Role of Metal Contaminants in the Mitochondrial Swelling Activities of Reduced and Oxidized Glutathione Preparations

Cash, William D.; Gardy, Martin

doi:10.1016/s0021-9258(18)97240-6

Cited by 15 publications

(2 citation statements)

References 9 publications

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“…Whether the catalytic activity of some GSSG samples is due to selenium contaminants is not known at present, but the possibility of GSSeSG or other selenium impurities should not be ruled out. Substantial variation in the content of trace mineral contaminants in commercial samples of glutathione has been reported (Cash and Gardy, 1965). It should also be pointed out that different commercial samples of GSSG have different potencies as mitochondrial swelling agents (Levander et al, 1972) and that those samples of GSSG which are most effective as swelling agents are those which are also generally most effective as catalysts in the reduction of cytochrome c by GSH.…”

Section: Discussionmentioning

confidence: 99%

Selenium as a catalyst for the reduction of cytochrome c by glutathion

Levander¹,

Morris²,

Higgs³

1973

Biochemistry

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Selenite at 10-5-10-6 M is a n effective catalyst for the reduction of cytochrome c by glutathione (GSH). Selenocystine was more effective and selenate less effective than selenite. Selenomethionine had no catalytic effect. A strong catalysis of selenite on the reduction of cytochrome c was still observed when mercaptoethylamine or cysteine replaced GSH as the thiol, but smaller catalytic effects of Se were seen when thioglycolate or mercaptoethanol was used in lieu of GSH. Cysteine was a more active reductant for cytochrome c than GSH either in the presence or absence of Se. Dithiothreitol and 2,3-dimercaptopropanol were both potent reducing agents for cytochrome c without Se, but a catalytic

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Section: Discussionmentioning

confidence: 99%

Selenium as a catalyst for the reduction of cytochrome c by glutathion

Levander¹,

Morris²,

Higgs³

1973

Biochemistry

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“…Although there has been interest in mitochondrial GSH since the 1960s [17][18][19][20][21] and identification of a distinctly regulated mitochondrial pool was first reported in the early 1980s, 10 the concept that GSH was transported into mitochondria was not considered until about 1990. 22,23 A few other studies in that era 24,25 demonstrated different activities of mitochondrial GSH transport under different redox or energetic conditions.…”

Section: Pathways Of Gsh Transport Into Renal Mitochondriamentioning

confidence: 99%

Mitochondrial glutathione in toxicology and disease of the kidneys

Lash

2012

Toxicology Research

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The tripeptide glutathione (GSH), comprised of the amino acids l-cysteine, glycine, and l-glutamate, is found in all cells of aerobic organisms and plays numerous, critical roles as an antioxidant and nucleophile in regulating cellular homeostasis and drug metabolism. GSH is synthesized exclusively in the cytoplasm of most cells by two ATP-dependent reactions. Despite this compartmentation, GSH is found in other subcellular compartments, including mitochondria. As the GSH molecule has a net negative charge at physiological pH, it cannot cross cellular membranes by diffusion. Rather, GSH is a substrate for a variety of anion and amino acid transporters. Two organic anion carriers in the inner membrane of renal mitochondria, the dicarboxylate carrier (DIC; Slc25a10) and the 2-oxoglutarate carrier (OGC; Slc25a11), are responsible for most of the transport of GSH from cytoplasm into mitochondrial matrix. Genetic manipulation of DIC and/or OGC expression in renal cell lines demonstrated the ability to produce sustained increases in mitochondrial GSH content, which then protected these cells from cytotoxicity due to several oxidants and mitochondrial toxicants. Several diseases and pathological states are associated with mitochondrial dysfunction and oxidative stress, suggesting that the mitochondrial GSH pool may be a therapeutic target. One such disease that is of particular concern for public health is diabetic nephropathy. Another chronic, pathological state that is associated with bioenergetic and redox changes is compensatory renal hypertrophy that results from reductions in functional renal mass. This review summarizes pathways of mitochondrial GSH transport and discusses studies on its manipulation in toxicological and pathological states.

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