دورية أكاديمية

Intracellular glutathione pools are heterogeneously concentrated.

التفاصيل البيبلوغرافية
العنوان: Intracellular glutathione pools are heterogeneously concentrated.
المؤلفون: Montero D; Division of Molecular & Systems Toxicology, Department of Pharmaceutical Sciences, University of Basel, Klingelbergstrasse 50, 4056 Basel, Switzerland., Tachibana C, Rahr Winther J, Appenzeller-Herzog C
المصدر: Redox biology [Redox Biol] 2013 Oct 28; Vol. 1, pp. 508-13. Date of Electronic Publication: 2013 Oct 28 (Print Publication: 2013).
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Elsevier, B.V Country of Publication: Netherlands NLM ID: 101605639 Publication Model: eCollection Cited Medium: Internet ISSN: 2213-2317 (Electronic) Linking ISSN: 22132317 NLM ISO Abbreviation: Redox Biol Subsets: MEDLINE
أسماء مطبوعة: Original Publication: [Amsterdam]: Elsevier, B.V., [2013]-
مواضيع طبية MeSH: Endoplasmic Reticulum/*metabolism , Glutaredoxins/*metabolism , Glutathione/*metabolism, Cytosol/metabolism ; Glutaredoxins/genetics ; HeLa Cells ; Homeostasis ; Humans
مستخلص: Glutathione is present in millimolar concentrations in the cell, but its relative distribution among cellular compartments remains elusive. We have chosen the endoplasmic reticulum (ER) as an example organelle to study compartment-specific glutathione levels. Using a glutaredoxin sensor (sCGrx1pER), which rapidly and specifically equilibrates with the reduced glutathione (GSH)-glutathione disulfide (GSSG) redox couple with known equilibrium constant, we showed that the [GSH]:[GSSG] ratio in the ER of intact HeLa cells is less than 7:1. Taking into consideration the previously determined value for [GSH](2):[GSSG] in the ER of 83 mM, this translates into a total glutathione concentration in the ER ([GStot]=[GSH]+2[GSSG]) of greater than 15 mM. Since the integrated, intracellular [GStot] was measured as ~7 mM, we conclude the existence of a [GStot] gradient across the ER membrane. A possible homeostatic mechanism by which cytosol-derived glutathione is trapped in the ER is discussed. We propose a high [GStot] as a distinguishing feature of the ER environment compared to the extracellular space.
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فهرسة مساهمة: Keywords: DTT, Dithiothreitol; EGSH, Half cell reduction potential of glutathione; ER, Endoplasmic reticulum; Endoplasmic reticulum; GSH, Reduced glutathione; GSSG, Glutathione disulfide; Glutaredoxin; Glutathione; NEM, N-ethylmaleimide; OxD, Percentage of oxidation; PDI, Protein disulfide isomerase; PERK, Double stranded RNA-activated protein kinase (PKR)-like ER kinase; RGS, [GSH]:[GSSG]; Redox Homeostasis; Redox compartmentalization; Redox, Reduction–oxidation; Reduction potential; TMM(PEG)12, Maleimide-activated polyethylene glycol; UPR, Unfolded protein response; XBP1, X-box binding protein 1; [GStot], Total glutathione concentration; sCGrx1p, C30S mutant of yeast glutaredoxin 1
Note: Original DateCompleted: 20131119
المشرفين على المادة: 0 (Glutaredoxins)
GAN16C9B8O (Glutathione)
تواريخ الأحداث: Date Created: 20131120 Date Completed: 20150513 Latest Revision: 20211021
رمز التحديث: 20221213
مُعرف محوري في PubMed: PMC3830055
DOI: 10.1016/j.redox.2013.10.005
PMID: 24251119
قاعدة البيانات: MEDLINE
الوصف
تدمد:2213-2317
DOI:10.1016/j.redox.2013.10.005