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PMID: 7447929 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Role of cytoplasmic thioltransferase in cellular regulation by thiol-disulphide interchange.

The Biochemical journal ·Vol. 190 ·No. 1 ·1980-07-15 ·Pages 125-30

Mannervik B, Axelsson K

Abstract

Cytoplasmic thioltransferase purified from rat liver [Axelsson, Eriksson & Mannervik (1978) Biochemistry 17, 2978--2984] catalyses the formation and decomposition of mixed disulphides of proteins and glutathione. The enzyme was found to catalyse the reversible thiol-disulphide interchange between glutathione disulphide and a crude thiol-containing protein fraction from rat liver. This finding indicates a role of the thioltransferase in the regulation of the 'glutathione status' of the cell. Specifically, it was found that thioltransferase catalyses the reactivation of pyruvate kinase from rat liver that had previously been inactivated by glutathione disulphide. It is suggested that thioltransferase may have a general role in regulatory processes involving thiol-disulphide interchange.

MeSH Terms

Animals Cytoplasm/enzymology Disulfides/metabolism Enzyme Activation/drug effects Glutaredoxins Glutathione/metabolism,pharmacology In Vitro Techniques Liver/enzymology Oxidoreductases/metabolism Protein Disulfide Reductase (Glutathione) Proteins/metabolism Pyruvate Kinase/metabolism Rats Sulfhydryl Compounds/metabolism Transferases/pharmacology

Chemicals

Disulfides Glutaredoxins Proteins Sulfhydryl Compounds Oxidoreductases Protein Disulfide Reductase (Glutathione) Transferases Pyruvate Kinase Glutathione

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Mannervik B

Axelsson K

References (23)

23 references, click to expand

Regulation of fructose diphosphatase activity by disulfide exchange.
Proc Natl Acad Sci U S A. 1967 Jul;58(1):286-93 PMID: 4292102
Cellular mixed disulphides between thiols and proteins, and their possible implication for radiation protection.
Biochem Pharmacol. 1968 Feb;17(2):177-86 PMID: 5647044
Regulatory sulfhydryl groups and activation by homocystine in liver fructose diphosphatase.
Arch Biochem Biophys. 1970 Dec;141(2):579-87 PMID: 4322288
Control of -aminolevulinate synthetase activity in Rhodopseudomonas spheroides. II. Requirement of a disulfide compound for the conversion of the inactive form of fraction I to the active form.
Arch Biochem Biophys. 1972 Jun;150(2):690-7 PMID: 4537847
Mechanism of action of pyruvate kinase. Role of sulfhydryl groups in catalytic activity as determined by disulfide interchange.
J Biol Chem. 1972 Dec 25;247(24):8114-21 PMID: 4640939
Two interconvertible forms of L-type pyruvate kinase from rat liver.
Biochim Biophys Acta. 1973 Jan 12;293(1):118-24 PMID: 4685271
Regulation of rat liver glycogen synthetase. Reversible inactivation of glycogen synthetase D by sulfhydryl-disulfide exchange.
J Biol Chem. 1973 Mar 10;248(5):1550-5 PMID: 4632914
The occurrence of protein-bound mixed disulfides in rat tissues.
Biochim Biophys Acta. 1973 May 17;310(1):104-10 PMID: 4710586
Synthesis of a mixed disulfide of egg white lysozyme and glutathione - a model substrate for enzymatic reduction of protein mixed disulfides.
FEBS Lett. 1975 Apr 15;53(1):40-3 PMID: 1095406
[The status of glutathione of the rat liver and its dependence on the age and acute stress].
Z Naturforsch C. 1974 May-Jun;29(5-6):261-6 PMID: 4283042
Reduction of disulphide bonds in proteins mixed disulphides catalysed by a thioltransferase in rat liver cytosol.
Biochem J. 1975 Sep;149(3):785-8 PMID: 1201003
Glutathione dependent control of protein disulfide-sulfhydryl content by subcellular fractions of hepatic tissue.
Biochim Biophys Acta. 1977 Mar 29;497(1):192-204 PMID: 557349
Cyclic AMP-dependent control of the rat hepatic glutathione disulfide-sulfhydryl ratio.
Biochim Biophys Acta. 1977 Jun 23;498(1):29-38 PMID: 18207
Inhibition of gamma-glutamylcysteine synthetase by cystamine: an approach to a therapy of 5-oxoprolinuria (pyroglutamic aciduria).
Biochem Biophys Res Commun. 1977 Dec 7;79(3):919-25 PMID: 23121
Purification and characterization of cytoplasmic thioltransferase (glutathione:disulfide oxidoreductase) from rat liver.
Biochemistry. 1978 Jul 25;17(15):2978-84 PMID: 698179
Inactivation of phosphorylase phosphatase by a factor from rabbit liver and its chemical characterization as glutathione disulfide.
J Biol Chem. 1978 Oct 25;253(20):7376-82 PMID: 212423
Reversible inhibition of adenylate cyclase activity of rat brain caudate nucleus by oxidized glutathione.
Biochem Biophys Res Commun. 1978 Dec 14;85(3):1204-10 PMID: 736960
Glutathione-dependent synthesis of deoxyribonucleotides. Characterization of the enzymatic mechanism of Escherichia coli glutaredoxin.
J Biol Chem. 1979 May 10;254(9):3672-8 PMID: 34620
Phosphorylation-dephosphorylation of enzymes.
Annu Rev Biochem. 1979;48:923-59 PMID: 38740
The glutathione status of cells.
Int Rev Cytol. 1978;54:109-60 PMID: 42630
A possible role of cytoplasmic thioltransferase in the intracellular degradation of disulfide-containing proteins.
Acta Chem Scand B. 1980;34(2):139-40 PMID: 6998236
Tissue sulfhydryl groups.
Arch Biochem Biophys. 1959 May;82(1):70-7 PMID: 13650640
The inhibitory effect at the hexokinase level of disulphides on glucose metabolism in human erythrocytes.
Biochem J. 1962 Aug;84:286-91 PMID: 13889797

Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj1900125

Published

1980-07-15

Pages

125-30

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1162070

Subset

External Links

PubMed source DOI: 10.1042/bj1900125 PMC Full Text View journal details

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Role of cytoplasmic thioltransferase in cellular regulation by thiol-disulphide interchange.

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