • Transcription Factors
  • p70 Jak2-interacting protein, mouse
  • TOR Serine-Threonine Kinases
  • Mechanistic Target of Rapamycin Complex 1