Methods for Determining the Rates of Catalase Synthesis and Destruction in vivo

Ve, Price; Rechcigl, Miloslav; Rw, Hartley

doi:10.1038/189062a0

Cited by 48 publications

(53 citation statements)

References 5 publications

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“…In related studies, Price et al (23,24) demonstrated that the return of catalase activity following administration of AT in vivo was accompanied by a corresponding uptake of radioactive iron into the catalase. They concluded that the return of catalase activity was due to the synthesis of new catalase, and recent studies by de Duve and coworkers (22) add support to this conclusion.…”

Section: Discussionmentioning

confidence: 99%

“…There is biochemical evidence that catalase within the hepatic cells of rats has a rapid turnover with an approximate hag-life of 11/'~ days (4,22,24), and Poole et al (22) recently suggested that this may represent the turnover of the whole microbody. At this time, there is little morphological evidence to support such a rapid turnover of hepatic microbodies as complete entities, although they occasionally appear within autophagic vacuoles.…”

Section: Inti~oductionmentioning

confidence: 99%

“…Several investigators have shown that the biochemical activity of liver catalase may be inhibited by 3-amino-1,2,4-triazole (AT), a potent herbicide and defoliant, which produces a rapid decrease in liver catalase activity after injection into rats (10,11). Later studies (8,14,19,20,(22)(23)(24) indicate that AT combines irreversibly with the catalase and apparently destroys its enzymatic activity without affecting its synthesis, this feature being exploited for in vivo studies on catalase turnover (14,(22)(23)(24). Because of its inhibitory actions on catalase, AT has been used as cytochemical control for microbody staining with the peroxidase technique; it totally abolishes the microbody reaction on addition to the reaction medium (2,6,7,13,25,26,30).…”

Section: Inti~oductionmentioning

confidence: 99%

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Peroxidase Activity in Rat Liver Microbodies After Amino-Triazole Inhibition

Wood

Legg

1970

The Journal of Cell Biology

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The in vivo effccts of 3-amino-I, 2,4-triazolc (AT) on the fine structure of microbodics in hepatic cclls of malc rats has becn studicd by thc pcroxidase-staining technique. Within l hr of intrapcritoncal injection AT abolishes microbody pcroxidasc-staining, and thc rcturn of staining coincides temporally with the known pattcrn of return of catalasc activity following AT inhibition; this is further cvidcncc that the peroxidasc staining of microbodics is due to catalasc activity. Pcroxidasc staining reappcars in the microbody matrix without cvidcncc of either massivc dcgradation or rapid prolifcration of the organclles. Furthermore, during the period of return of activity, ribosomal staining occurs adjaccnt to microbodics whose matrix shows little or no pcroxidase staining. Thesc obscrvations arc intcrprctcd as cvidcncc that (a) catalase is capable of entering preexisting microbodies without traversing the cisternae of the rough endoplasmic reticulum or the Golgi apparatus, and that (b) the ribosomal staining is probably not cytochemical diffusion artifact and may represent a localized site of synthesis or activation of catalase.

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Section: Discussionmentioning

confidence: 99%

Section: Inti~oductionmentioning

confidence: 99%

Section: Inti~oductionmentioning

confidence: 99%

See 1 more Smart Citation

Peroxidase Activity in Rat Liver Microbodies After Amino-Triazole Inhibition

Wood

Legg

1970

The Journal of Cell Biology

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“…However, there is also the possibility that the turnover of catalase is increased while synthesis remains unaffected. In the liver, the half-life of catalase is species-dependent and varies from 1.5 to 5 days (Price et al 1962;Jones and Masters 1976;Geerts et al 1984). Degradation of peroxisomes in toto via autophagocytosis was not observed, and inhibition of the enzyme can be ruled out because the antigen is equally disappearing, as detected by the decreasing ␣-catalase immunofluorescence signal.…”

Section: Discussionmentioning

confidence: 97%

Inverse Expression of Peroxisomes and Connexin-43 in the Granulosa Cells of the Quail Follicle

Farioli-Vecchioli

Raes

Espeel

et al. 2000

J Histochem Cytochem.

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SUMMARY Studying the regulation of peroxisome (Px) expression could improve our understanding of human peroxisomal disorders. The granulosa of the largest preovulatory quail follicles proved to be a relevant model because (a) Px expression changes according to the follicular maturation stage and (b) Px expression varies regionally according to the distance of the granulosa relative to the germinal disc region containing the female gamete (oocyte). The question was asked whether Px expression is related to the extent of metabolic cell coupling and whether zonal Px variation is causally related to oocytal factors. This was evaluated by the presence of catalase and Cx-43 (marker proteins for peroxisomes and gap junctions, respectively) and by in vitro experiments with granulosa explants. The data obtained show that the expression of Cx-43 and Px is inversely correlated both temporally and spatially. Uncoupling of gap junctions results in an upregulation of ␣ -catalase immunofluorescence. This is in agreement with reports that gap junctions are often negatively affected by Px proliferators. The zonal gradient in Px expression appears to be imposed by the oocyte, as is the case for steroidogenesis and proliferative capacity in the granulosa epithelium.

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“…The half-life of a peroxisomal enzyme was estimated at between 1.3 and 2.2 days by a study of the turnover rate of peroxisomal catalase (10,11). As the mechanism responsible for the excess peroxisome degradation in mammalian cells, several mechanisms have been proposed: (a) the action of peroxisomal Lon protease; (b) the membrane disrupting effect of 15-lipoxygenase (15-LOX); and, (c) autophagic degradation (Fig.…”

Section: Mechanisms For the Degradation Of Excess Peroxisomes-pslp 1mentioning

confidence: 99%

Peroxisome degradation in mammals

2011

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SummaryThis review summarizes the historical aspects of the study of peroxisome degradation in mammalian cells. Peroxisomes have diverse metabolic roles in response to environmental changes and are degraded in a preferential manner, by comparison with cytosolic proteins. This review introduces three hypotheses on the degradation mechanisms: (a) the action of the peroxisomespecific Lon protease; (b) the membrane disruption effect of 15-lipoxygenase; and (c) autophagy that sequesters and degrades the organelles by lysosomal enzymes. Among these hypotheses, autophagy is now recognized as the most important mechanism for excess peroxisome degradation. One of the most striking characteristics of peroxisomes is that they are markedly proliferated in the liver by the administration of hypolipidemic drugs and industrial plasticizers. The effects of these substances were fully reversed after withdrawal of the substances, and most of the excess peroxisomes were selectively degraded and recovered to a normal number and size. Autophagic degradation of peroxisomes has been examined using this characteristic phenomenon. Excessive peroxisome degradation that occurs after cessation of hypolipidemic drugs has been extensively investigated biochemically and morphologically. The evidence shows that the degradation of excess peroxisomes and peroxisomal enzymes is inhibited by 3-methyladenine (3-MA), a specific inhibitor of autophagy. Furthermore, in liver-specific autophagy-deficient mice, rapid removal of peroxisomes was exclusively impaired, and degradation of peroxisomal enzymes was not detected. Thus, the significant contribution of autophagic machinery to peroxisomal degradation in mammals was confirmed. However, the important question of the mechanism for the selective recognition of peroxisomes by autophagosomes remains to be fully elucidated.

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Methods for Determining the Rates of Catalase Synthesis and Destruction in vivo

Cited by 48 publications

References 5 publications

Peroxidase Activity in Rat Liver Microbodies After Amino-Triazole Inhibition

Peroxidase Activity in Rat Liver Microbodies After Amino-Triazole Inhibition

Inverse Expression of Peroxisomes and Connexin-43 in the Granulosa Cells of the Quail Follicle

Peroxisome degradation in mammals

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