Friday, October 7, 2011
A ffinity-based proteomics reveal cancer-specific networks coordinated by Hsp90
Hsp90 is a house keeping protein that assists in folding and transloction of proteins. It is also shown to be up-regulated in cancer cells. In this paper, the authors show that the small molecule, PU-H71, binds to and inhibits a fraction of Hsp90 that is more abundant in cancer cells. They then take PU-H71, and use an affinity capture method to identify proteins that are up regulated in different cancer types.
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The immobilized PU-H71 takes the place of an antibody in a co-immunoprecipitation. The lucky part is that the molecule selectively binds to a pocket that is only present when BCR and ABL are bound, which doesn't occur in healthy cells. They say that the antibody is not specific for HSP90 in the cancer cells, but why not just use only cancer cells as opposed to a mixture of cancer and healthy cells? It seems like this small molecule is fairly unique, so I don't think this method could be applied to lots of other proteins involved in cancer.
ReplyDeleteI think that they are trying to show how HSP90 BCR ABL is up-regulated in cancer by comparing it to healthy cells. From what I understood, the antibody binds to all forms of HSP90 so that way you can compare the amount that bound to PU-H71 over the total concentration.
ReplyDeleteThis paper reminds me a lot of the papers we read for small molecule target ID, specifically Zhang (2007). Yes, the molecule itself is unique, but the method of attaching a small molecule to a solid support is widely used.