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At least 19 recordsLinked to original sources
PubMed1969

Microbodies in experimentally altered cells. II. The relationship of microbody proliferation to endocrine glands.

The liver cells of intact male rats given ethyl-alpha-p-chlorophenoxyisobutyrate (CPIB) characteristically show a marked increase in microbodies and in catalase activity, while those of intact female rats do not. In castrated males given estradiol benzoate and CPIB the increase in catalase activity and microbody proliferation is abolished, while in castrated females given testosterone propionate and CPIB the livers show a marked increase in microbodies and in catalase activity. No sex difference in microbody and catalase response is apparent in fetal and neonatal rats. Both sexes show a sharp rise in catalase activity on the day of birth, with a rapid decline at 5 days after birth. Thyroidectomy abolishes the hypolipidemic effect of CPIB in rats, but microbody proliferation and increase in catalase activity persists in thyroidectomized male rats, indicating that microbody proliferation can be independent of hypolipidemia. Adrenalectomy does not alter appreciably the microbody-catalase response to CPIB. These experiments demonstrate that (1) in adult rats, hepatic microbody proliferation is dependent to a significant degree upon male sex hormone but is largely independent of thyroid or adrenal gland hormones; (2) hepatic microbody proliferation is independent of the hypolipidemic effect of CPIB; (3) displacement of thyroxine from serum protein may not be sufficient cause for stimulation of microbody formation.

Adrenalectomy↗
PubMed1985

Topogenesis of microbody enzymes: a sequence comparison of the genes for the glycosomal (microbody) and cytosolic phosphoglycerate kinases of Trypanosoma brucei.

To determine how microbody enzymes enter microbodies, we are studying the genes for cytosolic and glycosomal (microbody) isoenzymes in Trypanosoma brucei. We have found three genes (A, B and C) coding for phosphoglycerate kinase (PGK) in a tandem array in T. brucei. Gene B codes for the cytosolic and gene C for the glycosomal isoenzyme. Genes B and C are 95% homologous, and the predicted protein sequences share approximately 45% amino acid homology with other eukaryote PGKs. The microbody isoenzyme differs from the cytosolic form and other PGKs in two respects: a high positive charge and a carboxy-terminal extension of 20 amino acids. Our results show that few alterations are required to redirect a protein from cytosol to microbody. From a comparison of our results with the unpublished data for three other glycosomal glycolytic enzymes we infer that the high positive charge represents the major topogenic signal for uptake of proteins into glycosomes.

Amino Acid Sequence↗
PubMed1977

Microbody of n-alkane-grown yeast. Enzyme localization in the isolated microbody.

Microbodies appearing abundantly in n-alkane-grown cells of Candida tropicalis pK 233 were isolated by means of sucrose density gradient centrifugation. Electron microscopical observation showed that the microbodies isolated were intact. Localization of catalase and D-amino acid oxidase in the isolated microbodies was confirmed. Isocitrate lyase, melate synthase and NADP-linked isocitrate dehydrogenase were also located in the microbody, but malate dehydrogenase, citrate synthase, aconitase and NAD-linked isocitrate dehydrogenase were not. Neither cytochrome P-450 not NADPH-cytochrome c reductase, the components involved in the n-alkane hydroxylation system of the yeast, were detected in the microbody fraction.

Alkanes↗
PubMed1975

Microbody of methanol-grown yeasts. Localization of catalase and flavin-dependent alcohol oxidase in the isolated microbody.

Profuse appearance of microbodies was observed in the cells of methanol-utilizing yeasts in connection with the enhanced catalase activity. These microbodies were isolated successfully by means of sucrose gradient centrifugation from the methanol-grown cells of Kloeckera sp. no. 2201. Localization of a flavin-dependent alcohol oxidase as well as characteristic microbody enzymes (catalase and D-amino acid oxidase) were ascertained in the isolated microbodies, whereas formaldehyde and formate dehydrogenases were detected in the cytoplasmic region. Localization of catalase in the isolated microbody was also demonstrated by the cytochemical technique with 3,3'-diaminobenzidine.

Alcohol Oxidoreductases↗
PubMed1972

Microbodies in experimentally altered cells. IX. The fate of microbodies.

Male rats were given 0.25% CPIB (ethyl chlorophenoxyisobutyrate) for 4 weeks at which time their liver cells showed the typical increase in number of microbodies (peroxisomes). During the first week after withdrawal of CPIB and simultaneous injection of allylisopropylacetamide (AIA), an inhibitor of catalase synthesis, the microbody matrix, in peroxidase preparations, showed marked decrease in electron opacity. In liver cells of rats from which CPIB was withdrawn but which were not given AIA, there were interruption in the limiting membrane and almost total loss of microbody matrix within 3 days. Simultaneous with the loss of matrix content, the hepatic catalase activity decreased from an average 80 units/mg protein to less than 10 units/mg protein. In liver cells of Mastomys natalensis, a multimammate rodent, withdrawal of CPIB was associated with the frequent occurrence of bare microbody nucleoids situated free in the hyaloplasm. The ultrastructural observations and the associated decrease in catalase activity suggest that one means of disposal of microbodies is by rather rapid dissolution or leakage of their matrix enzymes into the surrounding hyaloplasm.

Acetamides↗
PubMed1971

Microbodies (Glyoxysomes and Peroxisomes) in Cucumber Cotyledons: Correlative Biochemical and Ultrastructural Study in Light- and Dark-grown Seedlings.

The changes in activities of glyoxysomal and peroxisomal enzymes have been correlated with the fine structure of microbodies in cotyledons of the cucumber (Cucumis sativus L.) during the transition from fat degradation to photosynthesis in light-grown plants, and in plants grown in the dark and then exposed to light. During early periods of development in the light (days 2 through 4), the microbodies (glyoxysomes) are interspersed among lipid bodies and contain relatively high activities of glyoxylate cycle enzymes involved in lipid degradation. Thereafter, these activities decrease rapidly as the cotyledons expand and become photosynthetic, and the activity of glycolate oxidase rises to a peak (day 7); concomitantly the microbodies (peroxisomes) become preferentially associated with chloroplasts.In seedlings grown in the dark for 10 days, the reserve lipid and the glyoxylate cycle enzyme activities persist for a longer time than in the light; correlated with this, there is a continued association of the microbodies with the lipid bodies. When these dark-grown seedlings are then exposed to 51 hours of the light-dark cycle, peroxisomal marker enzymes increase rapidly in activity, and the microbodies become appressed to chloroplasts. We conclude that the characteristic association observed between glyoxysomes and lipid bodies reflects their mutual involvement in net gluconeogenesis through the conversion of fatty acids to carbohydrate, while the close spatial relationship observed between peroxisomes and chloroplasts at later stages of development reflects their mutual involvement in glycolate metabolism.Although glyoxysomal enzyme activities are dropping rapidly while peroxisomal enzyme activities are increasing rapidly during the transition period in the light, the electron microscopic evidence does not indicate that glyoxysomes are being degraded or peroxisomes are being formed. Since in the dark-grown seedlings the activities of peroxisomal enzymes remain low and do not increase as they do in the light, an opportunity is afforded to compare quantitatively any changes in numbers of microbodies per cell with the changes in activities of glyoxysomal enzymes. It is found that the magnitude of the decrease in numbers of microbodies is considerably less than that of the decrease in glyoxysomal enzyme activities between days 4 and 10. When the cotyledons are exposed to light, peroxisomal enzyme activities increase greatly, but again there is no ultrastructural evidence for the synthesis of a new population of microbodies to accommodate this increase. These results allow us to conclude that the developmental transition from glyoxysomal to peroxisomal function almost certainly does not involve the actual replacement of one population of microbodies by another. Rather, the transition probably occurs within existing particles, either by a sequential functioning of two different kinds of microbodies or by a change in enzyme complement within a single population. Our findings with both light- and dark-grown cotyledons favor the latter possibility. The cytoplasmic invaginations into microbodies seen during greening of both light-grown cotyledons and etiolated cotyledons exposed to light may be morphological manifestations of the mechanism by which the microbodies lose or gain enzymes.

Journal Article↗
PubMed1973

Further evidence to suggest that microbodies do not exist as individual entities.

Male wild-type mice (Cs(a) strain) were treated with ethyl-alpha-p-chlorophenoxyisobutyrate (CPIB), a hypolipidemic drug which enhances hepatic catalase synthesis and induces rapid and significant increase in the number of microbody (peroxisome) profiles in liver cells. Numerous microbody profiles, several of them appearing in clusters and retaining membranous continuities, were observed in liver cells of CPIB-treated mice. They showed a significant variation in size and configuration, and the presence or absence of the nucleoid or core did not appear to bear any relation to the size or shape of microbody profiles. Nucleoids were encountered frequently in microbody profiles measuring as small as 0.1 mu in diameter. Numerous continuities between two or more anucleoid and/or nucleoid-containing microbody profiles of different sizes and shapes were seen. These findings are inconsistent with the concept that the smaller peroxisomes are the possible precursors or progenitors of their larger counterparts. Detailed examination of numerous electron micrographs revealed irregular dilatations and tortuosities of the endoplasmic reticulum (ER) containing electron-opaque peroxisomal material displaying the characteristic appearance of matrix and usually containing irregular cores. Transitions of rough ER to smooth ER in which microbody proteins accumulated were also apparent. Numerous continuities between several microbody profiles and continuities between microbody profiles and ER are interpreted as accumulations of peroxisomal proteins in dilated tortuous channels of ER. These observations strongly suggest that the microbody proteins constitute a common pool, circulating constantly in the dilated ER channels. The size, shape and number of microbody profiles appear to reflect the amount of peroxisomal proteins present in the pool. These observations clearly suggest that the microbodies do not exist as individual entities.

Animal Feed↗
PubMed1967

Microbodies in experimentally altered cells.

A rapid and sustained increase in the number of microbodies in liver and kidney cells can be induced in male rats by ethyl chlorophenoxyisobutyrate (CPIB), a hypolipidemic drug. This phenomenon permits investigation of several aspects of microbody behavior in experimental conditions. Reversal experiments demonstrate that liver cells revert to normal between 2 and 3 weeks after withdrawal of CPIB and that one of the mechanisms for removal of excess microbodies is their incorporation into structures indistinguishable from lysosomes. In a state of rapid cell division, such as that present during liver regeneration, microbody proliferation apparently occupies a high biological priority. In necrotic or degenerating cells microbody structure remains relatively normal. The increase in microbodies induced by CPIB is inhibited by chloramphenicol. No increase in microbodies occurred in female rats or in chickens, guinea pigs, or rabbits at the dosage used (0.25% in diet). No changes in microbodies were seen in monkey liver. Catalase activity was generally parallel to the numerical response in microbodies. Additional observations suggest that the microbody response to CPIB is not related to hepatomegaly induced by this agent but may be related to the hypolipidemic effect of CPIB, though hypolipidemia per se is not a specific or sufficient cause of microbody proliferation.

Animals↗
PubMed1969

Cytochemical localization of peroxidatic activity of catalase in rat hepatic microbodies (peroxisomes).

Prominent staining of rat hepatic microbodies was obtained by incubating sections of aldehyde-fixed rat liver in a modified Graham and Karnovsky's medium for ultrastructural demonstration of peroxidase activity. The electron-opaque reaction product was deposited uniformly over the matrix of the microbodies. The microbodies were identified by their size, shape, presence of tubular nucleoids, and other morphologic characteristics, and by their relative numerical counts. The staining reaction was inhibited by the catalase inhibitor, aminotriazole, and by KCN, azide, high concentrations of H(2)O(2), and by boiling of sections. These inhibition studies suggest that the peroxidatic activity of microbody catalase is responsible for the staining reaction. In the absence of exogenous H(2)O(2) appreciable staining of microbodies was noted only after prolonged incubation. Addition of sodium pyruvate, which inhibits endogenous generation of H(2)O(2) by tissue oxidases, or of crystalline catalase, which decomposes such tissue-generated H(2)O(2), completely abolished microbody staining in the absence of H(2)O(2). Neither diaminobenzidine nor the product of its oxidation had any affinity to bind nonenzymatically to microbody catalase and thus stain these organelles. The staining of microbodies was optimal at alkaline pH of 8.5. The biological significance of this alkaline pH in relation to the similar pH optima of several microbody oxidases is discussed. In addition to staining of microbodies, a heat-resistant peroxidase activity is seen in some of the peribiliary dense bodies. The relation of this reaction to the peroxidase activity of lipofuscin pigment granules is discussed.

Animals↗
PubMed1974

Nafenopin-induced hepatic microbody (peroxisome) proliferation and catalase synthesis in rats and mice. Absence of sex difference in response.

Nafenopin (2-methyl-2[p-(1,2,3,4-tetrahydro-1-naphthyl)phenoxy]-propionic acid; Su-13437), a potent hypolipidemic compound, was administered in varying concentrations in ground Purina Chow to male and female rats, wild type (Cs(a) strain) mice and acatalasemic (Cs(b) strain) mice to determine the hepatic microbody proliferative and catalase-inducing effects. In all groups of animals, administration of nafenopin at dietary levels of 0.125% and 0.25% produced a significant and sustained increase in the number of peroxisomes. The hepatic microbody proliferation in both male and female rats and wild type Cs(a) strain mice treated with nafenopin was of the same magnitude and was associated with a two-fold increase in catalase activity and in the concentration of catalase protein. The increase in microbody population in acatalasemic mice, although not accompanied by increase in catalase activity, was associated with a twofold increase in the amount of catalase protein. The absence of sex difference in microbody proliferative response in nafenopin-treated rats and wild type mice is of particular significance, since ethyl-alpha-p-chlorophenoxyisobutyrate (CPIB)-induced microbody proliferation and increase in catalase activity occurred only in males. Nafenopin can, therefore, be used as an inducer of microbody proliferation and of catalase synthesis in both sexes of rats and mice. The serum glycerol-glycerides were markedly lowered in all the animals given nafenopin, which paralleled the increase in liver catalase. All the above effects of nafenopin were fully reversed when the drug was withdrawn from the diet of male rats. During reversal, several microbody nucleoids were seen free in the hyaloplasm or in the dilated endoplasmic reticulum channels resulting from a rapid reduction in microbody matrix proteins after the withdrawal of nafenopin from the diet. Because of microbody proliferation and catalase induction with increasing number of hypolipidemic compounds, additional studies are necessary to determine the interrelationships of microbody proliferation, catalase induction, and hypolipidemia.

Animals↗
PubMed1975

Microbodies of the rat renal proximal tubule: ultrastructural and cytochemical investigations.

The present study was undertaken to provide a detailed morphological and cytochemical characterization of the microbodies of the rat renal proximal tubule following perfusion fixation. The following observations were made: 1) Two basic types of microbodies (Mb-I and Mb-II) can be identified. Mb-I have both circular and tubular profiles which are located peripherally within the granular matrix of these microbodies. Mb-II have marginal plates and crystalloid inclusion in addition to circular and tubular profiles. 2) Circular and tubular profiles, 100 nm in diameter, described by previous investigators as being infrequent in occurrence, are the most consistent morphological characteristic of rat renal microbodies after perfusion fixation. These profiles have a homogeneous center surrounded by a double or single ring of granules. The uniform size and spacing of these granules within profiles establish a basic 100 A periodicity found in both types of microbodies. 3) Evidence is presented which suggests that both "nucleoids" and "tubular protrusion rods" as described by other investigators of the rat renal microbodies may result from poor fixation and/or osmotic stress. 4) The density of the matrix of Mb-I is, in contrast to previous reports, greater than the density of adjacent mitochondria. 5) Marginal plates or crystalloid inclusions were demonstrated in some microbodies (Mb-II) of all the rats studied; periodicities of 100, 200, and 300 A were identified within these structures. 6) Both types of microbodies were positive for catalase activity, but were negative for acid phosphatase activity. On the basis of both morphological and cytochemical criteria, it seems plausible that these two populations of renal microbodies (Mb-I and Mb-II) represent a morphological and functional continuum.

Acid Phosphatase↗
PubMed1971

Development of Microbodies in Sunflower Cotyledons and Castor Bean Endosperm during Germination.

In cotyledons of sunflower seedlings glyoxysomal and peroxisomal enzymes exhibit different rates of development during germination. The total activity of isocitrate lyase, a glyoxysomal marker enzyme, rapidly increased during the first 3 days, and then decreased 89% by day 9. Exposure to light accelerated this decrease only slightly. The specific activity of glyoxysomal enzymes (malate synthetase, isocitrate lyase, citrate synthetase, and aconitase) in the microbody fraction from sucrose density gradients increased between days 2 and 4 about 2- to 3-fold, and thereafter it remained about constant in light or darkness.Total activity of the peroxisomal enzymes increased slowly in the dark during the first 4 days of germination and thereafter remained at a constant level of activity in the dark or increased 2-fold in 24 hours of light. The specific activties of glycolate oxidase, hydroxypyruvate reductase, and serine-glyoxylate aminotransferase in the isolated microbody fraction increased about 10-fold between days 2 and 4 in the dark and then remained constant or increased again 10-fold after an additional 48 hours in the light.The total activity of the common microbody marker, catalase, developed similarly to isocitrate lyase, but decreased only 72% by day 9. The specific activities of enzymes (catalase, malate dehydrogenase, and aspartate aminotransferase) common to both microbody systems were 10- to 1000-fold greater than those of other enzymes. It is proposed that malate and aspartate may be involved in hydrogen transport between microbodies and other cellular sites.Glutamate-glyoxylate aminotransferase was very active in microbodies from castor bean endosperm and sunflower cotyledons. The specific activity of this aminotransferase developed similarly to glyoxysomal enzymes in the dark but further increased in the light, as did peroxisomal enzymes.The microbody fraction of castor bean endosperm germinated in the dark for 5 days contained both glyoxysomal and peroxisomal enzymes of similar specific activity.Adjacent to the microbody fraction on sucrose gradients from sunflower cotyledons were etioplasts at slightly lower densities and protein bodies at similar and higher densities. Their presence in the microbody fractions resulted in artificially low specific activities.

Journal Article↗
PubMed1975

The development of microbodies (glyoxysomes and leaf peroxisomes) in cotyledons of germinating watermelon seedlings.

The ontogeny of glyoxysomes and leaf peroxisomes has been examined in the cotyledons of germinating watermelon (Citrullus vulgaris) seedlings. Organelles from the cotyledons were extracted by razor blade homogenization and microbodies were separated by sucrose density gradient fractionation. Both kinds of microbodies have the same mean equilibrium density on sucrose gradients.The development of leaf peroxisomes was examined in seedlings transferred to light at 4 days and 10 to 12 days. In seedlings maintained in darkness to the age of 10 to 12 days, glyoxysomal enzymes virtually disappeared, and the losses were paralleled by a corresponding loss in microbody protein. During this period peroxisomal activity was low and changed only slightly. On transfer to light at this stage, the activity of peroxisomal enzymes rose strikingly. The residual glyoxysomal activity disappeared completely, and the developmental pattern of microbody catalase and microbody protein paralleled the light-induced glyoxysomal disappearance.Similar patterns of microbody development were observed when 4-day-old dark-grown seedlings with maximum glyoxysomal activities were exposed to light. The activity of the peroxisomal enzymes increased and the glyoxysomal enzymes disappeared at a faster rate than in darkness. These changes were again paralleled by the accelerated demise of microbody catalase and microbody protein. Thus under both conditions glyoxysomes were selectively destroyed during peroxisomal development, and the amount of peroxisomes produced was insufficient to offset the loss of glyoxysomal protein. The results do not support the contention that glyoxysomes are transformed to leaf peroxisomes in developing cucurbit cotyledons and favor the view that the two kinds of microbody arise independently of each other.

Journal Article↗
PubMed1975

Development of microbodies in candida tropicalis during incubation in a n-alkane medium.

Development of microbodies in Candida tropicalis pK 233 was studied mainly by electron microscopical observation. The yeast cells, precultured on malt extract, scarcely contained microbodies and showed very low catalase activity. When the precultured cells were transferred to a n-alkane medium and incubated with shaking, the number of microbodies increased and concomitantly the activity of catalase was enhanced. That is, both the area ratio of microbodies in the cell and the ratio of microbodies to cytoplasm in area increased significantly during the utilization of n-alkanes for 8 hrs. Localization of catalase in the microbodies was demonstrated cytochemically by use of 3,3'-diaminobenzidine, but other organella in the cell, except for vacuoles appearing in the early growth phase and mitochondria, were not stained with this reagent. Microbodies seemed to grow by division. Biogenesis of microbodies in the yeast cells is also discussed.

3,3'-Diaminobenzidine↗
PubMed1986

How proteins get into microbodies (peroxisomes, glyoxysomes, glycosomes).

All microbody proteins studies, including one microbody membrane protein, are made on free polysomes and imported post-translationally. This holds for animal tissues, plants, and fungi. The majority of microbody protein sub-units are synthesized in a form not detectably different from mature sub-units. In five cases a larger precursor protein has been found. The position of the extra piece in this precursor is not known. In two of the five cases, processing of the precursor is not coupled to import; in the other three this remains to be determined. It is not even known whether information in the prepiece contributes to topogenesis, or serves other purposes. Microbody preparations from Neurospora, plant tissue and rat liver can take up some newly synthesized microbody proteins in vitro. In most cases uptake is inefficient. No special requirements for uptake have been established and whether a receptor is involved is not yet known. Several examples have been reported of peroxisomal enzymes with a counterpart in another cell compartment. With the exception of catalase, no direct evidence is available in any of these cases for two isoenzymes specified by the same gene. In the Zellweger syndrome, a lethal hereditary disease of man, characterized by a lack of peroxisomes, the levels of several enzymes of lipid metabolism are strongly decreased. In contrast, D-amino-acid oxidase, L-alpha-hydroxyacid oxidase and catalase levels are normal. The catalase resides in the cytosol. Since there is no separate gene for cytosolic catalase, the normal catalase levels in Zellweger cells show that some peroxisomal enzymes can mature and survive stably in the cytosol. It is possible that maturation of the peroxisomal enzyme in the cytoplasm can account for the finding of cytosolic catalase in some normal mammalian cells. The glycosomes of trypanosomes are microbodies that contain a glycolytic system. Comparison of the glycosomal phosphoglycerate kinase with its cytosolic counterpart has shown that these isoenzymes are 93% homologous in amino-acid sequence, but less than 50% homologous to the corresponding enzymes of yeast and mammals. This implies that few alterations are required to direct a protein into microbodies. This interpretation is supported by the evidence for homology between some microbody and mitochondrial isoenzymes in other organisms mentioned under point 4. The major changes of the glycosomal phosphoglycerate kinase relative to the cytosolic enzyme are a large increase in positive charge and a C-terminal extension of 20 amino acids.(ABSTRACT TRUNCATED AT 400 WORDS)

Acetyl-CoA C-Acyltransferase↗