Redox-assisted regulation of Ca
            <sup>2+</sup>
            homeostasis in the endoplasmic reticulum by disulfide reductase ERdj5

Ushioda, Ryo; Miyamoto, Akitoshi; Inoue, Masayasu; Watanabe, Satoshi; Okumura, Masaki; Maegawa, Ken Ichi; Uegaki, Kaiku; Fujii, Shohei; Fukuda, Yasuko; Umitsu, Masatomo; Takagi, Junichi; Inaba, Kenji; Mikoshiba, Katsuhiko; Nagata, Kazuhiro

doi:10.1073/pnas.1605818113

Cited by 77 publications

(98 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…ERdj5 not only recognizes misfolded proteins in the ER lumen, it activates an ER membrane calcium pump, regulating Ca 2+ uptake and, thus, cellular calcium homeostasis. It does so by reduction of critical disulfide bonds in the pump using its thioredoxin-like domains, independent of J-domain activity [71]. It remains to be resolved whether in the course of the J-protein evolution these J-domain independent functions emerged early or late.…”

Section: Do J-proteins Sometimes Go It Alone?mentioning

confidence: 99%

How Do J-Proteins Get Hsp70 to Do So Many Different Things?

Craig

Marszałek

2017

Trends in Biochemical Sciences

171

184

View full text Add to dashboard Cite

Hsp70 chaperone machineries play pivotal roles in a wide array of fundamental biological processes, through their facilitation of protein folding, disaggregation and remodeling. Hsp70’s obligate J-protein co-chaperones drive much of this remarkable multi-functionality, with most Hsp70s having multiple J-protein partners. Recent data suggest that J-protein-driven versatility is substantially due to precise localization within the cell and specificity of substrate protein binding. However, this relatively simple view belies the intricacy of J-protein function. Examples are emerging of J-protein interactions with Hsp70 and other chaperones, as well as integration into broader cellular networks. These interactions fine-tune, in critical ways, the ability of Hsp70 to participate in diverse cellular processes.

show abstract

Section: Do J-proteins Sometimes Go It Alone?mentioning

confidence: 99%

How Do J-Proteins Get Hsp70 to Do So Many Different Things?

Craig

Marszałek

2017

Trends in Biochemical Sciences

171

184

View full text Add to dashboard Cite

show abstract

“…; Ushioda et al. ). Oxidation of protein sulfhydryl groups diminishes Ca 2+ ‐ATPase activity (Horakova et al.…”

Section: Discussionmentioning

confidence: 96%

“…; Ushioda et al. ). Yet the concomitant addition of reducing compounds (GSH or DTT) failed to prevent the NADP restriction of uptake‐ this infers that the nucleotide effect on uptake was extraneous to the generation of ROS, thereby inhibiting SERCA.…”

Section: Discussionmentioning

confidence: 96%

“…Both the cytosolic and ER redox states can modulate not only ER calcium exit channels, but also uptake via transporter calcium ATPases (e.g. SERCA2b) (Morris and Sulakhe 1997;Xu et al 1997;Li and Camacho 2004;Zima et al 2004;Gorlach et al 2006;Ozawa 2010;Gorlach et al 2015;Ushioda et al 2016). Oxidation of protein sulfhydryl groups diminishes Ca 2+ -ATPase activity (Horakova et al 2013).…”

Section: Discussionmentioning

confidence: 99%

“…Of note, if ATP is omitted there was no microsomal calcium uptake. The effect of various redox modifiers (at 1 mmol/L) on calcium uptake were tested, including: ascorbate (Vergauwen et al 2015;Chen and Chang 2018), GSH and GSSG (Jessop and Bulleid 2004;Saaranen et al 2010;Foyer and Noctor 2011), dehydroascorbate (DHA) (Csala et al 1999;Saaranen et al 2010;Foyer and Noctor 2011), H 2 O 2 (Xu et al 1997;Csala et al 1999), and dithiothreitol (DTT) (Ushioda et al 2016).…”

Section: Calcium Uptakementioning

confidence: 99%

See 2 more Smart Citations

Pyridine nucleotide regulation of hepatic endoplasmic reticulum calcium uptake

2019

View full text Add to dashboard Cite

Pyridine nucleotides serve an array of intracellular metabolic functions such as, to name a few, shuttling electrons in enzymatic reactions, safeguarding the redox state against reactive oxygen species, cytochrome P450 (CYP) enzyme detoxification pathways and, relevant to this study, the regulation of ion fluxes. In particular, the maintenance of a steep calcium gradient between the cytosol and endoplasmic reticulum ( ER ), without which apoptosis ensues, is achieved by an elaborate combination of energy–requiring ER membrane pumps and efflux channels. In liver microsomes, net calcium uptake was inhibited by physiological concentrations of NADP . In the presence of 1 mmol/L NADP , calcium uptake was attenuated by nearly 80%, additionally, this inhibitory effect was blunted by concomitant addition of NADPH . No other nicotinamide containing compounds ‐save a slight inhibition by NAADP ‐hindered calcium uptake; thus, only oxidized pyridine nucleotides, or related compounds with a phosphate moiety, had an imposing effect. Moreover, the NADP inhibition was evident even after selectively blocking ER calcium efflux channels. Given the fundamental role of endoplasmic calcium homeostasis, it is plausible that changes in cytosolic NADP concentration, for example, during anabolic processes, could regulate net ER calcium uptake.

show abstract

Potential issues specific to cytotoxicity tests of cellulose nanofibrils

Moriyama

Ogura

Fujita

2022

J of Applied Toxicology

View full text Add to dashboard Cite

Cellulose nanofibrils (also called cellulose nanofibers or nanofibrillated cellulose [CNFs]) are novel polymers derived from biomass with excellent physicochemical properties and various potential applications. However, the introduction of such new materials into the market requires thorough safety studies to be conducted. Recently, toxicity testing using cultured cells has attracted attention as a safety assessment that does not rely on experimental animals. This article reviews recent information regarding the cytotoxicity testing of CNFs and highlights the issues relevant to evaluating tests. In the literature, we found that a variety of cell lines and CNF exposure concentrations was evaluated. Furthermore, the results of cytotoxicity results tests differed and were not necessarily consistent. Numerous reports that we examined had not evaluated endotoxin/microbial contamination or the interaction of CNFs with the culture medium used in the tests. The following potential specific issues involved in CNF in vitro testing, were discussed: (1) endotoxin contamination, (2) microbial contamination, (3) adsorption of culture medium components to CNFs, and (4) changes in aggregation/agglomeration and dispersion states of CNFs resulting from culture medium components. In this review, the available measurement methods and solutions for these issues are also discussed. Addressing these points will lead to a better understanding of the cellular effects of CNFs and the development of safer CNFs.

show abstract

Redox-assisted regulation of Ca ²⁺ homeostasis in the endoplasmic reticulum by disulfide reductase ERdj5

Cited by 77 publications

References 43 publications

How Do J-Proteins Get Hsp70 to Do So Many Different Things?

How Do J-Proteins Get Hsp70 to Do So Many Different Things?

Pyridine nucleotide regulation of hepatic endoplasmic reticulum calcium uptake

Potential issues specific to cytotoxicity tests of cellulose nanofibrils

Contact Info

Product

Resources

About

Redox-assisted regulation of Ca 2+ homeostasis in the endoplasmic reticulum by disulfide reductase ERdj5

Cited by 77 publications

References 43 publications

How Do J-Proteins Get Hsp70 to Do So Many Different Things?

How Do J-Proteins Get Hsp70 to Do So Many Different Things?

Pyridine nucleotide regulation of hepatic endoplasmic reticulum calcium uptake

Potential issues specific to cytotoxicity tests of cellulose nanofibrils

Contact Info

Product

Resources

About

Redox-assisted regulation of Ca ²⁺ homeostasis in the endoplasmic reticulum by disulfide reductase ERdj5