Uncoupled redox systems in the lumen of the endoplasmic reticulum

Pyridine nucleotides stay reduced in an oxidative environment

Simona Piccirella, Ibolya Czegle, Beáta Lizák, E. Margittai, Silvia Senesi, Eszter Papp, M. Csala, Rosella Fulceri, P. Csermely, J. Mandl, Angelo Benedetti, G. Bánhegyi

Research output: Contribution to journalArticle

66 Citations (Scopus)

Abstract

The redox state of the intraluminal pyridine nucleotide pool was investigated in rat liver microsomal vesicles. The vesicles showed cortisone reductase activity in the absence of added reductants, which was dependent on the integrity of the membrane. The intraluminal pyridine nucleotide pool could be oxidized by the addition of cortisone or metyrapone but not of glutathione. On the other hand, intraluminal pyridine nucleotides were slightly reduced by cortisol or glucose 6-phosphate, although glutathione was completely ineffective. Redox state of microsomal protein thiols/disulfides was not altered either by manipulations affecting the redox state of pyridine nucleotides or by the addition of NAD(P)+ or NAD(P)H. The uncoupling of the thiol/disulfide and NAD(P)+/NAD(P)H redox couples was not because of their subcompartmentation, because enzymes responsible for the intraluminal oxidoreduction of pyridine nucleotides were distributed equally in smooth and rough microsomal subfractions. Instead, the phenomenon can be explained by the negligible representation of glutathione reductase in the endoplasmic reticulum lumen. The results demonstrated the separate existence of two redox systems in the endoplasmic reticulum lumen, which explains the contemporary functioning of oxidative folding and of powerful reductive reactions.

Original languageEnglish
Pages (from-to)4671-4677
Number of pages7
JournalJournal of Biological Chemistry
Volume281
Issue number8
DOIs
Publication statusPublished - Feb 24 2006

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Endoplasmic Reticulum
Oxidation-Reduction
Nucleotides
NAD
Sulfhydryl Compounds
Disulfides
Cortisone Reductase
Glutathione
Metyrapone
Glucose-6-Phosphate
Glutathione Reductase
Cortisone
Reducing Agents
Liver
Hydrocortisone
Rats
pyridine
Membranes
Enzymes
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Uncoupled redox systems in the lumen of the endoplasmic reticulum : Pyridine nucleotides stay reduced in an oxidative environment. / Piccirella, Simona; Czegle, Ibolya; Lizák, Beáta; Margittai, E.; Senesi, Silvia; Papp, Eszter; Csala, M.; Fulceri, Rosella; Csermely, P.; Mandl, J.; Benedetti, Angelo; Bánhegyi, G.

In: Journal of Biological Chemistry, Vol. 281, No. 8, 24.02.2006, p. 4671-4677.

Research output: Contribution to journalArticle

Piccirella, Simona ; Czegle, Ibolya ; Lizák, Beáta ; Margittai, E. ; Senesi, Silvia ; Papp, Eszter ; Csala, M. ; Fulceri, Rosella ; Csermely, P. ; Mandl, J. ; Benedetti, Angelo ; Bánhegyi, G. / Uncoupled redox systems in the lumen of the endoplasmic reticulum : Pyridine nucleotides stay reduced in an oxidative environment. In: Journal of Biological Chemistry. 2006 ; Vol. 281, No. 8. pp. 4671-4677.
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