Effects of hyperthermia on Hsp27 (HSPB1), Hsp72 (HSPA1A) and DNA repair proteins hMLH1 and hMSH2 in human colorectal cancer hMLH1-deficient and hMLH1-proficient cell lines

Nadin, Silvina B.; Cuello-Carrión, F. Darío; Sottile, Mayra L.; Ciocca, Daniel R.; Vargas–Roig, Laura M.

doi:10.3109/02656736.2011.638962

Cited by 22 publications

(19 citation statements)

References 48 publications

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“…were translocated from the nucleus to the cytoplasm at 41 o C and 42 o C while exposure to these temperatures was also accompanied by an elevation in the expression rates of HSP27 and HSP72 in human colorectal cancer cell lines [79]. In addition, the co-localization of HSP27…”

Section: Mismatch Repair (Mmr)mentioning

confidence: 96%

Effects of hyperthermia as a mitigation strategy in DNA damage-based cancer therapies

Mantso

Goussetis

Franco

et al. 2016

Seminars in Cancer Biology

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Utilization of thermal therapy (hyperthermia) is defined as the application of exogenous heat induction and represents a concept that is far from new as it goes back to ancient times when heat was used for treating various diseases, including malignancies. Such therapeutic strategy has gained even more popularity (over the last few decades) since various studies have shed light into understanding hyperthermia's underlying molecular mechanism(s) of action. In general, hyperthermia is applied as complementary (adjuvant) means in therapeutic protocols combining chemotherapy and/or irradiation both of which can induce irreversible cellular DNA damage. Furthermore, according to a number of in vitro, in vivo and clinical studies, hyperthermia has been shown to enhance the beneficial effects of DNA targeting therapeutic strategies by interfering with DNA repair response cascades. Therefore, the continuously growing evidence supporting hyperthermia's beneficial role in cancer treatment can also encourage its application as a DNA repair mitigation strategy. In this review article, we aim to provide detailed information on how hyperthermia acts on DNA damage and repair pathways and thus potentially contributing to various adjuvant therapeutic protocols relevant to more efficient cancer treatment strategies.

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Section: Mismatch Repair (Mmr)mentioning

confidence: 96%

Effects of hyperthermia as a mitigation strategy in DNA damage-based cancer therapies

Mantso

Goussetis

Franco

et al. 2016

Seminars in Cancer Biology

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“…Today, at least Hsp27 and Hsp70 families are associated with heat exposure [137][138][139]. Indeed, it was demonstrated that HSF1 is able to respond to signalling by stress factors, including elevated temperature [140].…”

Section: Heat Stress and Heat Shock Proteins (Hsps)mentioning

confidence: 99%

Reactive oxygen species, heat stress and oxidative-induced mitochondrial damage. A review

Slimen¹,

Najar

Ghram

et al. 2014

International Journal of Hyperthermia

592

248

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In recent years there has been enormous interest in researching oxidative stress. Reactive oxygen species (ROS) are derived from the metabolism of oxygen as by-products of cell respiration, and are continuously produced in all aerobic organisms. Oxidative stress occurs as a consequence of an imbalance between ROS production and the available antioxidant defence against them. Nowadays, a variety of diseases and degenerative processes such as cancer, Alzheimer's and autoimmune diseases are mediated by oxidative stress. Heat stress was suggested to be an environmental factor responsible for stimulating ROS production because of similarities in responses observed following heat stress compared with that occurring following exposure to oxidative stress. This manuscript describes the main mitochondrial sources of ROS and the antioxidant defences involved to prevent oxidative damage in all the mitochondrial compartments. It also deals with discussions concerning the cytotoxic effect of heat stress, mitochondrial heat-induced alterations, as well as heat shock protein (HSP) expression as a defence mechanism.

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“…Nadin et al (2007) reported in peripheral blood lymphocytes from healthy subjects exposed in vitro to hyperthermia and cisplatin that MLH1 and MSH2 (MMR proteins) co-localize with HSPB1 and HSPA. Hyperthermia induced the nuclear accumulation of HSPB1 and affected the subcellular localization of MLH1 and MSH2 in human colon cancer cells (Nadin et al 2012). In patients with gliomas, deficiency of DNA MMR proteins seems to contribute to glioblastoma progression since in recurrent tumors, MLH1 expression was found significantly reduced (Stark et al 2010).…”

Section: Introductionmentioning

confidence: 99%

Effects of temozolomide (TMZ) on the expression and interaction of heat shock proteins (HSPs) and DNA repair proteins in human malignant glioma cells

Castro

Cayado-Gutiérrez

Zoppino

et al. 2015

Cell Stress and Chaperones

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We previously reported the association of HSPA1A and HSPB1 with high-grade astrocytomas, suggesting that these proteins might be involved in disease outcome and response to treatment. With the aim to better understand the resistance/susceptibility processes associated to temozolomide (TMZ) treatment, the current study was performed in three human malignant glioma cell lines by focusing on several levels: (a) apoptotic index and senescence, (b) DNA damage, and (c) interaction of HSPB1 with players of the DNA damage response. Three human glioma cell lines, Gli36, U87, and DBTRG, were treated with TMZ evaluating cell viability and survival, apoptosis, senescence, and comets (comet assay). The expression of HSPA (HSPA1A and HSPA8), HSPB1, O 6 -methylguanine-DNA methyltransferase (MGMT), MLH1, and MSH2 was determined by immunocytochemistry, immunofluorescence, and Western blot. Immunoprecipitation was used to analyze protein interaction. The cell lines exhibited differences in viability, apoptosis, and senescence after TMZ administration. We then focused on Gli36 cells (relatively unstudied) which showed very low recovery capacity following TMZ treatment, and this was related to high DNA damage levels; however, the cells maintained their viability. In these cells, MGMT, MSH2, HSPA, and HSPB1 levels increased significantly after TMZ administration. In addition, MSH2 and HSPB1 proteins appeared co-localized by confocal microscopy. This colocalization increased after TMZ treatment, and in immunoprecipitation analysis, MSH2 and HSPB1 appeared interacting. In contrast, HSPB1 did not interact with MGMT. We show in glioma cells the biological effects of TMZ and how this drug affects the expression levels of heat shock proteins (HSPs), MGMT, MSH2, and MLH1. In Gli36 cells, the results suggest that interactions between HSPB1 and MSH2, including co-nuclear localization, may be important in determining cell sensitivity to TMZ.

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Effects of hyperthermia on Hsp27 (HSPB1), Hsp72 (HSPA1A) and DNA repair proteins hMLH1 and hMSH2 in human colorectal cancer hMLH1-deficient and hMLH1-proficient cell lines

Cited by 22 publications

References 48 publications

Effects of hyperthermia as a mitigation strategy in DNA damage-based cancer therapies

Effects of hyperthermia as a mitigation strategy in DNA damage-based cancer therapies

Reactive oxygen species, heat stress and oxidative-induced mitochondrial damage. A review

Effects of temozolomide (TMZ) on the expression and interaction of heat shock proteins (HSPs) and DNA repair proteins in human malignant glioma cells

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