Targeting ER-Golgi Homeostasis in an Advantageous Therapeutic Strategy in Lung Cancer
- Conditions
- The Combined Effect of Hsp90 Inhibitor and HDAC/Proteasome Inhibitors on Lung Cancer Cell Fate and ER-Golgi Homeostasis Will be Examined.
- Registration Number
- NCT01270399
- Lead Sponsor
- Meir Medical Center
- Brief Summary
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.
- Detailed Description
Not available
Recruitment & Eligibility
- Status
- UNKNOWN
- Sex
- All
- Target Recruitment
- 20
- PATIENTS WITH PROVED DIAGNOSIS OF LUNG CARCINOMA THAT ARE CANDIDATS FOR RADICAL SURGICAL TREATMENT
- PATIENTS WITH SUSPICION FOR LUNG CARCINOMA WITHOUT PATHOLOGYCAL DIAFNOSIS BEFORE SURGERY
Study & Design
- Study Type
- OBSERVATIONAL
- Study Design
- Not specified
- Primary Outcome Measures
Name Time Method
- Secondary Outcome Measures
Name Time Method
Trial Locations
- Locations (1)
Meir Medical Center
🇮🇱Kfar Saba, Israel