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  • Inhibition of phospholipase D2 induces autophagy in colorectal cancer cells.

Inhibition of phospholipase D2 induces autophagy in colorectal cancer cells.

Experimental & molecular medicine (2014-12-06)
Won Chan Hwang, Mi Kyoung Kim, Ju Hyun Song, Kang-Yell Choi, Do Sik Min
ABSTRACT

Autophagy is a conserved lysosomal self-digestion process used for the breakdown of long-lived proteins and damaged organelles, and it is associated with a number of pathological processes, including cancer. Phospholipase D (PLD) isozymes are dysregulated in various cancers. Recently, we reported that PLD1 is a new regulator of autophagy and is a potential target for cancer therapy. Here, we investigated whether PLD2 is involved in the regulation of autophagy. A PLD2-specific inhibitor and siRNA directed against PLD2 were used to treat HT29 and HCT116 colorectal cancer cells, and both inhibition and genetic knockdown of PLD2 in these cells significantly induced autophagy, as demonstrated by the visualization of light chain 3 (LC3) puncta and autophagic vacuoles as well as by determining the LC3-II protein level. Furthermore, PLD2 inhibition promoted autophagic flux via the canonical Atg5-, Atg7- and AMPK-Ulk1-mediated pathways. Taken together, these results suggest that PLD2 might have a role in autophagy and that its inhibition might provide a new therapeutic basis for targeting autophagy.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Phospholipase D from Arachis hypogaea (peanut), Type II, lyophilized powder, ≥60 units/mg protein
Sigma-Aldrich
Phospholipase D from cabbage, Type IV, lyophilized powder, ≥100 units/mg solid
Sigma-Aldrich
Phospholipase D from Streptomyces sp., Type VII, lyophilized powder, ≥150 units/mg solid
Sigma-Aldrich
Phospholipase D from Streptomyces chromofuscus, ≥50,000 units/mL, buffered aqueous glycerol solution