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- W1553663144 abstract "Over the last decade, research has implicated a group of molecular chaperones termed Heat Shock Proteins (HSPs) as major contributors to cancer progression and the development of chemo-resistance. HSPs were initially discovered as a group of proteins that were strongly induced in response to heat shock and other cellular stresses. Under non-stress conditions, they have a wide variety of roles within many sub-cellular compartments where they facilitate protein folding, prevent protein unfolding and assist protein transport across membranes. Due to their roles in maintaining protein conformation, HSPs are vital when other cellular proteins start to unfold due to cellular stress such as high temperature, exposure to cytotoxic chemicals or oxidative stress and are up-regulated rapidly in these situations (Ciocca and Calderwood, 2005). Under these stressful conditions, HSPs prevent protein aggregation, stabilise cell membranes and inhibit many of the key steps in cell death pathways (Beere & Green, 2001), thereby enabling cell survival in conditions that would otherwise be lethal. Importantly, in normal cells, once the stress has passed, HSP levels return to baseline and these proteins return to their regular house-keeping duties. However, a growing body of research shows that in tumour cells, including Chronic Lymphocytic Leukaemia (CLL) cells, HSPs remain elevated and may contribute to prolonged tumour cell survival via several mechanisms that remain to be fully revealed." @default.
- W1553663144 created "2016-06-24" @default.
- W1553663144 creator A5019437477 @default.
- W1553663144 creator A5032652630 @default.
- W1553663144 creator A5082182199 @default.
- W1553663144 date "2012-02-10" @default.
- W1553663144 modified "2023-10-16" @default.
- W1553663144 title "Heat Shock Proteins in Chronic Lymphocytic Leukaemia" @default.
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