Title : (-)-Epigallocatechin-3-gallate inhibits Hsp90 function by impairing Hsp90 association with cochaperones in pancreatic cancer cell line Mia Paca-2.

Pub. Date : 2009 Jul-Aug

PMID : 19438225






12 Functional Relationships(s)
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Protein Name
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1 (-)-Epigallocatechin-3-gallate inhibits Hsp90 function by impairing Hsp90 association with cochaperones in pancreatic cancer cell line Mia Paca-2. epigallocatechin gallate heat shock protein 90 alpha family class A member 1 Homo sapiens
2 (-)-Epigallocatechin-3-gallate inhibits Hsp90 function by impairing Hsp90 association with cochaperones in pancreatic cancer cell line Mia Paca-2. epigallocatechin gallate heat shock protein 90 alpha family class A member 1 Homo sapiens
3 (-)-EGCG was reported to bind to the C-terminal domain of heat shock protein 90 (Hsp90). epigallocatechin gallate heat shock protein 90 alpha family class A member 1 Homo sapiens
4 (-)-EGCG was reported to bind to the C-terminal domain of heat shock protein 90 (Hsp90). epigallocatechin gallate heat shock protein 90 alpha family class A member 1 Homo sapiens
5 The purpose of this study is to investigate (-)-EGCG as a novel Hsp90 inhibitor to impair Hsp90 superchaperone complex for simultaneous downregulation of oncogenic proteins in pancreatic cancer cells. epigallocatechin gallate heat shock protein 90 alpha family class A member 1 Homo sapiens
6 The purpose of this study is to investigate (-)-EGCG as a novel Hsp90 inhibitor to impair Hsp90 superchaperone complex for simultaneous downregulation of oncogenic proteins in pancreatic cancer cells. epigallocatechin gallate heat shock protein 90 alpha family class A member 1 Homo sapiens
7 Western blotting analysis demonstrated that (-)-EGCG induced downregulation of oncogenic Hsp90 client proteins by approximately 70-95%, including Akt, Cdk4, Raf-1, Her-2, and pERK. epigallocatechin gallate heat shock protein 90 alpha family class A member 1 Homo sapiens
8 Co-immunoprecipitation showed that (-)-EGCG decreased the association of cochaperones p23 and Hsc70 with Hsp90 by more than 50%, while it had little effect on the ATP binding to Hsp90. epigallocatechin gallate heat shock protein 90 alpha family class A member 1 Homo sapiens
9 Proteolytic fingerprinting assay confirmed direct binding between (-)-EGCG and the Hsp90 C-terminal domain. epigallocatechin gallate heat shock protein 90 alpha family class A member 1 Homo sapiens
10 These data suggest that the binding of (-)-EGCG to Hsp90 impairs the association of Hsp90 with its cochaperones, thereby inducing degradation of Hsp90 client proteins, resulting antiproliferating effects in pancreatic cancer cells. epigallocatechin gallate heat shock protein 90 alpha family class A member 1 Homo sapiens
11 These data suggest that the binding of (-)-EGCG to Hsp90 impairs the association of Hsp90 with its cochaperones, thereby inducing degradation of Hsp90 client proteins, resulting antiproliferating effects in pancreatic cancer cells. epigallocatechin gallate heat shock protein 90 alpha family class A member 1 Homo sapiens
12 These data suggest that the binding of (-)-EGCG to Hsp90 impairs the association of Hsp90 with its cochaperones, thereby inducing degradation of Hsp90 client proteins, resulting antiproliferating effects in pancreatic cancer cells. epigallocatechin gallate heat shock protein 90 alpha family class A member 1 Homo sapiens