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Binding partners for curcumin in human schwannoma cells: biologic implications
Laura S Angelo1, David S Maxwell, Ji Yuan Wu
1Department of Investigational Cancer Therapeutics, (Phase I Program), The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA. lsangelo39@gmail.com
Bioorganic & Medicinal Chemistry
|January 9, 2013
Summary
Curcumin, a cancer-fighting compound, interacts with heat shock proteins (hsp70 and hsp90) and other proteins. This interaction may explain how curcumin works against cancer cells, offering new therapeutic insights.
Area of Science:
- Biochemistry
- Molecular Biology
- Cancer Research
Background:
- Curcumin exhibits anti-inflammatory and anti-tumorigenic properties.
- Curcumin up-regulates heat shock protein 70 (hsp70) mRNA in cancer cells.
- Hsp70 can protect cancer cells from curcumin-induced apoptosis.
Purpose of the Study:
- To investigate direct interactions between curcumin and hsp70.
- To identify other binding partners of curcumin.
- To elucidate the molecular mechanisms of curcumin's anti-cancer effects.
Main Methods:
- Synthesis of biotinylated curcumin (bio-curcumin).
- Treatment of human schwannoma cells (HEI-193) with bio-curcumin.
- Affinity purification using avidin-coated beads and mass spectrometry for peptide sequencing.
Main Results:
- Biotinylated curcumin directly binds to hsp70 and hsp90.
- Additional binding partners identified include 3-phosphoglycerate dehydrogenase and a β-actin variant.
- These findings suggest multiple molecular targets for curcumin.
Conclusions:
- Curcumin interacts with multiple proteins, including heat shock proteins, in cancer cells.
- These interactions provide new insights into curcumin's anti-cancer mechanisms.
- Identification of binding partners may guide the development of novel cancer therapies.
