The Combined Effect of Hsp90 Inhibitor and HDAC/Proteasome Inhibitors on Lung Cancer Cell Fate and ER-Golgi Homeostasis Will be Examined. Clinical Trial
Official title:
Targeting ER-Golgi Homeostasis in an Advantageous Therapeutic Strategy in Lung Cancer
Lung cancer remains the most common cause of cancer-related death in the world. The major
advances in treatment of lung cancer have brought only minor improvements in survival
therefore novel systemic treatment methods are urgently needed.
Protein levels are regulated by the protein homeostasis network that generates and protects
the protein fold (ER and Golgi included).
The heat shock protein 90 (Hsp90) is an essential molecular chaperon involved in the
posttranslational folding and stability of proteins. Hsp90 inhibition leads to accumulation
of unfolded proteins and ER stress. The therapeutic efficacy of such inhibition may be
augmented by co-administering it with other drugs that disrupt ER-Golgi homeostasis like
histone deacetylase (HDAC) or proteasome inhibitors. ER-Golgi homeostasis disruption affects
a wide network of proteins and pathways as such affords a systemic target. Thus, the
investigators aimed to examine the effect of combined treatment of Hsp90 antagonist with
proteasome or HDAC inhibitors on human lung cancer cell lines and primary cells.
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Observational Model: Case Control, Time Perspective: Prospective