The detection of S-glutathionation of hepatic carbonic anhydrase III in rats treated with paraquat or diquat

Lii, Chong‐Kuei; Wang, Shih-Tsung; Chen, Haw‐Wen

doi:10.1016/0378-4274(95)03621-0

Cited by 7 publications

(4 citation statements)

References 30 publications

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“…The expression patterns of MoCA1 increased under oxidative stress, that is, H 2 O 2 and NaHCO 3 stress ( Figures 2D , E ) show its potential cellular defense system under oxidative stress. This property was mostly found to be a major function of carbonic anhydrase III ( Lii et al, 1996 ), however, CA Nce103p of yeast S. cerevisiae also showed tolerance to oxidative stress ( Götz et al, 1999 ). Furthermore, the accumulation of internal ROS in hyphae of MoCA1 deleted strains compared to wild type ( Figures 5A , C ) showed the disruption of CO 2 /HCO 3 − /pH sensing mechanism thus modulating the fungal aerobic metabolism that leads to the accumulation of excessive ROS in mutant.…”

Section: Discussionmentioning

confidence: 99%

Contribution of the Mitochondrial Carbonic Anhydrase (MoCA1) to Conidiogenesis and Pathogenesis in Magnaporthe oryzae

Dang

Batool

et al. 2022

Front. Microbiol.

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The interconversion of CO2 and HCO3− catalyzed by carbonic anhydrases (CAs) is a fundamental biochemical process in organisms. During mammalian–pathogen interaction, both host and pathogen CAs play vital roles in resistance and pathogenesis; during planta–pathogen interaction, however, plant CAs function in host resistance but whether pathogen CAs are involved in pathogenesis is unknown. Here, we biologically characterized the Magnaporthe oryzae CA (MoCA1). Through detecting the DsRED-tagged proteins, we observed the fusion MoCA1 in the mitochondria of M. oryzae. Together with the measurement of CA activity, we confirmed that MoCA1 is a mitochondrial zinc-binding CA. MoCA1 expression, upregulated with H2O2 or NaHCO3 treatment, also showed a drastic upregulation during conidiogenesis and pathogenesis. When MoCA1 was deleted, the mutant ΔMoCA1 was defective in conidiophore development and pathogenicity. 3,3′-Diaminobenzidine (DAB) staining indicated that more H2O2 accumulated in ΔMoCA1; accordingly, ATPase genes were downregulated and ATP content decreased in ΔMoCA1. Summarily, our data proved the involvement of the mitochondrial MoCA1 in conidiogenesis and pathogenesis in the rice blast fungus. Considering the previously reported HCO3− transporter MoAE4, we propose that MoCA1 in cooperation with MoAE4 constitutes a HCO3− homeostasis-mediated disease pathway, in which MoCA1 and MoAE4 can be a drug target for disease control.

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Section: Discussionmentioning

confidence: 99%

Contribution of the Mitochondrial Carbonic Anhydrase (MoCA1) to Conidiogenesis and Pathogenesis in Magnaporthe oryzae

Dang

Batool

et al. 2022

Front. Microbiol.

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“…We believe that these are unmodified and acidic forms of CAIII. Rat liver CAIII has namely been shown to undergo posttranslational modifications in vivo, involving oxidative S-thiolation (a mixed disulfide between a cysteine residue and glutathione) (5,14,19), and carbonylation (the introduction of aldehydes and ketones into certain amino acid residues of the enzyme) (1). S-thiolation is a reversible process, and occurs at two reactive sulfhydryl groups (8), localised on residues 181 and 186 (9).…”

Section: Charge Isoforms Of Caiiimentioning

confidence: 99%

“…CAIII would therefore appear to be a major component of the Sthiolation/dethiolation response to oxidative stress (5). Such a stress occurs when the balance between prooxidants and antioxidants in a cell is disturbed in favour of the prooxidants (14). It is therefore interesting that recent data suggest that CAIII indeed may act as an antioxidant (1,5,17,18).…”

Section: Function Of Caiiimentioning

confidence: 99%

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Carbonic Anhydrase III in Liver and Muscle of Male Rats Purification and Properties

Wistrand

2002

Upsala Journal of Medical Sciences

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Cytosolic carbonic anhydrases CAI, CAII, and CAIII from liver, and CAII, and CAIII from muscle of adult male Sprague-Dawley rats were purified to homogeneity. CAIII from liver and muscle had the same amino acid composition and were immunochemically similar. Their kinetic properties at 0 degrees C were also similar. Km(CO2) was 4 mM and kcat 3x105 s(-1). Ki was 0.4 and 0.2 M for acetazolamide and NaCl, respectively. Both CAIIIs ran as single bands on SDS-electrophoresis and high-speed centrifugation, with a mol wt of 29.3 kDa. Their hydrodynamic properties suggest that CAIII is a compact, nearly spherical molecule. It contained 0.9 M zinc per M protein. In both tissues isoelectric focusing identified neutral and acidic isoforms with pIs near 7.0 and 6.3, respectively. These forms were immunologically identical and had the same amino acid composition and mol wts. The acidic forms probably represent subspecies of CAIII in different states of oxidation. CAIII is the major soluble protein in rat liver and muscle. Its function is probably to protect proteins of these tissues from oxidation catalyzed by iron-containing degradation products of haemoglobin and myoglobin. Liver CAI and CAII and muscle CAII were identical to CAI and CAII of rat erythrocytes.

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Analysis of Recombinant Human ADP-Ribosylation Factors by Reversed-Phase High-Performance Liquid Chromatography and Electrospray Mass Spectrometry

Berger

Claude

Melançon

1998

Analytical Biochemistry

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The detection of S-glutathionation of hepatic carbonic anhydrase III in rats treated with paraquat or diquat

Cited by 7 publications

References 30 publications

Contribution of the Mitochondrial Carbonic Anhydrase (MoCA1) to Conidiogenesis and Pathogenesis in Magnaporthe oryzae

Contribution of the Mitochondrial Carbonic Anhydrase (MoCA1) to Conidiogenesis and Pathogenesis in Magnaporthe oryzae

Carbonic Anhydrase III in Liver and Muscle of Male Rats Purification and Properties

Analysis of Recombinant Human ADP-Ribosylation Factors by Reversed-Phase High-Performance Liquid Chromatography and Electrospray Mass Spectrometry

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