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Drug Metabolism Reviews 1987
Review
Topics: Animals; Humans; Kidney; Microbodies; Microsomes; Microsomes, Liver; Mitochondria; Mitochondria, Liver
PubMed: 3286171
DOI: 10.3109/03602538708994130 -
Histochemistry and Cell Biology Sep 1997In situ hybridization, cytochemical and immunocytochemical techniques have contributed significantly to the understanding of the biology of peroxisomes, since they... (Review)
Review
Application of in situ hybridization, cytochemical and immunocytochemical techniques for the investigation of peroxisomes. A review including novel data. Robert Feulgen Prize Lecture 1997.
In situ hybridization, cytochemical and immunocytochemical techniques have contributed significantly to the understanding of the biology of peroxisomes, since they permit in situ demonstration of the sites of synthesis and distribution of peroxisomal proteins without the necessity of homogenization and subcellular fractionation of tissues or cultured cells. This article reviews the results of research on mammalian peroxisomal metabolism, biogenesis and proliferation in which morphological techniques have played a significant role in the elucidation of the biological problem. Some new data on peroxisomal heterogeneity and morphogenesis are included. The morphological methods applied have made it possible to characterize the differences in distribution of mRNAs encoding peroxisomal proteins in different tissues, as well as to monitor the marked heterogeneity in the protein composition and in the activity of specific enzymes in the peroxisomal population of single cells, or in tissues with complex organization (e.g. liver and kidney). In addition, the dynamic alterations and high plasticity of the peroxisomal compartment--partly dependent on contact of the peroxisomes to the microtubular network-are presented.
Topics: Animals; Bezafibrate; Catalase; Fatty Acids; Histocytochemistry; Humans; Immunohistochemistry; In Situ Hybridization; Kidney; L-Lactate Dehydrogenase; Liver; Male; Microbodies; Microscopy, Electron; Microtubules; Oxidoreductases; RNA, Messenger; Rats; Tumor Cells, Cultured; Urate Oxidase
PubMed: 9342614
DOI: 10.1007/s004180050160 -
Tanpakushitsu Kakusan Koso. Protein,... Jul 1987
Review
Topics: Cell Fractionation; Microbodies; Plant Physiological Phenomena; Plants
PubMed: 3334481
DOI: No ID Found -
Critical Reviews in Toxicology 1983In this critical review, I would like to provide a brief outline of the morphology, biochemical composition, distribution, and functions of peroxisomes. The induction of... (Review)
Review
In this critical review, I would like to provide a brief outline of the morphology, biochemical composition, distribution, and functions of peroxisomes. The induction of peroxisome proliferation and peroxisome-associated enzymes in the rodent liver by two classes of chemicals (hypolipidemic drugs and the industrial plasticizers) will be considered. The role of peroxisomes in lipid metabolism will be discussed. Carcinogenicity studies in rats and mice with these peroxisome proliferators will be evaluated critically. Careful consideration will be given to the hypothesis that "potent hepatic peroxisome proliferators as a class are carcinogenic." The possible mechanism(s) by which peroxisome proliferators induce liver tumors will be outlined. Particular attention will be paid to the possible role of peroxisome proliferation-mediated radical toxicity and generation of endogenous initiators of carcinogenesis.
Topics: Animals; Cell Division; Enzyme Induction; Female; Hepatomegaly; Humans; Hypolipidemic Agents; Liver; Liver Neoplasms; Male; Mice; Microbodies; Mutagens; Plasticizers; Rats; Risk
PubMed: 6360536
DOI: 10.3109/10408448309029317 -
Hoppe-Seyler's Zeitschrift Fur... Mar 1976Methods were developed to charcterize membranes and membrane components of leaf peroxisomes from Lens culinaris. While microbodies from etiolated young leaves exhibited...
Methods were developed to charcterize membranes and membrane components of leaf peroxisomes from Lens culinaris. While microbodies from etiolated young leaves exhibited an equilibrium density of 1.19 g/cm3, older leaves or leaves exposed to light for increasing periods of time contained microbodies banding at higher densities up to 1.235 g/cm3. Similar values were also found for the corresponding microbody membranes, which could be labelled with diazotized [35S]sulphanilic acid. Labelling was also performed using proteins extracted from the membranes. Their main structural protein (SP-63) was solubilized with sodium dodecylsulphate and labelled with fluorescent compounds as well as with diazotized [35S]sulphanilic acid or [3H]iodoacetic acid. These conversions greatly facilitate all analytical procedures, e.g. tracing the migration of SP-63 in gels or the movement in sucrose gradients containing sodium dodecylsulphate during zonal centrifugation. Also, labelling of SP-63 in vivo was accomplished when labelled amino acids were infused into etiolated leaves while exposing them to light.
Topics: Darkness; Isotope Labeling; Light; Membranes; Methods; Microbodies; Organoids; Plant Proteins
PubMed: 955565
DOI: 10.1515/bchm2.1976.357.1.393 -
Cell Nov 1995
Review
Topics: Biological Transport; Humans; Microbodies; Proteins; Yeasts
PubMed: 7585954
DOI: 10.1016/0092-8674(95)90091-8 -
Laboratory Investigation; a Journal of... Sep 1974
Topics: Animals; Biphenyl Compounds; Butyrates; Cell Nucleus; Clofibrate; Cytoplasm; Diet, Atherogenic; Endoplasmic Reticulum; Ethers; Freeze Etching; Lipids; Liver; Male; Membranes; Mice; Microbodies; Microscopy, Electron; Mitochondria, Liver; Organoids
PubMed: 4413769
DOI: No ID Found -
Biochemical Society Transactions May 1995
Review
Topics: Animals; Carcinogens; Humans; Liver; Liver Neoplasms; Liver Neoplasms, Experimental; Mice; Mice, Inbred C57BL; Microbodies; Vitamin A Deficiency; Xenobiotics
PubMed: 7672435
DOI: 10.1042/bst0230425 -
FEMS Microbiology Letters Dec 1992In wild-type Hansenula polymorpha the proliferation of peroxisomes in induced by various unconventional carbon- and nitrogen sources. Highest induction levels, up to 80%... (Review)
Review
In wild-type Hansenula polymorpha the proliferation of peroxisomes in induced by various unconventional carbon- and nitrogen sources. Highest induction levels, up to 80% of the cytoplasmic volume, are observed in cells grown in methanol-limited chemostat cultures. Based on our accumulated experience, we are now able to precisely adjust both the level of the peroxisome induction as well as their protein composition by specific adaptations in growth conditions. During the last few years a series of "peroxisome-deficient (per) mutants of H. polymorpha have been isolated and characterized. Phenotypically these mutants are characterized by the fact that they are not able to grow on methanol. Three mutant phenotypes were defined on the basis of morphological criteria, namely: (a) mutants completely lacking peroxisomes (Per-;13 complementation groups); (b) mutants containing few small peroxisomes which are partly impaired in the peroxisomal import of matrix proteins (Pim-; five complementation groups); and (c) mutants with aberrations in the peroxisomal substructure (Pss-; two complementation groups). In addition, several conditional Per-, Pim- and Pss- mutants have been obtained. In all cases the mutant phenotype was shown to be caused by a recessive mutation in one gene. However, we observed that different mutations in one gene may cause different morphological mutant phenotypes. A detailed genetic analysis revealed that several PER genes, essential for peroxisome biogenesis, are tightly linked and organized in a hierarchical fashion. The use of both constitual and conditional per mutants in current and future studies of the molecular mechanisms controlling peroxisome biogenesis and function is discussed.
Topics: Fungal Proteins; Microbodies; Microscopy, Electron; Models, Biological; Mutation; Pichia
PubMed: 1478473
DOI: 10.1111/j.1574-6968.1992.tb14068.x -
European Journal of Biochemistry Dec 19781. Isocitrate lyase from cotyledons of cucumber seedlings (Cucumis sativus) has been purified 100-fold. Two methods of preparing the soluble glyoxylate cycle enzyme are...
1. Isocitrate lyase from cotyledons of cucumber seedlings (Cucumis sativus) has been purified 100-fold. Two methods of preparing the soluble glyoxylate cycle enzyme are described: an elaborated method which used crude extracts of cucumber cotyledons, and another procedure which started with purified glyoxysomes from 4-day-old cotyledons and included a separation of glyoxysomal matrix enzymes by zonal centrifugation. The product behaved as a single species when tested by (a) polyacrylamide gel electrophoresis in the presence of dodecyl sulfate, (b) zonal centrifugation, and (c) double immunodiffusion against rabbit antibody to isocitrate lyase. 2. Isocitrate lyase of cucumber glyoxysomes exhibited a molecular weight of 255,000 and was composed of four apparently identical subunits of Mr 64,000. An isoelectric point of 5.9 was determined. 3. It was shown that isocitrate lyase is a glycoprotein, (a) by Schiff stain on polyacrylamide gels, (b) by periodate oxidation of the enzyme, subsequent reduction with NaB[3H]4 and electrophoretic analysis of the labelled glycoprotein, and (c) by incorporation of [3H]glucosamine in vivo into a protein which could be precipitated with antibodies to isocitrate lyase and revealed a 64,000-Mr band upon electrophoresis.
Topics: Carbohydrates; Glycoproteins; Immunodiffusion; Immunoelectrophoresis; Isocitrate Lyase; Kinetics; Microbodies; Molecular Weight; Organoids; Oxo-Acid-Lyases; Plant Proteins; Plants
PubMed: 103713
DOI: 10.1111/j.1432-1033.1978.tb12720.x