Concomitant alterations in distribution of 70kDa heat shock proteins, cytoskeleton and organelles in heat shocked 9L cells

Wang, Tingting; Chiang, Ann‐Shyn; Chu, Jao-Jia; Cheng, Ting‐Jen R.; Chen, Tzu-Mei; Lai, Yiu‐Kay

doi:10.1016/s1357-2725(97)00133-7

Cited by 29 publications

(33 citation statements)

References 52 publications

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“…For this reason in our study we observed Hsp70 localization. Other previous works have demonstrated that in some cell lines HSP70 is associated with tubulin, with a generic chaperone function (Cheng and Lai 1994;Wang et al 1998), while in rat embryo fibroblasts it has been found associated with actin microfilaments (La Thangue 1984;Margulis and Welsh 1991a, b is a physical interaction between Hsp70 and actin not only a co-localization. A different intracellular distribution was evident for the constitutive chaperone Hsc70.…”

Section: Discussionmentioning

confidence: 92%

“…After the stress Hsp70 turns back to the cytoplasm (Velazquez and Lindquist 1984;Welch and Feramisco 1984;Rada et al 2005). Heat shock also induces a reorganization of the cytoskeleton with consequent changes in cellular shape and actin, in the same way of Hsp70, migrates into the nucleus (Wang et al 1998;Welch and Mizzen 1988). Hsc70 is also a cytoplasmic protein and it translocates within the nucleus after heat shock (Lagunas et al 2004).…”

Section: Introductionmentioning

confidence: 99%

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Hsp70 localizes differently from chaperone Hsc70 in mouse mesoangioblasts under physiological growth conditions

et al. 2008

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Mouse A6 mesoangioblasts express Hsp70 even in the absence of cellular stress. Its expression and its intracellular localization were investigated under normal growth conditions and under hyperthermic stress. Immunofluorescence assays indicated that without any stress a fraction of Hsp70 co-localized with actin microfilaments, in the cell cortex and in the contractile ring of dividing cells, while the Hsc70 chaperone did not. Hsp70 immunoprecipitation assays confirmed that a portion of Hsp70 binds actin. Immunoblot assays showed that both proteins were present in the nucleus. After heat treatment Hsp70 and actin continued to co-localize in the leading edge of A6 cells but not on microfilaments. Although Hsp70 and Hsc70 are both basally synthesized they showed different cellular distribution, suggesting an Hsp70 different activity respect to the Hsc70 chaperone. Moreover, we found Hsp70 in the culture medium as it has been described in other cell types.

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Section: Discussionmentioning

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Hsp70 localizes differently from chaperone Hsc70 in mouse mesoangioblasts under physiological growth conditions

et al. 2008

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“…We, therefore, chose this organism to study the e¡ects of heat shock on cell morphology, pseudopodia and F-actin formation, recovery from heat shock and adaptation during continued exposure. We focused on F-actin dynamics, because heat shock was shown to cause a rapid loss of stress ¢bers [11,12] and a disorganization of actin ¢laments in mammalian cells [13]. The negative e¡ect of heat shock on the F-actin level that we measured in these experiments may be causally related to the observed retraction of pseudopodia and prompted us to analyze possible factors involved in the heat-induced actin depolymerization.…”

Section: Introductionmentioning

confidence: 99%

Changes in cell morphology and actin organization during heat shock in Dictyostelium discoideum: does HSP70 play a role in acquired thermotolerance?

Xiang

1999

FEMS Microbiology Letters

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In response to heat shock (34³C, 30 min), cell morphology and actin organization in Dictyostelium discoideum are drastically changed. Loss of pseudopodia and disappearance of F-actin-containing structures were observed by using fluorescence microscopy. These changes were paralleled by a rapid decrease of the F-actin content measured by a TRITC-phalloidin binding assay. The effects of heat shock on cell morphology and actin organization are transient : After heat shock (34³C) or during a long-term heat treatment (30³C), cell morphology, F-actin patterns and F-actin content recovered/adapted to a state which is characteristic for untreated cells. Because F-actin may be stabilized by increased amounts of heat shock proteins, their response and interaction with F-actin was analyzed. After a 1 h heat treatment (34³C), the major heat shock protein of D. discoideum (HSP70) showed maximally increased synthesis rates and levels. During recovery from a 34³C shock or during a continuous heat treatment at 30³C, the HSP70 content first increased and then declined slowly toward normal levels. Pre-treatment of cells with a short heat shock of 30 min at 34³C stabilized the F-actin content when the cells were exposed to a second heat shock. Furthermore, a transient colocalization of HSP70 and actin was observed at the beginning of heat treatment (30³C) using immunological detection of HSP70 in the cytoskeletal actin fraction. ß

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“…In fact, rearrangements of the actin filaments accompanied by striking changes in cell shapes in MX1 human breast cancer cells were reported under comparatively mild heat stress conditions (Dressler et al 2013). Also, it was reported that 9L rat brain tumor cells had contracted cell shape after a 15 min 45 ºC heat stress (Wang et al 1998). It has been reported that hyperthermia favors changes in human cancer cell shapes through the integrin modifications (Pawlik et al 2013).…”

Section: Rac1 Is Involved In Heat Induced Changes In Cell Morphologymentioning

confidence: 98%

“…It has been reported that hyperthermia favors changes in human cancer cell shapes through the integrin modifications (Pawlik et al 2013). Besides this, both microtubules and actin filaments are known to be affected by heat stress in a variety of organisms (Wang et al 1998) and Rac1 has been shown to play important roles in cytoskeletal organization (B. . Indeed, flow cytometer and SE Microscopy results showed that at mild stress conditions of 41.5 °C, filamentous actin cytoskeleton and cell shape were not affected in B16F10 cells whereas, exposure of stress temperature of 43 °C caused striking changes of cell shapes and rearrangements of actin filaments.…”

Section: Rac1 Is Involved In Heat Induced Changes In Cell Morphologymentioning

confidence: 99%

The role of small GTPase Rac1 in stress signaling

Güngör

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Concomitant alterations in distribution of 70kDa heat shock proteins, cytoskeleton and organelles in heat shocked 9L cells

Cited by 29 publications

References 52 publications

Hsp70 localizes differently from chaperone Hsc70 in mouse mesoangioblasts under physiological growth conditions

Hsp70 localizes differently from chaperone Hsc70 in mouse mesoangioblasts under physiological growth conditions

Changes in cell morphology and actin organization during heat shock in Dictyostelium discoideum: does HSP70 play a role in acquired thermotolerance?

The role of small GTPase Rac1 in stress signaling

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