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. 2018 Oct 18;19(10):3221. doi: 10.3390/ijms19103221

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© 2018 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Alpha-hederin (α-Hed) induced the increased number of autophagosomes in human non-small cell lung cancer (NSCLC) cells. (A) The chemical structure of α-Hed. (B,C) α-Hed promoted microtubule-associated protein light chain 3 (LC3)-II accumulation in a dose- and time-dependent manner. NCI-H1299 and NCI-H1650 cells were treated with α-Hed (12.5 μM) or bafilomycin A1(Baf, 0.1 μM) for the indicated time courses (C), or treated with α-Hed or Baf at the indicated doses for 24 h (B). LC3-II was quantified and the fold increase is presented. *** p < 0.001. (D) Effect of α-Hed on green fluorescent protein (GFP)-LC3 punctation. NCI-H1299 and NCI-H1650 cells were transiently transfected with GFP-LC3 plasmid, α-Hed (12.5 μM), Baf (0.1 μM) for 24 h, or with Hank’s balanced salt solution (HBSS) for 6 h. Typical images are shown.

Alpha-hederin (α-Hed) induced the increased number of autophagosomes in human non-small cell lung cancer (NSCLC) cells. (A) The chemical structure of α-Hed. (B,C) α-Hed promoted microtubule-associated protein light chain 3 (LC3)-II accumulation in a dose- and time-dependent manner. NCI-H1299 and NCI-H1650 cells were treated with α-Hed (12.5 μM) or bafilomycin A1(Baf, 0.1 μM) for the indicated time courses (C), or treated with α-Hed or Baf at the indicated doses for 24 h (B). LC3-II was quantified and the fold increase is presented. *** p < 0.001. (D) Effect of α-Hed on green fluorescent protein (GFP)-LC3 punctation. NCI-H1299 and NCI-H1650 cells were transiently transfected with GFP-LC3 plasmid, α-Hed (12.5 μM), Baf (0.1 μM) for 24 h, or with Hank’s balanced salt solution (HBSS) for 6 h. Typical images are shown.