Hsps 70 and 105 associate with a group of hsp90 client proteins that are selectively found in human breast cancer

Christopher Shipp; Kenneth Watson; Graham L Jones

doi:10.3288/contoo.paper.295

Abstract

This study investigated the interaction of heat shock proteins (hsps) and their client proteins in tumour and normal human breast tissue. The objective of the study was to discover hsp interactions specific to cancer cells. Hsps have been observed to be over-expressed in a range of human cancers. Of which hsps 70, 90 and others have been noted to be up-regulated in breast cancer. Up-regulation of these hsps has been shown to predict patient prognosis and response to therapies [1, 2]. The majority of hsp90's client proteins are signal transduction proteins. In addition, hsp90 is essential for cellular survival and has been proposed to participate in all 6 "hallmarks of cancer" [3]. Hsp90 inhibitors are under intense investigation and are currently in phase III clinical trials for the treatment of cancer. Hsp90 is known to associate with other hsps in the assembly and function of chaperone complexes. These experiments examined the hsp chaperone complexes and the effect of geldanamycin (an hsp90 inhibitor) on these complexes in human breast cancer.

Original language	English
DOIs	https://doi.org/10.3288/contoo.paper.295
Publication status	Published - 2009
Event	International Meeting on Signal Transduction Disease and Trinational Fall Meeting of the Societies of Biochemistry and Molecular Biology - Aachen, Germany Duration: 27 Sept 2009 → 30 Sept 2009

Conference

Conference	International Meeting on Signal Transduction Disease and Trinational Fall Meeting of the Societies of Biochemistry and Molecular Biology
City	Aachen, Germany
Period	27/09/09 → 30/09/09

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

Molecular Targets

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10.3288/contoo.paper.295

https://hdl.handle.net/1959.11/5654

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Shipp, C., Watson, K., & Jones, G. L. (2009). Hsps 70 and 105 associate with a group of hsp90 client proteins that are selectively found in human breast cancer. Abstract from International Meeting on Signal Transduction Disease and Trinational Fall Meeting of the Societies of Biochemistry and Molecular Biology, Aachen, Germany. https://doi.org/10.3288/contoo.paper.295

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abstract = "This study investigated the interaction of heat shock proteins (hsps) and their client proteins in tumour and normal human breast tissue. The objective of the study was to discover hsp interactions specific to cancer cells. Hsps have been observed to be over-expressed in a range of human cancers. Of which hsps 70, 90 and others have been noted to be up-regulated in breast cancer. Up-regulation of these hsps has been shown to predict patient prognosis and response to therapies [1, 2]. The majority of hsp90's client proteins are signal transduction proteins. In addition, hsp90 is essential for cellular survival and has been proposed to participate in all 6 {"}hallmarks of cancer{"} [3]. Hsp90 inhibitors are under intense investigation and are currently in phase III clinical trials for the treatment of cancer. Hsp90 is known to associate with other hsps in the assembly and function of chaperone complexes. These experiments examined the hsp chaperone complexes and the effect of geldanamycin (an hsp90 inhibitor) on these complexes in human breast cancer.",

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author = "Christopher Shipp and Kenneth Watson and Jones, \{Graham L\}",

year = "2009",

doi = "10.3288/contoo.paper.295",

language = "English",

note = "International Meeting on Signal Transduction Disease and Trinational Fall Meeting of the Societies of Biochemistry and Molecular Biology ; Conference date: 27-09-2009 Through 30-09-2009",

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Shipp, C, Watson, K & Jones, GL 2009, 'Hsps 70 and 105 associate with a group of hsp90 client proteins that are selectively found in human breast cancer', International Meeting on Signal Transduction Disease and Trinational Fall Meeting of the Societies of Biochemistry and Molecular Biology, Aachen, Germany, 27/09/09 - 30/09/09. https://doi.org/10.3288/contoo.paper.295

Hsps 70 and 105 associate with a group of hsp90 client proteins that are selectively found in human breast cancer. / Shipp, Christopher; Watson, Kenneth; Jones, Graham L.
2009. Abstract from International Meeting on Signal Transduction Disease and Trinational Fall Meeting of the Societies of Biochemistry and Molecular Biology, Aachen, Germany.

Research output: Contribution to conference › Abstract

TY - CONF

T1 - Hsps 70 and 105 associate with a group of hsp90 client proteins that are selectively found in human breast cancer

AU - Shipp, Christopher

AU - Watson, Kenneth

AU - Jones, Graham L

PY - 2009

Y1 - 2009

N2 - This study investigated the interaction of heat shock proteins (hsps) and their client proteins in tumour and normal human breast tissue. The objective of the study was to discover hsp interactions specific to cancer cells. Hsps have been observed to be over-expressed in a range of human cancers. Of which hsps 70, 90 and others have been noted to be up-regulated in breast cancer. Up-regulation of these hsps has been shown to predict patient prognosis and response to therapies [1, 2]. The majority of hsp90's client proteins are signal transduction proteins. In addition, hsp90 is essential for cellular survival and has been proposed to participate in all 6 "hallmarks of cancer" [3]. Hsp90 inhibitors are under intense investigation and are currently in phase III clinical trials for the treatment of cancer. Hsp90 is known to associate with other hsps in the assembly and function of chaperone complexes. These experiments examined the hsp chaperone complexes and the effect of geldanamycin (an hsp90 inhibitor) on these complexes in human breast cancer.

AB - This study investigated the interaction of heat shock proteins (hsps) and their client proteins in tumour and normal human breast tissue. The objective of the study was to discover hsp interactions specific to cancer cells. Hsps have been observed to be over-expressed in a range of human cancers. Of which hsps 70, 90 and others have been noted to be up-regulated in breast cancer. Up-regulation of these hsps has been shown to predict patient prognosis and response to therapies [1, 2]. The majority of hsp90's client proteins are signal transduction proteins. In addition, hsp90 is essential for cellular survival and has been proposed to participate in all 6 "hallmarks of cancer" [3]. Hsp90 inhibitors are under intense investigation and are currently in phase III clinical trials for the treatment of cancer. Hsp90 is known to associate with other hsps in the assembly and function of chaperone complexes. These experiments examined the hsp chaperone complexes and the effect of geldanamycin (an hsp90 inhibitor) on these complexes in human breast cancer.

KW - Molecular Targets

U2 - 10.3288/contoo.paper.295

DO - 10.3288/contoo.paper.295

M3 - Abstract

T2 - International Meeting on Signal Transduction Disease and Trinational Fall Meeting of the Societies of Biochemistry and Molecular Biology

Y2 - 27 September 2009 through 30 September 2009

ER -