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  • CLU (clusterin) and PPARGC1A/PGC1α coordinately control mitophagy and mitochondrial biogenesis for oral cancer cell survival.

CLU (clusterin) and PPARGC1A/PGC1α coordinately control mitophagy and mitochondrial biogenesis for oral cancer cell survival.

Autophagy (2024-03-07)
Prakash P Praharaj, Srimanta Patra, Amruta Singh, Debasna P Panigrahi, Hwa Y Lee, Mohammad F Kabir, Muhammad K Hossain, Samir K Patra, Birija S Patro, Shankargouda Patil, Daniel J Klionsky, Han J Chae, Sujit K Bhutia
ZUSAMMENFASSUNG

Mitophagy involves the selective elimination of defective mitochondria during chemotherapeutic stress to maintain mitochondrial homeostasis and sustain cancer growth. Here, we showed that CLU (clusterin) is localized to mitochondria to induce mitophagy controlling mitochondrial damage in oral cancer cells. Moreover, overexpression and knockdown of CLU establish its mitophagy-specific role, where CLU acts as an adaptor protein that coordinately interacts with BAX and LC3 recruiting autophagic machinery around damaged mitochondria in response to cisplatin treatment. Interestingly, CLU triggers class III phosphatidylinositol 3-kinase (PtdIns3K) activity around damaged mitochondria, and inhibition of mitophagic flux causes the accumulation of excessive mitophagosomes resulting in reactive oxygen species (ROS)-dependent apoptosis during cisplatin treatment in oral cancer cells. In parallel, we determined that PPARGC1A/PGC1α (PPARG coactivator 1 alpha) activates mitochondrial biogenesis during CLU-induced mitophagy to maintain the mitochondrial pool. Intriguingly, PPARGC1A inhibition through small interfering RNA (siPPARGC1A) and pharmacological inhibitor (SR-18292) treatment counteracts CLU-dependent cytoprotection leading to mitophagy-associated cell death. Furthermore, co-treatment of SR-18292 with cisplatin synergistically suppresses tumor growth in oral cancer xenograft models. In conclusion, CLU and PPARGC1A are essential for sustained cancer cell growth by activating mitophagy and mitochondrial biogenesis, respectively, and their inhibition could provide better therapeutic benefits against oral cancer.

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Proteasehemmer-Cocktail, for use with mammalian cell and tissue extracts, DMSO solution
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Phosphatasehemmer-Cocktail 3, DMSO solution
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N-Acetyl-L-Cystein, BioReagent, suitable for cell culture
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cis-Diamminplatin(II)-dichlorid, crystalline
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MitoTEMPO, ≥98% (HPLC)
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Anti-LC3B in Kaninchen hergestellte Antikörper, ~1 mg/mL, affinity isolated antibody, buffered aqueous solution
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Bafilomycin A1, Streptomyces griseus, Bafilomycin A1, CAS 88899-55-2, acts as a highly potent and specific inhibitor of vacuolar-type H+-ATPase (Ki = 500 pM). Blocks the fusion of autophagosome with lysosome.
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Anti-Kaninchen-IgG (Gesamtmolekül)-FITC in Ziege hergestellte Antikörper, affinity isolated antibody, buffered aqueous solution
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SR-18292 Maleate, ≥98% (HPLC)