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Targeting ER-Golgi Homeostasis in an Advantageous Therapeutic Strategy in Lung Cancer

NCT01270399 · Status: UNKNOWN · Type: OBSERVATIONAL · Enrollment: 20

Last updated 2012-10-30

No results posted yet for this study

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.

Conditions

  • The Combined Effect of Hsp90 Inhibitor and HDAC/Proteasome Inhibitors on Lung Cancer Cell Fate and ER-Golgi Homeostasis Will be Examined.

Sponsors & Collaborators

  • Meir Medical Center

    lead OTHER

Eligibility

Min Age
18 Years
Sex
ALL
Healthy Volunteers
No

Timeline & Regulatory

Start
2011-01-31
Primary Completion
2013-01-31
Completion
2013-01-31

Countries

  • Israel

Study Locations

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Read the full study record

This page highlights key information. For complete eligibility criteria, study locations, investigator contacts, and the full protocol, visit the original record on ClinicalTrials.gov.

View NCT01270399 on ClinicalTrials.gov