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. 2020 Jun 16;10:915. doi: 10.3389/fonc.2020.00915

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Copyright © 2020 Nie, Qian, Shi, Li, Peng, Ding, Zhang, Zhang, Xu, Lv, Wang, Friess, Kong, Zou and Shen.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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ALDH1A3 promotes glycolysis by regulating the expression of HK2. (A) The knockdown efficacy of HK2 in ALDH1A3-overexpression cells (M24 and M31) was guaranteed at both mRNA and protein level. (B–D) After HK2 was knocked down in M24 cells, glucose uptake, lactate production and ATP production decreased in return. (E) Knockdown of HK2 inhibited PI3K/AKT/mTOR signaling in M24 cells. (F) The migration ability of ALDH1A3 could be impaired by HK2 knockdown in M24 cells. (G) In PDAC tissues, HK2 immunostaining signals were primarily detected in the cytoplasm. Bar: 20 μm. (H,I) The expression of HK2 was higher in ALDH1A3-positive PDAC tissues and correlated positively with the expression of ALDH1A3 in human PDAC tumor tissues. (J) The PDAC patients with both ALDH1A3 and HK2 positive expression suffered from poorer overall survival than that with both ALDH1A3 and HK2 negative expression (p = 0.0202).