Isolation of glyoxalase II from two different compartments of rat liver mitochondria. Kinetic and immunochemical characterization of the enzymes

Talesa, Vincenzo; Uotila, Lasse; Koivusalo, Martti; Principato, Giovanni; Giovannini, Elvio; Rosi, Gabriella

doi:10.1016/0304-4165(89)90135-9

Cited by 36 publications

(30 citation statements)

References 21 publications

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“…The mechanism proposed for the glyoxalase IIcatalysed reaction involves an active site histidine residue. (1984, 1985, 1987a,b), Talesa et al (1988Talesa et al ( , 1989, Uotila (1973Uotila ( , 1979 (Ball & Vander Jagt, 1981). This is in keeping with the nucleophilicity of the imidazole group and the reactivity of N-acylimidazoles towards hydrolysis (Hall et al, 1978;Jencks & Carriuolo, 1959) (Fig.…”

Section: Glyoxalase IIsupporting

confidence: 65%

The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life

Thornalley

1990

Biochemical Journal

732

502

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Section: Glyoxalase IIsupporting

confidence: 65%

The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life

Thornalley

1990

Biochemical Journal

732

502

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“…Previous studies suggested that a pool of glyoxalase II that is immunologically related to the cytosolic form is present in the intermembrane space (9,11), in contrast to the matrix distribution observed above. To determine whether the subcompartments of the mitochondria can be adequately resolved by confocal fluorescence microscopy, pGII-DsRed2 was co-expressed with GFP-tagged carnitine palmitoyltransferase I (CPT-EGFP), a fusion protein previously used as an outer membrane marker (20).…”

Section: Resultsmentioning

confidence: 69%

“…Previous studies of rat liver mitochondria reported that multiple isoforms of glyoxalase II were present in the intermembrane space and matrix (9,11). Although the isoforms were similar in size, only glyoxalase II present in the intermembrane space was reported to react with an antiserum raised to the polymerized cytosolic enzyme, whereas matrix glyoxalase II was found to be antigenically distinct (11), however, primary data was not shown.…”

Section: Fig 3 Immunoblotting Of Glyoxalase Ii-luciferase Fusion Prmentioning

confidence: 85%

“…Although the isoforms were similar in size, only glyoxalase II present in the intermembrane space was reported to react with an antiserum raised to the polymerized cytosolic enzyme, whereas matrix glyoxalase II was found to be antigenically distinct (11), however, primary data was not shown. In contrast, we find that the mitochondrial targeting sequence present on glyoxalase II would give rise to a matrix form having 260 amino acids in common with the cytosolic form and so would be expected to be immunochemically similar.…”

Section: Fig 3 Immunoblotting Of Glyoxalase Ii-luciferase Fusion Prmentioning

confidence: 94%

“…The function of the mitochondrial pool of glyoxalase II activity is unknown. Of interest, glyoxalase I appears to be absent from mitochondria in the rat (9,11), however, S-D-lactoylglutathione has been detected in the mitochondria (12) and so may ultimately provide a substrate for glyoxalase II.…”

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confidence: 99%

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The Human Hydroxyacylglutathione Hydrolase (HAGH) Gene Encodes Both Cytosolic and Mitochondrial Forms of Glyoxalase II

Cordell¹,

Futers

Grant

et al. 2004

Journal of Biological Chemistry

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In yeast and higher plants, separate genes encode the cytosolic and mitochondrial forms of glyoxalase II. In contrast, although glyoxalase II activity has been detected both in the cytosol and mitochondria of mammals, only a single gene encoding glyoxalase II has been identified. Previously it was thought that this gene (the hydroxyacylglutathione hydrolase gene), comprised 8 exons that are transcribed into mRNA and that the resulting mRNA species encoded a single cytosolic form of glyoxalase II. Here we show that this gene gives rise to two distinct mRNA species transcribed from 9 and 10 exons, respectively. The 9-exon-derived transcript encodes two protein species: mitochondrially targeted glyoxylase II, which is initiated from an AUG codon in a previously uncharacterized part of the mRNA sequence, and cytosolic glyoxalase II, which is initiated by internal ribosome entry at a downstream AUG codon. The transcript deriving from 10 exons has an in-frame termination codon between the two initiating AUG codons and hence only encodes the cytosolic form of the protein. Confocal fluorescence microscopy indicates that the mitochondrially targeted form of glyoxalase II is directed to the mitochondrial matrix. Analysis of glyoxalase II mRNA sequences from a number of species indicates that dual initiation from alternative AUG codons is conserved throughout vertebrates.

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Specific interaction of cytosolic and mitochondrial glyoxalase II with acidic phospholipids in form of liposomes results in the inhibition of the cytosolic enzyme only

et al. 2000

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Kinetics of cytosolic recombinant human glyoxalase II and bovine liver mitochondrial glyoxalase II were studied in the presence of liposomes made of different phospholipids (PLs). Neutral PLs such as egg phosphatidylcholine or dipalmitoylphosphatidylcholine did not affect the enzymatic activity of either enzymatic form. Liposomes made of dioleoyl phosphatidic acid or cardiolipin or phosphatidylserine also did not affect the enzymatic activity of mitochondrial glyoxalase II. Conversely, these negatively charged PLs exerted noncompetitive inhibition on cytosolic glyoxalase II only, dioleoyl phosphatidic acid and bovine brain phosphatidylserine exerting the highest and lowest inhibition, respectively. Binding studies, carried out by using a resonant mirror biosensor, revealed that liposomes made of negatively charged PLs interact specifically with both enzymatic forms of glyoxalase II, whereas interactions were not detected with neutral PLs. Once bound on glyoxalase II, negatively charged liposomes could not be removed by 3 M NaCl, suggesting that interactions between glyoxalase II and negatively charged PLs, besides ionic, may be also hydrophobic. These data suggest a possible role of negatively charged phospholipids in the regulation of level of lactoylglutathione in the cell. The data are also discussed in terms of a possible regulation of reduced glutathione supply to mitochondria. Proteins 2000;41:33–39. © 2000 Wiley‐Liss, Inc.

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Isolation of glyoxalase II from two different compartments of rat liver mitochondria. Kinetic and immunochemical characterization of the enzymes

Cited by 36 publications

References 21 publications

The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life

The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life

The Human Hydroxyacylglutathione Hydrolase (HAGH) Gene Encodes Both Cytosolic and Mitochondrial Forms of Glyoxalase II

Specific interaction of cytosolic and mitochondrial glyoxalase II with acidic phospholipids in form of liposomes results in the inhibition of the cytosolic enzyme only

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