Coffee induces autophagy in vivo.
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.
Equipe 11 labellisée par la Ligue Nationale Contre le Cancer; INSERM U1138; Centre de Recherche des Cordeliers; Paris, France; Metabolomics and Molecular Cell Biology Platforms; Gustave Roussy; Villejuif, France; Université de Paris Sud; Villejuif, France.
Federico
F
Pietrocola
Equipe 11 labellisée par la Ligue Nationale Contre le Cancer; INSERM U1138; Centre de Recherche des Cordeliers; Paris, France; Metabolomics and Molecular Cell Biology Platforms; Gustave Roussy; Villejuif, France; Université de Paris Sud; Villejuif, France; Directorate of Medical Sciences; Government College University; Faisalabad, Pakistan.
Shoaib Ahmad
SA
Malik
Equipe 11 labellisée par la Ligue Nationale Contre le Cancer; INSERM U1138; Centre de Recherche des Cordeliers; Paris, France; Metabolomics and Molecular Cell Biology Platforms; Gustave Roussy; Villejuif, France.
Guillermo
G
Mariño
Equipe 11 labellisée par la Ligue Nationale Contre le Cancer; INSERM U1138; Centre de Recherche des Cordeliers; Paris, France; Metabolomics and Molecular Cell Biology Platforms; Gustave Roussy; Villejuif, France; Université de Paris Sud; Villejuif, France.
Erika
E
Vacchelli
INSERM U1015; Gustave Roussy; Villejuif, France.
Laura
L
Senovilla
Equipe 11 labellisée par la Ligue Nationale Contre le Cancer; INSERM U1138; Centre de Recherche des Cordeliers; Paris, France; Metabolomics and Molecular Cell Biology Platforms; Gustave Roussy; Villejuif, France.
Kariman
K
Chaba
Equipe 11 labellisée par la Ligue Nationale Contre le Cancer; INSERM U1138; Centre de Recherche des Cordeliers; Paris, France; Metabolomics and Molecular Cell Biology Platforms; Gustave Roussy; Villejuif, France.
Mireia
M
Niso-Santano
Equipe 11 labellisée par la Ligue Nationale Contre le Cancer; INSERM U1138; Centre de Recherche des Cordeliers; Paris, France; Metabolomics and Molecular Cell Biology Platforms; Gustave Roussy; Villejuif, France.
Maria Chiara
MC
Maiuri
Institute of Molecular Biosciences; University of Graz; Graz, Austria.
Frank
F
Madeo
Equipe 11 labellisée par la Ligue Nationale Contre le Cancer; INSERM U1138; Centre de Recherche des Cordeliers; Paris, France; Metabolomics and Molecular Cell Biology Platforms; Gustave Roussy; Villejuif, France; Pôle de Biologie; Hôpital Européen Georges Pompidou; AP-HP; Paris, France; Université Paris Descartes; Sorbonne Paris Cité; Paris, France.
Guido
G
Kroemer
D000107:Acetylation; D048868:Adaptor Proteins, Signal Transducing / Q000378:metabolism; D000818:Animals; D001343:Autophagy; D003069:Coffee / Q000378:metabolism*; D005260:Female; D008099:Liver / Q000378:metabolism; D000076222:Mechanistic Target of Rapamycin Complex 1; D008810:Mice, Inbred C57BL; D046912:Multiprotein Complexes / Q000378:metabolism; D018482:Muscle, Skeletal / Q000378:metabolism; D009206:Myocardium / Q000378:metabolism; D010588:Phagosomes / Q000378:metabolism; D058570:TOR Serine-Threonine Kinases / Q000378:metabolism; D051758:Transcription Factor TFIIH; D014157:Transcription Factors / Q000378:metabolism
D048868:Adaptor Proteins, Signal Transducing; D003069:Coffee; C490981:Gtf2h1 protein, mouse; D046912:Multiprotein Complexes; D014157:Transcription Factors; C467906:p70 Jak2-interacting protein, mouse; D051758:Transcription Factor TFIIH; D000076222:Mechanistic Target of Rapamycin Complex 1; D058570:TOR Serine-Threonine Kinases
acetyl-coenzyme A; acetylation; mTOR; macroautophagy