The Antioxidative Effect of Heat‐Shock Protein 70 in Dendritic Cells

Je, Jung Hwan; Kim, D. Y.; Roh, Hyo Jin; Pak, Charles C.; Kim, D. H.; Byamba, Dashlkhumbe; Jee, Hyunseok; Kim, T.-G.; Park, J. M.; Lee, S.-K.; Lee, M.-G.

doi:10.1111/sji.12078

Cited by 3 publications

(2 citation statements)

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“…(Je et al . ) Regarding HSP‐90, recent evidence suggest that an increase in HO‐1 expression may cause a suppression in HSP‐90 protein expression in neuronal cells. (Lee et al .…”

Section: Discussionmentioning

confidence: 99%

Neuroprotective effects of Argon are mediated via an ERK‐1/2 dependent regulation of heme‐oxygenase‐1 in retinal ganglion cells

Ulbrich

Kaufmann

Coburn

et al. 2015

Journal of Neurochemistry

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Retinal ischemia and reperfusion injuries (R-IRI) damage neuronal tissue permanently. Recently, we demonstrated that Argon exerts anti-apoptotic and protective properties. The molecular mechanism remains unclear. We hypothesized that Argon inhalation exert neuroprotective effects in rats retinal ganglion cells (RGC) via an ERK-1/2 dependent regulation of heat-shock proteins. Inhalation of Argon (75 Vol%) was performed after R-IRI on the rats 0 left eyes for 1 h immediately or with delay. Abbreviations used: ChAT, choline acetyltransferase; CO 2 , carbon dioxcide; DAPI, 4 0 , 6-diamino-2-phenylindole dihydrochloride hydrate; DMSO, dimethylsulfoxid; ERK, extracellular regulated protein kinase; FG, Fluorogold; GFAP, glial fibrillary acidic protein; HO-1, hemeoxygenase-1; HSP, heat-shock protein(s); Iba1, ionized calcium binding adaptor molecule 1; JNK, c-Jun N-terminale kinase; MAPK, mitogen activated protein kinases; NF-jB, nuclear factor j B; PBS, phosphate buffered saline; PD98059, ERK inhibitor; RGC, retinal ganglion cell(s); R-IRI, retinal ischemia/reperfusion injury.

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“…(Je et al . ) Regarding HSP‐90, recent evidence suggest that an increase in HO‐1 expression may cause a suppression in HSP‐90 protein expression in neuronal cells. (Lee et al .…”

Section: Discussionmentioning

confidence: 99%

Neuroprotective effects of Argon are mediated via an ERK‐1/2 dependent regulation of heme‐oxygenase‐1 in retinal ganglion cells

Ulbrich

Kaufmann

Coburn

et al. 2015

Journal of Neurochemistry

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“…Post-translational modifications (PTMs) are an important means of functional regulation and signal transduction, and a number of PTMs have been identified in Hsp70, including phosphorylation (14), acetylation (15), ubiquitination (16), methylation (17), carboxylation (18), Snitrosylation (19,20) and S-glutathionylation (21)(22)(23)(24)(25)(26)(27). It is predicted that PTMs can also regulate the functional cycle of Hsp70 (28).…”

Section: Structuresmentioning

confidence: 99%

S-Glutathionylation of human inducible Hsp70 reveals a regulatory mechanism involving the C-terminal α-helical lid

Yang

Zhang

Gong

et al. 2020

Journal of Biological Chemistry

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Heat shock protein 70 (Hsp70) proteins are a family of ancient and conserved chaperones. Cysteine modifications have been widely detected among different Hsp70 family members in vivo, but their effects on Hsp70 structure and function are unclear. Here, we treated HeLa cells with diamide, which typically induces disulfide bond formation except in the presence of excess GSH, when glutathionylated cysteines predominate. We show that in these cells, HspA1A (hHsp70) undergoes reversible cysteine modifications, including glutathionylation, potentially at all five cysteine residues. In vitro experiments revealed that modification of cysteines in the nucleotide-binding domain of hHsp70 is prevented by nucleotide binding but that Cys-574 and Cys-603, located in the C-terminal α-helical lid of the substrate-binding domain, can undergo glutathionylation in both the presence and absence of nucleotide. We found that glutathionylation of these cysteine residues results in unfolding of the α-helical lid structure. The unfolded region mimics substrate by binding to and blocking the substrate-binding site, thereby promoting intrinsic ATPase activity and competing with binding of external substrates, including heat shock transcription factor 1 (Hsf1). Thus, post-translational modification can alter the structure and regulate the function of hHsp70.

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Modulating effect of extracellular HSP70 on generation of reactive oxigen species in populations of phagocytes

et al. 2015

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Reactive oxygen species (ROS) produced by phagocytic cells of the innate immune system play an important role in the first line of defense protecting the host from pathogens. The NADPH oxidase multi-subunit complex is the main source of ROS in all types of the phagocytes. Formation of the membrane-associated enzyme complex and its activity are dependent on many different factors controlling both intensification and suppression of the ROS production rate. However, the evidences are emerging in recent years indicating existence of poorly studied mechanisms of restriction of ROS generation level in phagocytes directed at protection of host tissues in the sites of inflammation from destruction caused by the oxygen free radicals. Our previous data and results of other authors demonstrate that a mechanism of the limitation of ROS production by phagocytes may by connected with immunomodulating activity of extracellular pool. of HSP70. In the present work, we used inhibitors of NADPH oxidase and in vitro cultures of different phagocytes to study a possible relationship between down-regulating effect of exogenous HSP70 on ROS generation and the interaction of the protein with the enzyme subunits. Our results confirmed the literature data concerning the ability of extracellular HSP70 to modulate NADPH oxidase activity and demonstrated for the first time an inhibitory effect of the protein on intracellular ROS generation in phagocytes.

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The Antioxidative Effect of Heat‐Shock Protein 70 in Dendritic Cells

Cited by 3 publications

References 50 publications

Neuroprotective effects of Argon are mediated via an ERK‐1/2 dependent regulation of heme‐oxygenase‐1 in retinal ganglion cells

Neuroprotective effects of Argon are mediated via an ERK‐1/2 dependent regulation of heme‐oxygenase‐1 in retinal ganglion cells

S-Glutathionylation of human inducible Hsp70 reveals a regulatory mechanism involving the C-terminal α-helical lid

Modulating effect of extracellular HSP70 on generation of reactive oxigen species in populations of phagocytes

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