Title : Proteasome inhibitor-induced cleavage of HSP90 is mediated by ROS generation and caspase 10-activation in human leukemic cells.

Pub. Date : 2017 Oct

PMID : 28715732






7 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 In this study, we found that HSP90 was cleaved to a 55kDa protein after treatment with proteasome inhibitors including MG132 in leukemia cells but was not cleaved in other tissue-derived cells. benzyloxycarbonylleucyl-leucyl-leucine aldehyde heat shock protein 90 alpha family class A member 1 Homo sapiens
2 HSP90 has two major isoforms (HSP90alpha and HSP90beta), and both were cleaved by MG132 treatment. benzyloxycarbonylleucyl-leucyl-leucine aldehyde heat shock protein 90 alpha family class A member 1 Homo sapiens
3 HSP90 has two major isoforms (HSP90alpha and HSP90beta), and both were cleaved by MG132 treatment. benzyloxycarbonylleucyl-leucyl-leucine aldehyde heat shock protein 90 alpha family class A member 1 Homo sapiens
4 MG132 treatment also induced a decrease in HSP90 client proteins. benzyloxycarbonylleucyl-leucyl-leucine aldehyde heat shock protein 90 alpha family class A member 1 Homo sapiens
5 MG132 treatment generated ROS, and the cleavage of HSP90 was blocked by a ROS scavenger, N-acetylcysteine (NAC). benzyloxycarbonylleucyl-leucyl-leucine aldehyde heat shock protein 90 alpha family class A member 1 Homo sapiens
6 Based on an inhibitor study, the cleavage of HSP90 induced by MG132 was dependent on caspase 10 activation. benzyloxycarbonylleucyl-leucyl-leucine aldehyde heat shock protein 90 alpha family class A member 1 Homo sapiens
7 Taken all together, our results suggest that the cleavage of HSP90 by MG132 treatment is mediated by ROS generation and caspase 10 activation. benzyloxycarbonylleucyl-leucyl-leucine aldehyde heat shock protein 90 alpha family class A member 1 Homo sapiens