Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2008-4-28
pubmed:abstractText
Resistance to current cancer therapies has forced scientists to investigate new avenues of therapy distinct from those aimed at single targets, to strategies based on targeting families of proteins, on which cancers rely for their ability to survive stress. Two such protein families are the heat shock proteins (HSP), especially the HSP90 family, and proteins involved in mediating the unfolded protein response (UPR). HSP90 stabilises key survival factors in cancer cells including AKT, ERB2 and HIF1alpha, which alone makes HSP90 inhibitors extremely interesting as potential therapies. In addition targeting HSP90 can destabilise the UPR inducing cell death. A broad range of cancer-types rely on the UPR to correctly fold key signalling proteins properly, as well as to allow the cell to cope with the hypoxic environment associated with tumour development. These associations suggest that a range of tumours may be targeted using HSP90 inhibitors and that the development of specific inhibitors of the UPR may be of interest. In this article, based on work in multiple myeloma, we highlight the importance of targeting multiple signalling pathways simultaneously, using the UPR and heat shock proteins as examples, as a means of effectively killing cancer cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1551-4005
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
865-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Untangling the unfolded protein response.
pubmed:affiliation
Section of Haemato-Oncology, The Institute of Cancer Research, Sutton, Surrey, UK.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't