Common antigenicity of mouse 42°C-specific heat-shock protein with mouse hsp 105

Honda, Kenichi; Hatayama, Takumi; Yukioka, Munehiko

doi:10.1016/0006-291x(89)91620-3

Cited by 34 publications

(21 citation statements)

References 12 publications

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“…The following antibodies were used for western blotting, immunofluorescence, and gel shift experiments: Hsp105, rabbit anti‐(human Hsp105 IgG) [27]; Hsp70, mouse anti‐(human Hsp70 IgG), which only reacted with inducible Hsp70 (clone C92F3A‐5; Stressgen, Ann Arbor, MI, USA); myc tag, mouse anti‐myc IgG (Invitrogen, Carlsbad, CA, USA); HSF1, rabbit anti‐(human HSF1 IgG) (Stressgen); STAT3, rabbit anti‐(mouse STAT3 IgG) (K‐15; Santa Cruz Biotechnology, Santa Cruz, CA, USA); phosphorylated STAT3, rabbit anti‐[phospho‐STAT3 (Tyr705) IgG] (D3A7; Cell Signaling Technology, Danvers, MA, USA); α‐tubulin, mouse anti‐α‐tubulin IgG (clone DM1A; Sigma, Saint Louis, MI, USA).…”

Section: Methodsmentioning

confidence: 99%

“…The following antibodies were used for western blotting, immunofluorescence, and gel shift experiments: Hsp105, rabbit anti-(human Hsp105 IgG) [27]; Hsp70, mouse anti-(human Hsp70 IgG), which only reacted with inducible Hsp70 (clone C92F3A-5; Stressgen, Ann Arbor, MI, USA); myc tag, mouse anti-myc IgG (Invitrogen, Carlsbad, CA, USA); HSF1, rabbit anti-(human HSF1 IgG) (Stressgen); STAT3, rabbit anti-(mouse STAT3 IgG) (K-15; Santa Cruz A B Fig. 7.…”

Section: Antibodiesmentioning

confidence: 99%

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Hsp105β upregulates hsp70 gene expression through signal transducer and activator of transcription‐3

et al. 2009

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Hsp105α and Hsp105β are mammalian members of the Hsp105/110 family, a divergent subgroup of the Hsp70 family. Hsp105α is expressed constitutively and induced by various forms of stress, whereas Hsp105β is an alternatively spliced form of Hsp105α that is expressed specifically during mild heat shock. In a report, it was shown that Hsp105α and Hsp105β localize to the cytoplasm and of nucleus of cells, respectively, and that Hsp105β, but not Hsp105α, induces the expression of Hsp70 in mammalian cells. Here, we examined the mechanism by which Hsp105β induces the expression of Hsp70. Using a series of deletion mutants of Hsp105β, it was revealed that the region between amino acids 642 and 662 of Hsp105β is necessary for the activation of the hsp70 promoter by Hsp105β. Furthermore, it was shown that signal transducer and activator of transcription (STAT)‐3 bound to the sequence of the hsp70 promoter between −206 and −187 bp, and that mutations of this sequence abrogated the activation of the hsp70 promoter by Hsp105β. In addition, overexpression of Hsp105β stimulated the phosphorylation of STAT3 at Tyr705 and its translocation to the nucleus. Downregulation of STAT3 expression resulted in reduction of the activation of the hsp70 promoter by Hsp105β. Furthermore, downregulation of Hsp105β reduced the expression of Hsp70 in heat‐shocked cells. On the basis of these findings, it is suggested that Hsp105β induces Hsp70 expression markedly through the STAT3 pathway in heat‐shocked cells. This may represent the mechanism that connects the heat shock protein and STAT families for cell defense against deleterious stress.

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Section: Methodsmentioning

confidence: 99%

Section: Antibodiesmentioning

confidence: 99%

Hsp105β upregulates hsp70 gene expression through signal transducer and activator of transcription‐3

et al. 2009

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“…Hsp110 is also denoted as Hsp105 (Hatayama et al 1994;Honda et al 1989). In mouse FM3A cells, 2 alternative forms, 105 ␣ and 105 ␤, are observed, with 105 ␤ having 43 fewer amino acids than 105 ␣.…”

Section: The Mammalian Members Of the Hsp110/ Sse Family: An Overviewmentioning

confidence: 99%

The Hsp110 and Grp170 stress proteins: newly recognized relatives of the Hsp70s

Easton

Kaneko²,

Subjeck³

2000

Cell Stress Chaper

292

259

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“…The following antibodies were used for immunoblotting and immunofluorescence experiments: Hsp105, rabbit polyclonal anti‐mouse Hsp105, which only reacts with mouse Hsp105 [62], or rabbit anti‐human Hsp105, which reacts with human, mouse, rat, and monkey Hsp105 [15]; PARP, rabbit polyclonal anti‐PARP (#sc‐7150; Santa Cruz Biotechnology, Santa Cruz, CA, USA); cleaved caspase‐3, rabbit polyclonal anti‐cleaved caspase‐3 (Asp175) (#9661; Cell Signaling Technology, Danvers, MA, USA); caspase‐9, rabbit polyclonal anti‐caspase‐9 (#9502; Cell Signaling Technology); cytochrome c , rabbit polyclonal anti‐cytochrome c (#sc‐7159; Santa Cruz); Bax, rabbit polyclonal anti‐Bax (#06‐499; Upstate Biotechnology, Lake Placid, NY, USA); Hsp60, mouse monoclonal anti‐Hsp60 clone LK‐1 (#SR‐B806; Medical & Biological Laboratories; Nagoya, Japan); G3DPH, rabbit polyclonal anti‐G3PDH (#2275‐PC‐1; Trevigen, Gaithersburg, MD, USA); JNK phosphorylated at Thr183 and Tyr185, rabbit polyclonal anti‐phospho‐SAPK/JNK (Thr183/Tyr185) (#9251; Cell Signaling Technology); JNK, rabbit polyclonal anti‐SAPK/JNK (#9252; Cell Signaling Technology); p38 MAPK phosphorylated at Thr180 and Tyr182, rabbit polyclonal anti‐phospho‐p38 MAPK (Thr180/Tyr182) (#9211; Cell Signaling Technology); p38 MAPK, rabbit polyclonal anti‐p38 MAPK (#9212; Cell Signaling Technology); MAPKAP‐2 phosphorylated at Thr222, rabbit polyclonal anti‐phospho‐MAPKAP‐2 (Thr222) (#9211; Cell Signaling Technology); phosphorylated c‐Jun at Ser63, rabbit polyclonal anti‐phospho‐c‐Jun (Ser63) (#9261; Cell Signaling Technology).…”

Section: Methodsmentioning

confidence: 99%

Mammalian 105 kDa heat shock family proteins suppress hydrogen peroxide‐induced apoptosis through a p38 MAPK‐dependent mitochondrial pathway in HeLa cells

2008

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Hsp105α and Hsp105β are major heat shock proteins in mammalian cells that belong to a subgroup of the HSP70 family, HSP105/110. Previously, we have shown that Hsp105α has opposite effects on stress‐induced apoptosis depending on the cell type. However, it is not fully understood how Hsp105 regulates stress‐induced apoptosis. In this study, we examined how Hsp105α and Hsp105β regulate H2O2‐induced apoptosis by using HeLa cells in which expression of Hsp105α or Hsp105β was regulated using doxycycline. Overexpression of Hsp105α and Hsp105β suppressed the activation of caspase‐3 and caspase‐9 by preventing the release of cytochrome c from mitochondria in H2O2‐treated cells. Furthermore, both c‐Jun N‐terminal kinase (JNK) and p38 mitogen‐activated protein kinase (p38 MAPK) were activated by treatment with H2O2, and the activation of both kinases was suppressed by overexpression of Hsp105α and Hsp105β. However, H2O2‐induced apoptosis was suppressed by treatment with a potent inhibitor of p38 MAPK, SB202190, but not a JNK inhibitor, SP600125. These findings suggest that Hsp105α and Hsp105β suppress H2O2‐induced apoptosis by suppression of p38 MAPK signaling, one of the essential pathways for apoptosis.

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Common antigenicity of mouse 42°C-specific heat-shock protein with mouse hsp 105

Cited by 34 publications

References 12 publications

Hsp105β upregulates hsp70 gene expression through signal transducer and activator of transcription‐3

Hsp105β upregulates hsp70 gene expression through signal transducer and activator of transcription‐3

The Hsp110 and Grp170 stress proteins: newly recognized relatives of the Hsp70s

Mammalian 105 kDa heat shock family proteins suppress hydrogen peroxide‐induced apoptosis through a p38 MAPK‐dependent mitochondrial pathway in HeLa cells

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