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Association of p38MAPK‐p53‐Fas aggregation in S‐allyl cysteine mediated regulation of hepatocarcinoma
Author(s) -
Chatterjee Sujan,
Patra Debajyoti,
Chakraborti Udipta,
Sengupta Dipanwita,
Ghosh Pujita,
Basu Anupam,
Sadhukhan Gobinda Chandra,
Chowdhury Kaustav Dutta
Publication year - 2019
Publication title -
environmental toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.813
H-Index - 77
eISSN - 1522-7278
pISSN - 1520-4081
DOI - 10.1002/tox.22764
Subject(s) - apoptosis , fas ligand , fadd , phosphorylation , mapk/erk pathway , chemistry , programmed cell death , microbiology and biotechnology , cancer research , signal transduction , p38 mitogen activated protein kinases , protein kinase a , caspase , biology , biochemistry
Bioactive components of dietary phytochemicals have been reported to possess antitumor activities. Evidences suggested key role of stress responsive p38MAPK in the induction of nutraceuticals mediated apoptosis in hepatocellular carcinoma (HCC). Current study demonstrated detailed molecular bagatelle associated with p38 MAPK mediated effective suppression of cell growth both in HepG2 and chemically induced liver carcinoma after S‐allyl cysteine (SAC) treatment. SAC promoted p38MAPK activity responsible for p53 phosphorylation, its stabilization followed by nuclear translocation leading to induction in expression and oligomerization of Fas protein. Distinctive p38MAPK‐p53 axis dependent Fas‐FasL‐FADD mediated caspase activities along with perturbed cell cycling became normalized with continuation of SAC treatment for another month to diethylnitrosamine induced liver carcinoma. Co‐treatment with SB203580, the p38MAPK inhibitor, prevented pro‐apoptotic effect of SAC by altering p53 phosphorylation and death inducing signaling complex conformation in HepG2 and induced HCC. Collectively study suggested significant contribution of p38MAPK‐p53‐DISC‐Caspase pathway in the regulation of anti‐neoplastic activity of SAC against HCC.

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