Dobutamine mediates cytoprotection by induction of heat shock protein 70 in vitro

Roesslein, Martin; Froehlich, Christian; Jans, Frank; Piegeler, Tobias; Goebel, Ulrich; Loop, Torsten

doi:10.1016/j.lfs.2014.01.005

Cited by 6 publications

(12 citation statements)

References 44 publications

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“…This is in accordance with our findings: Inhibition of Hsp70 by KNK 437, which has been shown to inhibit the expression of hsp70 at the mRNA level by us [14] and others [15,16], substantially blunted the thiopental-mediated protection from apoptosis. Another linkage between thiopental and Hsp70 is provided by the fact that both have been shown to inhibit…”

Section: Accepted Manuscriptsupporting

confidence: 93%

“…Pharmacological inhibition of Hsp70 was achieved by incubation with Nformyl-3,4-methylenedioxy-benzylidene-gammabutyrolaetam (KNK437, 100 μM) for 24 h prior to thiopental incubation as previously shown [14][15][16].…”

Section: Experimental Protocolmentioning

confidence: 99%

“…Cells were harvested using trypsine-EDTA and nuclear and cytoplasmic proteins were extracted using a salt detergent buffer as previously described [14]. Nuclear proteins were isolated using a commercial kit (40010, Active Motif, La Hulpe, Belgium) according to the manufacturer's recommendations.…”

Section: Protein Extractionmentioning

confidence: 99%

“…Electrophoretic mobility shift assay was performed as previously described [14]. Briefly, total cell extracts were incubated with a 32 P-labeled HSF-1 oligonucleotide, loaded on an acrylamide gel, vacuum dried and then exposed to X-ray film.…”

Section: Electrophoretic Mobility Shift Assaymentioning

confidence: 99%

“…When Hsp70 expression was pharmacologically inhibited by N-formyl-3,4-methylenedioxybenzylidene-gammabutyrolaetam (KNK437, previously shown in [14][15][16]) before the incubation with thiopental, the thiopental-mediated reduction was altered and caspase-3- …”

Section: Hsp70 Seems To Be Involved In the Thiopental-induced Protectmentioning

confidence: 99%

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Thiopental protects human neuroblastoma cells from apoptotic cell death — Potential role of heat shock protein 70

et al. 2015

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Section: Accepted Manuscriptsupporting

confidence: 93%

Section: Experimental Protocolmentioning

confidence: 99%

Section: Protein Extractionmentioning

confidence: 99%

Section: Electrophoretic Mobility Shift Assaymentioning

confidence: 99%

Section: Hsp70 Seems To Be Involved In the Thiopental-induced Protectmentioning

confidence: 99%

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Thiopental protects human neuroblastoma cells from apoptotic cell death — Potential role of heat shock protein 70

et al. 2015

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Chalcones from Angelica keiskei: Evaluation of Their Heat Shock Protein Inducing Activities

et al. 2015

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Five new chalcones, 4,2',4'-trihydroxy-3'-[(2E,5E)-7-methoxy-3,7-dimethyl-2,5-octadienyl]chalcone (1), (±)-4,2',4'-trihydroxy-3'-[(2E)-6-hydroxy-7-methoxy-3,7-dimethyl-2-octenyl]chalcone (2), 4,2',4'-trihydroxy-3'-[(2E)-3-methyl-5-(1,3-dioxolan-2-yl)-2-pentenyl]chalcone (3), 2',3'-furano-4-hydroxy-4'-methoxychalcone (4), and (±)-4-hydroxy-2',3'-(2,3-dihydro-2-methoxyfurano)-4'-methoxychalcone (5), were isolated from the aerial parts of Angelica keiskei Koidzumi together with eight known chalcones, 6-13, which were identified as (±)-4,2',4'-trihydroxy-3'-[(6E)-2-hydroxy-7-methyl-3-methylene-6-octenyl]chalcone (6), xanthoangelol (7), xanthoangelol F (8), xanthoangelol G (9), 4-hydroxyderricin (10), xanthoangelol D (11), xanthoangelol E (12), and xanthoangelol H (13), respectively. Chalcones 1-13 were evaluated for their promoter activity on heat shock protein 25 (hsp25, murine form of human hsp27). Compounds 1 and 6 activated the hsp25 promoter by 21.9- and 29.2-fold of untreated control at 10 μM, respectively. Further protein expression patterns of heat shock factor 1 (HSF1), HSP70, and HSP27 by 1 and 6 were examined. Compound 6 increased the expression of HSF1, HSP70, and HSP27 by 4.3-, 1.5-, and 4.6-fold of untreated control, respectively, without any significant cellular cytotoxicities, whereas 1 did not induce any expression of these proteins. As a result, 6 seems to be a prospective HSP inducer.

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Increased extracellular heat shock protein 90α in severe sepsis and SIRS associated with multiple organ failure and related to acute inflammatory-metabolic stress response in children

Fitrolaki

Dimitriou²,

Venihaki³

et al. 2016

Medicine

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Mammalian heat-shock-protein (HSP) 90α rapidly responses to environmental insults. We examined the hypothesis that not only serum HSP72 but also HSP90α is increased in the systemic inflammatory response syndrome (SIRS), severe-sepsis (SS), and/or sepsis (S) compared to healthy children (H); we assessed HSP90α relation to (a) multiple organ system failure (MOSF) and (b) inflammatory-metabolic response and severity of illness.A total of 65 children with S, SS, or SIRS and 25 H were included. ELISA was used to evaluate extracellular HSP90α and HSP72, chemiluminescence interleukins (ILs), flow-cytometry neutrophil-CD64 (nCD64)-expression.HSP90α, along with HSP72, were dramatically increased among MOSF patients. Patients in septic groups and SIRS had elevated HSP90α compared to H (P < 0.01). HSP90α was independently related to predicted death rate and severity of illness; positively to HSP72, nCD64, ILs, length of stay, days on ventilator, and fever; negatively to HDL and LDL (P < 0.05). The HSP72 was increased in SS/S and related negatively to HDL and LDL (P < 0.05).Serum HSP90α is markedly elevated in children with severe sepsis and is associated with MOSF. Better than the HSP72, also increased in SS, SIRS, and MOSF, HSP90α is related to the inflammatory stress, fever, outcome endpoints, and predicted mortality and inversely related to the low-LDL/low-HDL stress metabolic pattern.

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Dobutamine mediates cytoprotection by induction of heat shock protein 70 in vitro

Cited by 6 publications

References 44 publications

Thiopental protects human neuroblastoma cells from apoptotic cell death — Potential role of heat shock protein 70

Thiopental protects human neuroblastoma cells from apoptotic cell death — Potential role of heat shock protein 70

Chalcones from Angelica keiskei: Evaluation of Their Heat Shock Protein Inducing Activities

Increased extracellular heat shock protein 90α in severe sepsis and SIRS associated with multiple organ failure and related to acute inflammatory-metabolic stress response in children

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