|
Type |
Poster Presentation |
Area |
Life Chemistry |
Room No. |
Event Hall |
Time |
4월 20일 (금요일) 11:00~12:30 |
Code |
BIO.P-315 |
Subject |
A small molecule of Hsp70 has anticancer activities |
Authors |
Sang-Hyun PARK, Injae Shin* Department of Chemistry, Yonsei University, Korea |
Abstract |
The heat shock protein Hsp70 has an antiapoptotic function and is overexpressed in various cancer cells. Here we describe a small molecule which inhibits the ATPase activity of Hsp70 by binding to its ATPase domain and induces apoptosis of cancer cells. The results of affinity chromatography showed that the Hsp70 inhibitor selectively binds to Hsp70 but not to other heat shock proteins such as Hsp40, Hsp60 and Hsp90. In addition, the results of the mechanism study showed that the Hsp70 inhibitor promoted caspase activation leading to caspase-dependent apoptosis by interfering with the interaction of Hsp70 with Apaf-1. Also, animal studies of tumor growth in a xenograft mouse model showed that treatment of Az significantly reduced the tumor size without affecting mouse viability. Taken together, the findings suggest that the Hsp70 inhibitor can be used as a chemical probe to understand the diverse functions of Hsp70 and ultimately as a new cancer chemotherapy. |
E-mail |
romeopsh@yonsei.ac.kr |
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