The Synthesis and Turnover of Rat Liver Peroxisomes

Lazarow, Paul B.; Duve, Christian de

doi:10.1083/jcb.59.2.507

Cited by 195 publications

(67 citation statements)

References 40 publications

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“…For instance, in the mutant, peroxisomes might be more readily disrupted by homogenization. The mutation might alter the peroxisomal membrane either to make it more leaky or to prevent the import of enzymes (33). More speculatively, there could be metabolic links through which the xanthine oxidase enzyme might affect catalase.…”

Section: Discussionmentioning

confidence: 99%

Peroxisomes in wild-type and rosy mutant Drosophila melanogaster.

Beard

Holtzman

1987

Proc. Natl. Acad. Sci. U.S.A.

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This study shows that peroxisomes are abundant in the Malpighian tubule and gut of wild-type Oregon R Drosophila melanogaster and that the peroxisomal population of the rosy-506 eye-color mutant differs from that of the wild type. Catalase activity in wild-type flies is demonstrable in bodies of appearance and centrifugal behavior comparable to the perixosomes of vertebrate tissues. Xanthine oxidase (xanthine:oxygen oxidoreductase, EC 1. Deficits in one or more of the peroxisomal enzymes and possible defects in peroxisomal structure are correlated with certain human inherited metabolic diseases (1-4). These diseases are still poorly understood, in part because different tissues show different effects of the mutation and in part because alterations in single genes can seemingly have multiple effects on the peroxisomes. Studies of the disorders are made difficult by their rareness and by the obvious limits of working with human material. It would be helpful to study analogues of the disorders in animals amenable to detailed analysis, but thus far such analogues have not been available. We chose to initiate our explorations for peroxisomal mutants in Drosophila by comparing wild-type Oregon R strain flies with the rosy-506 eye-color mutant, in which 90% of the structural gene for xanthine dehydrogenase (xanthine: NAD+ oxidoreductase, EC 1.1.1.204) is deleted (5, 6). This protein is a bifunctional oxidoreductase that can act as a dehydrogenase or as an oxidase (xanthine:oxygen oxidoreductase, EC 1.1.3.22) depending upon substrate and acceptor availability (7,8). The oxidase activity of the enzyme is critical to the degradation of purines in many organisms; the dehydrogenase function is central to the formation of pterinebased eye-color pigments in Drosophila. We suspected that this protein might be peroxisomal because (i) when acting as an oxidase, it produces hydrogen peroxide, a common feature of peroxisomal oxidases; (ii) it requires flavin in generating peroxide, as is found for many other peroxisomal oxidases; and (iii) its role in punine degradation is potentially functionally linked to activity of allantoicase and uricase, known peroxisomal enzymes (9). The subcellular localization of xanthine oxidase is not clearly established. Some cell fractionation studies show most of the enzyme to be soluble (9, 10), while other investigations report some xanthine oxidase cosedimenting with peroxisomal enzymes (11, 12).The study reported here identifies peroxisomes in the Malpighian tubule and gut of adult Drosophila wild-type Oregon R and rosy-506 strains, by virtue of their content of catalase, the peroxisomal "marker" enzyme. To localize xanthine oxidase, we have adapted cytochemical methods used to demonstrate other oxidases. With these methods, we have shown the presence of xanthine oxidase in peroxisomes of wild-type flies and the absence of this enzyme in rosy-506 flies. We also find signs that, as in the human mutations, a relatively simple genetic change can have complex effects on the peroxisomes. Prel...

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Section: Discussionmentioning

confidence: 99%

Peroxisomes in wild-type and rosy mutant Drosophila melanogaster.

Beard

Holtzman

1987

Proc. Natl. Acad. Sci. U.S.A.

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“…A problem yet to be solved is the process of assemblage of alcohol oxidase and its transport into the peroxisomes where it becomes active. It is possible that inactive subunits and/or apoenzyme are intermediates in the biosynthesis of active alcohol oxidase, a process which may be similar to that of the biosynthesis of peroxisomal catalase as outlined by Lazarow and De Duve (1973). Activation or inactivation of alcohol oxidase may then be accomplished by association or dissociation of FAD which is bound non-covalently to each of the eight subunits of the enzyme (Sahm and Wagner, 1973;Kato et al, 1976).…”

Section: Discussionmentioning

confidence: 99%

Development of crystalline peroxisomes in methanol-grown cells of the yeast Hansenula polymorpha and its relation to environmental conditions

et al. 1978

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“…[1]) . For example, catalase, the principal matrix protein of the peroxisome, does not pass through the ER on its way to the peroxisomes (30)(31)(32)(33) .…”

Section: Peroxisome Biogenesismentioning

confidence: 99%

Polypeptide and phospholipid composition of the membrane of rat liver peroxisomes: comparison with endoplasmic reticulum and mitochondrial membranes.

Fujiki¹,

Fowler²,

Shio³

et al. 1982

The Journal of Cell Biology

364

158

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Membranes were isolated from highly purified peroxisomes, mitochondria, and rough and smooth microsomes of rat liver by the one-step Na2CO3 procedure described in the accompanying paper (1982, J. Cell Biol . 93 :97-102) . The polypeptide compositions of these membranes were determined by SDS PAGE and found to be greatly dissimilar . The peroxisomal membrane contains 12% of the peroxisomal protein and consists of three major polypeptides (21,700, 67,700 and 69,700 daltons) as well as some minor polypeptides . The major peroxisomal membrane proteins as well as most of the minor ones are absent from the endoplasmic reticulum (ER) . Conversely, most ER proteins are absent from peroxisomes.By electron microscopy, purified peroxisomal membranes are -6 .8 nm thick and have a typical trilaminar appearance . The phospholipid/protein ratio of peroxisomal membranes is -200 nmol/mg; the principal phospholipids are phosphatidyl choline and phosphatidyl ethanolamine, as in ER and mitochondrial membranes. In contrast to the mitochondria, peroxisomal membranes contain no cardiolipin . All the membranes investigated contain a polypeptide band with a molecular mass of 15,000 daltons. Whether this represents an exceptional common membrane protein or a coincidence is unknown. The implications of these results for the biogenesis of peroxisomes are discussed.Knowledge of the peroxisomal membrane's properties is essential to an understanding both of the organelle's functions and of its biogenesis . The membrane separates the peroxisomal contents from the cytosol and defines the peroxisomal interior as a distinct intracellular space. The permeability properties of the membrane determine to what extent the peroxisome functions as a separate biochemical compartment. Knowledge of how the membrane is formed is essential to an understanding of the biogenesis of the organelle as a whole. If the membrane is derived from some other intracellular membrane, for example the endoplasmic reticulum (ER) (as is widely assumed), then one might expect to see some similarity in composition between them . If, on the other hand, the peroxisomes exist as a separate intracellular compartment, as has recently been suggested (1), then the peroxisomal membrane needs to have no structural similarity to the ER . THE JOURNAL OF CELL BIOLOGY " VOLUME 93 APRIL 1982 103-110 ©The Rockefeller University Press -0021-9525/82/04/0103/08 $1 .00We have applied the newly-developed sodium carbonate procedure described in the accompanying paper (2) to isolate peroxisomal, mitochondrial, and ER membranes.' We have partially characterized these three membranes, and found that their polypeptide compositions are almost entirely different, but their phospholipid compositions are similar. Some of these results have appeared in abstract form (3, 4) .' Rat liver microsomes were subfractionated by isopycnic centrifugation in linear sucrose gradients according to Beaufay et al. (7). The fractions selected as the "rough microsomal fraction" have been shown by these authors to c...

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The Synthesis and Turnover of Rat Liver Peroxisomes

Cited by 195 publications

References 40 publications

Peroxisomes in wild-type and rosy mutant Drosophila melanogaster.

Peroxisomes in wild-type and rosy mutant Drosophila melanogaster.

Development of crystalline peroxisomes in methanol-grown cells of the yeast Hansenula polymorpha and its relation to environmental conditions

Polypeptide and phospholipid composition of the membrane of rat liver peroxisomes: comparison with endoplasmic reticulum and mitochondrial membranes.

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