Targeting ER-Golgi Homeostasis in an Advantageous Therapeutic Strategy in Lung Cancer
NCT ID: NCT01270399
Last Updated: 2012-10-30
Study Results
The study team has not published outcome measurements, participant flow, or safety data for this trial yet. Check back later for updates.
Basic Information
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UNKNOWN
20 participants
OBSERVATIONAL
2011-01-31
2013-01-31
Brief Summary
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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
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Conditions
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Study Design
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CASE_CONTROL
PROSPECTIVE
Study Groups
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malignant neoplasm's cells
No interventions assigned to this group
natural cells
No interventions assigned to this group
Eligibility Criteria
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Inclusion Criteria
Exclusion Criteria
18 Years
ALL
No
Sponsors
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Meir Medical Center
OTHER
Responsible Party
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Locations
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Meir Medical Center
Kfar Saba, , Israel
Countries
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Facility Contacts
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Maya Gottfried, MD
Role: primary
Other Identifiers
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MMC10160-2010CTIL
Identifier Type: -
Identifier Source: org_study_id