Biochemical and Biophysical Research Communications
Regular ArticleRyanodine Receptor Channel-Dependent Glutathione Transport in the Sarcoplasmic Reticulum of Skeletal Muscle☆
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2021, BiomaterialsCitation Excerpt :A small part of GSH enters the subcellular organelles including mitochondria, nucleus, and endoplasmic reticulum [39]. Although the mechanism of GSH transportation into organelles has not been well elucidated, it was reported that the dicarboxylate carrier and the oxoglutarate carrier probably contributed to the transportation of GSH across the mitochondrial inner membrane [162], and the ryanodine receptor type 1 might participate in the accumulation of GSH in endoplasmic reticulum [163]. Part of GSH is transported out of the cells to maintain the dynamic balance of cellular redox level.
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2013, Biochimica et Biophysica Acta - General SubjectsCitation Excerpt :However other studies have questioned whether this might be a consequence of S-glutathionylation of the large number of cysteines in the molecule. Furthermore, the kinetics of glutathione transport across the ER membrane in liver cells is different from that observed in SR in skeletal muscles [21,73]. The mitochondrial pool of GSH is substantial and has been estimated to be almost 10-15% of the cellular pools of glutathione.
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2011, Nutrition ResearchCitation Excerpt :Therefore, sustained calcium leak can lead to derangements in protein folding in the ER lumen because of depletion of luminal calcium stores. Because RyR1 is both regulated by [91] and permeable for glutathione [92,93], its activation by EGCG can be expected to affect the redox environment and hence oxidative folding in the lumen. It can be concluded that the effects of EGCG on ER calcium homeostasis through direct or indirect molecular targets are largely cell type–specific because of different PLC isoenzymes, SERCA pumps, and Ca2+ channels.
Plasma membrane glutathione transporters and their roles in cell physiology and pathophysiology
2009, Molecular Aspects of MedicineTransport and transporters in the endoplasmic reticulum
2007, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :The transport was fastest in muscle terminal cisternae, fast in muscle microsomes and slow in liver, heart and brain microsomes. GSH influx could be inhibited by RyR1 blockers, and the inhibitory effect was counteracted by RyR1 agonists [179]. These results suggest that RyR1 may act as glutathione transporter on its own, or may interact with a putative GSH/GSSG transporter.
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Abbreviations used: RyR, ryanodine receptor; ER, endoplasmic reticulum; SR, sarcoplasmic reticulum; GSH, reduced glutathione; GSSG, glutathione disulfide; Mops, 4-morpholinepropanesulfonic acid.
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