Injectable Glutathione Guide (Updated)

Episode 293 is your updated complete guide to injectable glutathione! Glutathione (GSH) has so much misunderstanding and misinformation in our industry that I want to ensure people understand a lot of the interactions and MoA going on with this compound. It has tremendous application as a "health", restoration, and progression tool when utilized in the proper setting. Sit back, take notes, and enjoy the references I'll attach to this episode!   REFERENCES Aniya Y., Imaizumi N. (2011). Mitochondrial glutathione transferases involving a new function for membrane permeability transition pore regulation. Drug Metab. Rev. 43 292–299 Arakane F., King S. R., Du Y., Kallen C. B., Walsh L. P., Watari H., et al. (1997). Phosphorylation of steroidogenic acute regulatory protein (StAR) modulates its steroidogenic activity. J. Biol. Chem. 272 32656–32662 10.1074/jbc.272.51.32656 Armeni T., Cianfruglia L., Piva F., Urbanelli L., Luisa Caniglia M., Pugnaloni A., et al. (2014). S-D-Lactoylglutathione can be an alternative supply of mitochondrial glutathione. Free Radic. Biol. Med. 67 451–459 10.1016/j.freeradbiomed.2013.12.005 Armstrong J. S., Jones D. P. (2002). Glutathione depletion enforces the mitochondrial permeability transition and causes cell death in Bcl-2 overexpressing HL60 cells. FASEB J. 16 1263–1265 10.1096/fj.02-0097fje Baines C. P. (2010). The cardiac mitochondrion: nexus of stress. Annu. Rev. Physiol. 72 61–80 10.1146/annurev-physiol-021909-135929 Baines C. P., Kaiser R. A., Purcell N. H., Blair N. S., Osinska H., Hambleton M. A., et al. (2005). Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature 434 658–662 10.1038/nature03434 Banmeyer I., Marchand C., Clippe A., Knoops B. (2005). Human mitochondrial peroxiredoxin 5 protects from mitochondrial DNA damages induced by hydrogen peroxide. FEBS Lett. 579 2327–2333 10.1016/j.febslet.2005.03.027 Basso E., Fante L., Fowlkes J., Petronilli V., Forte M. A., Bernardi P. (2005). Properties of the permeability transition pore in mitochondria devoid of Cyclophilin D. J. Biol. Chem. 280 18558–18561 10.1074/jbc.C500089200 Beer S. M., Taylor E. R., Brown S. E., Dahm C. C., Costa N. J., Runswick M. J., et al. (2004). Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: implications for mitochondrial redox regulation and antioxidant DEFENSE. J. Biol. Chem. 279 47939–47951 10.1074/jbc.M408011200 Benipal B., Lash L. H. (2013). Modulation of mitochondrial glutathione status and cellular energetics in primary cultures of proximal tubular cells from remnant kidney of uninephrectomized rats. Biochem. Pharmacol. 85 1379–1388 10.1016/j.bcp.2013.02.013 Brand M. D. (2010). The sites and topology of mitochondrial superoxide production. Exp. Gerontol. 45 466–472 10.1016/j.exger.2010.01.003 Brigelius-Flohe R., Maiorino M. (2013). Glutathione peroxidases. Biochim. Biophys. Acta 1830 3289–3303 10.1016/j.bbagen.2012.11.020 Casagrande S., Bonetto V., Fratelli M., Gianazza E., Eberini I., Massignan T., et al. (2002). Glutathionylation of human thioredoxin: a possible crosstalk between the glutathione and thioredoxin systems. Proc. Natl. Acad. Sci. U.S.A. 99 9745–9749 10.1073/pnas.152168599 Chang T. S., Cho C. S., Park S., Yu S., Kang S. W., Rhee S. G. (2004). Peroxiredoxin III, a mitochondrion-specific peroxidase, regulates apoptotic signaling by mitochondria. J. Biol. Chem. 279 41975–41984 10.1074/jbc.M407707200 Garcia-Ruiz C., Fernandez-Checa J. C. (2006). Mitochondrial glutathione: hepatocellular survival-death switch. J. Gastroenterol. Hepatol. 21(Suppl. 3) S3–S6 10.1111/j.1440-1746.2006.04570. Garcia-Ruiz C., Morales A., Ballesta A., Rodes J., Kaplowitz N., Fernandez-Checa J. C. (1994). Effect of chronic ethanol feeding on glutathione and functional integrity of mitochondria in periportal and perivenous rat hepatocytes. J. Clin. Invest. 94 193–201 10.1172/JCI117306 Griffith O. W., Meister A. (1985). Origin and turnover of mitochondrial glutathione. Proc. Natl. Acad. Sci. U.S.A. 82 4668–4672 10.1073/pnas.82.14.4668 Kokoszka J. E., Waymire K. G., Levy S. E., Sligh J. E., Cai J., Jones D. P., et al. (2004). The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore. Nature 427 461–465 10.1038/nature02229 Kroemer G., Galluzzi L., Brenner C. (2007). Mitochondrial membrane permeabilization in cell death. Physiol. Rev. 87 99–163 10.1152/physrev.00013.2006 Kulawiak B., Hopker J., Gebert M., Guiard B., Wiedemann N., Gebert N. (2013). The mitochondrial protein import machinery has multiple connections to the respiratory chain. Biochim. Biophys. Acta 1827 612–626 10.1016/j.bbabio.2012.12.004 Lash L. H. (2006). Mitochondrial glutathione transport: physiological, pathological and toxicological implications. Chem. Biol. Interact. 163 54–67 10.1016/j.cbi.2006.03.001 Miller W. L. (2013). Steroid hormone synthesis in mitochondria. Mol. Cell. Endocrinol. 379 62–73 10.1016/j.mce.2013.04.014 Muller F. L., Lustgarten M. S., Jang Y., Richardson A, Van Remmen H. (2007). Trends in oxidative aging theories. Free Radic. Biol. Med. 43 477–503 10.1016/j.freeradbiomed.2007.03.034 Munoz-Pinedo C., Guio-Carrion A., Goldstein J. C., Fitzgerald P., Newmeyer D. D., Green D. R. (2006). Different mitochondrial intermembrane space proteins are released during apoptosis in a manner that is coordinately initiated but can vary in duration. Proc. Natl. Acad. Sci. U.S.A. 103 11573–11578 10.1073/pnas.0603007103 Schumacker P. T. (2006). Reactive oxygen species in cancer cells: live by the sword, die by the sword. Cancer Cell 10 175–176 10.1016/j.ccr.2006.08.015 Sena L. A., Chandel N. S. (2012). Physiological roles of mitochondrial reactive oxygen species. Mol. Cell 48 158–167 10.1016/j.molcel.2012.09.025 Serviddio G., Bellanti F., Tamborra R., Rollo T., Capitanio N., Romano A. D., et al. (2008). Uncoupling protein-2 (UCP2) induces mitochondrial proton leak and increases susceptibility of non-alcoholic steatohepatitis (NASH) liver to ischaemia-reperfusion injury. Gut 57 957–965 10.1136/gut.2007.147496 Venditti P., Di Stefano L, Di Meo S. (2013). Mitochondrial metabolism of reactive oxygen species. Mitochondrion 13 71–82 10.1016/j.mito.2013.01.008 Yin F., Sancheti H., Cadenas E. (2012). Mitochondrial thiols in the regulation of cell death pathways. Antioxid. Redox Signal. 17 1714–1727 10.1089/ars.2012.4639 Yue P., Zhou Z., Khuri F. R., Sun S. Y. (2006). Depletion of intracellular glutathione contributes to JNK-mediated death receptor 5 upregulation and apoptosis induction by the novel synthetic triterpenoid methyl-2-cyano-3, 12-dioxooleana-1, 9-dien-28-oate (CDDO-Me). Cancer Biol. Ther. 5 492–497 10.4161/cbt.5.5.2565 Zhao P., Kalhorn T. F., Slattery J. T. (2002). Selective mitochondrial glutathione depletion by ethanol enhances acetaminophen toxicity in rat liver. 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