TAK1 is involved in sodium L-lactate-stimulated p38 signaling and promotes apoptosis

In the present study, we found that the phosphorylation of p38 mitogen-activated protein kinase (p38) was significantly increased in L-lactate-treated HeLa cells, which is under concentration- and time-dependent manner. The protein level of Bcl-2 was significantly reduced and Bax and C-caspase3 were...

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Bibliographic Details
Published in:Molecular and cellular biochemistry 2021-02, Vol.476 (2), p.873-882
Main Authors: Da, Qingen, Yan, Zilong, Li, Zhangfu, Han, Zhen, Ren, Mingming, Huang, Lei, Zhang, Xiaowei, Liu, Jikui, Wang, Tao
Format: Article
Language:English
Subjects:
Analysis
Apoptosis
BAX protein
Bcl-2 protein
Biochemistry
Biomedical and Life Sciences
c-Myc protein
Cardiology
FasL protein
Gene expression
Kinases
Lactates
Lactic acid
Life Sciences
MAP kinase
Medical Biochemistry
Myc protein
Oncology
Phosphorylation
Protein kinase
Protein kinases
Proteins
siRNA
TAK1 protein
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Summary:In the present study, we found that the phosphorylation of p38 mitogen-activated protein kinase (p38) was significantly increased in L-lactate-treated HeLa cells, which is under concentration- and time-dependent manner. The protein level of Bcl-2 was significantly reduced and Bax and C-caspase3 were significantly increased in L-lactate-treated cells. qRT-PCR analysis suggested that the expression level of apoptosis-related genes Bax , C-myc, and FasL were significantly upregulated by L-lactate treatment. In addition, p38 inhibitor SB203580 blocked the L-lactate-stimulated phosphorylation of p38 (p-p38) and apoptosis, which suggested that L-lactate-stimulated apoptosis may be related to the activation of p38. Moreover, TAK1 inhibitor Takinib reduced L-lactate-triggered phosphorylation of p38 and also apoptosis; however, ASK1 inhibitor NQDI-1 did not. Cells transfected with siRNA of TAK1(siTAK1) showed similar results with Takinib inhibitor. These results suggested that the L-lactate treatment elevated activation of p38 and apoptosis was related to TAK1. In this study, we suggested that TAK1 plays an important role in L-lactate-stimulated activation of p38 affecting apoptosis in HeLa cells.
ISSN:0300-8177
1573-4919
DOI:10.1007/s11010-020-03952-y