On the relative rates of synthesis and degradation of catalase in vertebrate tissues

Crane, Denis I.; Holmes, Roger S.; Masters, C.J.

doi:10.1016/0020-711x(78)90119-2

Cited by 10 publications

(3 citation statements)

References 17 publications

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“…It has been reported that mammalian and avian kidney and liver generally have higher catalase turnover rates due to elevated kd values relative to those of other tissues in these organisms [ 111, and Drosophila catalase turnover parameters are generally consistent with these observations. In addition, the kd values for Drosophila catalase fall within the range of values that have been reported for the catalases from these same organisms [1,11], which tends to verify the accuracy and reliability of using aminotriazole perturbation for the determination of catalase turnover parameters in Drosophila.…”

Section: Sdsupporting

confidence: 71%

Developmental and tissue‐specific control of catalase expression in Drosophila melanogaster: Correlations with rates of enzyme synthesis and degradation

1983

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The ontogenetic and tissue-specific expression of catalase (E.C. 1.11.1.6) has been determined in a wild type strain of Drosophila rnelunogusrer derived from a natural population. Two distinct peaks of activity are observed during development with the first peak occurring in late third instar larvae just prior to puparium formation, and the second and larger of the two peaks occurring during metamorphosis. These peaks of catalase activity are coincident with the two major peaks of ecdysone titer. Of the tissues assayed, larval malpighian tubules, gut, and fat body demonstrated the highest specific activities. Adult abdomen exhibited a two-to three-fold higher specific activity than either head or thorax. Of the abdominal tissues assayed, malpighian tubules and abdominal wall had the highest specific activities. Malpighian tubules were the only sexually dimorphic tissue with respect to catalase activity and are apparently largely responsible for an overall increase observed in female abdominal activity. Catalase-specific CRM levels parallel the enzyme activity levels indicating that these tissue-specific activity differences reflect differences in the rate of accumulation of catalase molecules.Turnover studies employing the catalase inhibitor 3-amino-1,2,4-triazole were conducted on head, thorax, and abdomen of male adult flies. Rates of catalase degradation were similar in the three body segments with a slightly higher rate in abdominal tissue. Therefore the different steady statc levels observed largely reflect different rates of catalase synthesis.

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Section: Sdsupporting

confidence: 71%

Developmental and tissue‐specific control of catalase expression in Drosophila melanogaster: Correlations with rates of enzyme synthesis and degradation

1983

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“…Although catalase has been one of the most intensively investigated enzymes, the extent and nature of its multiplicity remains to be resolved. Catalase extracted from tissues and organs of many mammalian species exists as a single electrophoretic form; whereas, multiple electrophoretic forms ofthe enzyme have been reported in crude extracts of mouse, rat, and rabbit liver (12), human erythrocytes (22), and mouse brain, heart, and spleen (2).…”

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confidence: 99%

Heterogeneity of Catalase in Maturing and Germinated Cotton Seeds

Kunce¹,

Trelease²

1986

Plant Physiol.

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To investigate possible charge and size heterogeneity of catalase (EC 1.11.1.6) in cotton (Gossypium hirsutum L. cv Deltapine 62), extracts of cotyledons from different developmental ages were subjected to nondenaturing polyacrylamide gel electrophoresis and isoelectric focusing. Special precautions (e.g. fresh homogenates, reducing media) were necessary to prevent artefacts due to enzyme modification during extraction and storage. When the gels were stained for enzyme activity, two distinct electrophoretic forms of catalase were resolved in extracts of maturing and mature cotton seeds. In germinated seeds, three additional cathodic forms were detected revealing a total of five electrophoretic variants. In green cotyledons, the two anodic forms characteristic of ungerminated seeds were less active; whereas, the most cathodic form was predominant.

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“…The nascent catalase polypeptide is synthesized on free polysomes as an apomonomer and then rapidly targeted into peroxisomes. The apomonomer is believed to first gain heme followed by tetramerization to form the functional catalase enzyme (Lazarow and de Duve, 1973;Goldman and Blobel, 1978 ;Lazarow and Fujiki, 1985) ; however, the detailed mechanism of posttranslational assembly of the catalase and incorporation of the heme into catalase remains to be elucidated because active catalase tetramer has different intracellular distribution in different species (Crane et al ., 1978 ;Geerts et al, 1984 ;Yamamoto et al ., 1988) . In rat the majority of the catalase is localized in peroxisomes, whereas in sheep and guinea pig liver almost all of the catalase is in the cytoplasm .…”

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confidence: 99%

Abnormality in Translational Regulation of Catalase Expression in Disorders of Peroxisomal Biogenesis

Singh

Kremser

Ghosh

et al. 1996

Journal of Neurochemistry

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Peroxisomal disorders are a newly described group of inherited neurological diseases. In disorders of peroxisomal biogenesis, e.g., Zellweger syndrome, owing to the lack of peroxisomes, catalase, a peroxisomal enzyme, is found to be present in the cytoplasm instead. We observed higher catalase activity (7.59 ± 0.41 mU/mg of protein) in cultured skin fibroblasts from Zellweger patients than in control fibroblasts (4.45 ± 0.29 mU/mg of protein). Moreover, we also found that the majority of the catalase in Zellweger cells was present in the inactive form. The specific activities following reactivation in Zellweger and control cells were 12.1 and 4.9 mU/mg of protein, respectively. To understand the molecular basis of higher levels of catalase in Zellweger than control cells, we examined the rate of synthesis and turnover of catalase and levels of catalase mRNA and protein levels in Zellweger cells as compared with control cells. The initial rates of synthesis of catalase in Zellweger (1.68 ± 0.15 mU/mg of protein) and control (1.51 ± 0.14 mU/mg of protein) cells were similar. The rates of turnover of catalase in Zellweger (t1/2 = 47 ± 8 h) and control (t1/2 = 49 ± 7 h) were also similar. Consistent with the enzyme activity, the levels of catalase protein were higher in Zellweger cells as compared with control cells. On the other hand, there was no difference in the level of catalase mRNA between control and Zellweger cells. Although the rate of synthesis in Zellweger and control cells were initially similar, it was down‐regulated to a lower level at ∼72 h of culture in control fibroblasts as compared with Zellweger cells, which continued to synthesize catalase at the same rate up to 5 days in culture. The presence of similar levels of mRNA in control and Zellweger cells and continued synthesis of catalase in Zellweger cells at a higher level as compared with control cells suggest a loss of regulation at the translational level.

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On the relative rates of synthesis and degradation of catalase in vertebrate tissues

Cited by 10 publications

References 17 publications

Developmental and tissue‐specific control of catalase expression in Drosophila melanogaster: Correlations with rates of enzyme synthesis and degradation

Developmental and tissue‐specific control of catalase expression in Drosophila melanogaster: Correlations with rates of enzyme synthesis and degradation

Heterogeneity of Catalase in Maturing and Germinated Cotton Seeds

Abnormality in Translational Regulation of Catalase Expression in Disorders of Peroxisomal Biogenesis

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