Relevant bibliographies by topics / Microbodies

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Academic literature on the topic 'Microbodies'

Author: Grafiati
Published: 4 June 2021
Last updated: 29 July 2024

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Journal articles on the topic "Microbodies"

1

Titus, D. E., and W. M. Becker. "Investigation of the glyoxysome-peroxisome transition in germinating cucumber cotyledons using double-label immunoelectron microscopy." Journal of Cell Biology 101, no. 4 (October 1, 1985): 1288–99. http://dx.doi.org/10.1083/jcb.101.4.1288.

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Microbodies in the cotyledons of cucumber seedlings perform two successive metabolic functions during early postgerminative development. During the first 4 or 5 d, glyoxylate cycle enzymes accumulate in microbodies called glyoxysomes. Beginning at about day 3, light-induced activities of enzymes involved in photorespiratory glycolate metabolism accumulate rapidly in microbodies. As the cotyledonary microbodies undergo a functional transition from glyoxysomal to peroxisomal metabolism, both sets of enzymes are present at the same time, either within two distinct populations of microbodies with different functions or within a single population of microbodies with a dual function. We have used protein A-gold immunoelectron microscopy to detect two glyoxylate cycle enzymes, isocitrate lyase (ICL) and malate synthase, and two glycolate pathway enzymes, serine:glyoxylate aminotransferase (SGAT) and hydroxypyruvate reductase, in microbodies of transition-stage (day 4) cotyledons. Double-label immunoelectron microscopy was used to demonstrate directly the co-existence of ICL and SGAT within individual microbodies, thereby discrediting the two-population hypothesis. Quantitation of protein A-gold labeling density confirmed that labeling was specific for microbodies. Quantitation of immunolabeling for ICL or SGAT in microbodies adjacent to lipid bodies, to chloroplasts, or to both organelles revealed very similar labeling densities in these three categories, suggesting that concentrations of glyoxysomal and peroxisomal enzymes in transition-stage microbodies probably cannot be predicted based on the apparent associations of microbodies with other organelles.
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Kim, Ki Woo, Eun Woo Park, and Kyung Soo Kim. "Glyoxysomal Nature of Microbodies Complexed with Lipid Globules in Botryosphaeria dothidea." Phytopathology® 94, no. 9 (September 2004): 970–77. http://dx.doi.org/10.1094/phyto.2004.94.9.970.

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The glyoxysomal nature of microbodies was determined in Botryosphaeria dothidea hyphae based on morphology and in situ enzyme characteristics by transmission electron microscopy and cytochemistry. Bound by a single membrane, microbodies had a homogeneous matrix and varied in size ranging from 200 to 400 nm in diameter. Microbodies often had crystalline inclusions that consisted of parallel arrays of fine tubules in their matrices. Microbodies and lipid globules were placed in close association with each other, forming microbody-lipid globule complexes in hyphae. The cytochemical activities of catalase and malate synthase were localized in microbodies, showing intense electron density of the organelle. In addition, immunogold labeling detected the presence of catalase in a multivesicular body-like organelle and the cell wall as well as in the matrix and crystalline inclusion of microbodies, supporting the enzyme secretion outward. Meanwhile, isocitrate lyase was localized only in matrices of microbodies. These results suggest that the microbodies complexed with lipid globules in B. dothidea hyphae are functionally defined as glyoxysomes which may enable the fungus to survive latent periods using lipids via the glyoxylate cycle and catalase secretion.
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Carson, David B., and Joseph J. Cooney. "Characterization of partially purified microbodies from hydrocarbon-grown cells of Cladosporium resinae." Canadian Journal of Microbiology 35, no. 5 (May 1, 1989): 565–72. http://dx.doi.org/10.1139/m89-090.

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Cells of the filamentous fungus Cladosporium resinae synthesize many more microbodies when they are grown on an n-alkane than when they are grown on glucose. Cladosporium resinae was grown on n-dodecane and spheroplasts were prepared, disrupted, and fractionated by differential and density gradient centrifugation. A fraction was isolated which was enriched in catalase, a marker enzyme for microbodies. Another fraction was isolated which was enriched in cytochrome c oxidase, a marker for mitochondria. Urate oxidase, a second marker for microbodies, was not detected in cell extracts. The microbody and mitochondrial fractions were relatively free of contamination from the endoplasmic reticulum and cytosol as indicated by the amounts of glucose-6-phosphatase and glucose-6-phosphate dehydrogenase present, respectively. Transmission electron microscopy revealed that the catalase-enriched fraction contained intact microbodies, with mitochondria as a minor contaminant. Catalase was localized in microbodies by staining with 3,3′-diaminobenzidine. Mitochrondria were present in the cytochrome c oxidase enriched fraction and took up the vital stain Janus green B. In similar preparations from cells grown on glucose, catalase was largely nonparticulate. Microbodies were not observed in thin sections prepared from density gradient fractions, but mitochondria were present in a cytochrome c oxidase enriched fraction.Key words: Cladosporium resinae, microbodies, mitochondria, catalase, cytochrome c oxidase.
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Schliebs, Wolfgang, Christian Würtz, Wolf-Hubert Kunau, Marten Veenhuis, and Hanspeter Rottensteiner. "A Eukaryote without Catalase-Containing Microbodies: Neurospora crassa Exhibits a Unique Cellular Distribution of Its Four Catalases." Eukaryotic Cell 5, no. 9 (September 2006): 1490–502. http://dx.doi.org/10.1128/ec.00113-06.

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ABSTRACT Microbodies usually house catalase to decompose hydrogen peroxide generated within the organelle by the action of various oxidases. Here we have analyzed whether peroxisomes (i.e., catalase-containing microbodies) exist in Neurospora crassa. Three distinct catalase isoforms were identified by native catalase activity gels under various peroxisome-inducing conditions. Subcellular fractionation by density gradient centrifugation revealed that most of the spectrophotometrically measured activity was present in the light upper fractions, with an additional small peak coinciding with the peak fractions of HEX-1, the marker protein for Woronin bodies, a compartment related to the microbody family. However, neither in-gel assays nor monospecific antibodies generated against the three purified catalases detected the enzymes in any dense organellar fraction. Furthermore, staining of an N. crassa wild-type strain with 3,3′-diaminobenzidine and H2O2 did not lead to catalase-dependent reaction products within microbodies. Nonetheless, N. crassa does possess a gene (cat-4) whose product is most similar to the peroxisomal type of monofunctional catalases. This novel protein indeed exhibited catalase activity, but was not localized to microbodies either. We conclude that N. crassa lacks catalase-containing peroxisomes, a characteristic that is probably restricted to a few filamentous fungi that produce little hydrogen peroxide within microbodies.
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Carson, David B., and Joseph J. Cooney. "Microbodies in fungi: a review." Journal of Industrial Microbiology 6, no. 1 (September 1990): 1–18. http://dx.doi.org/10.1007/bf01576172.

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Stabenau, Helmut, Werner Säftel, and Uwe Winkler. "Microbodies of the alga Chara." Physiologia Plantarum 118, no. 1 (April 16, 2003): 16–20. http://dx.doi.org/10.1034/j.1399-3054.2003.00004.x.

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Hajra, A. "Glycerolipid biosynthesis in peroxisomes (microbodies)." Progress in Lipid Research 34, no. 4 (December 1995): 343–64. http://dx.doi.org/10.1016/0163-7827(95)00013-5.

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Veenhuis, M., M. Mateblowski, W. H. Kunau, and W. Harder. "Proliferation of microbodies inSaccharomyces cerevisiae." Yeast 3, no. 2 (June 1987): 77–84. http://dx.doi.org/10.1002/yea.320030204.

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Pan, Yanhong, Wenxia Zheng, Alison E. Moyer, Jingmai K. O’Connor, Min Wang, Xiaoting Zheng, Xiaoli Wang, Elena R. Schroeter, Zhonghe Zhou, and Mary H. Schweitzer. "Molecular evidence of keratin and melanosomes in feathers of the Early Cretaceous bird Eoconfuciusornis." Proceedings of the National Academy of Sciences 113, no. 49 (November 21, 2016): E7900—E7907. http://dx.doi.org/10.1073/pnas.1617168113.

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Microbodies associated with feathers of both nonavian dinosaurs and early birds were first identified as bacteria but have been reinterpreted as melanosomes. Whereas melanosomes in modern feathers are always surrounded by and embedded in keratin, melanosomes embedded in keratin in fossils has not been demonstrated. Here we provide multiple independent molecular analyses of both microbodies and the associated matrix recovered from feathers of a new specimen of the basal bird Eoconfuciusornis from the Early Cretaceous Jehol Biota of China. Our work represents the oldest ultrastructural and immunological recognition of avian beta-keratin from an Early Cretaceous (∼130-Ma) bird. We apply immunogold to identify protein epitopes at high resolution, by localizing antibody–antigen complexes to specific fossil ultrastructures. Retention of original keratinous proteins in the matrix surrounding electron-opaque microbodies supports their assignment as melanosomes and adds to the criteria employable to distinguish melanosomes from microbial bodies. Our work sheds new light on molecular preservation within normally labile tissues preserved in fossils.
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Keller, G. A., S. Krisans, S. J. Gould, J. M. Sommer, C. C. Wang, W. Schliebs, W. Kunau, S. Brody, and S. Subramani. "Evolutionary conservation of a microbody targeting signal that targets proteins to peroxisomes, glyoxysomes, and glycosomes." Journal of Cell Biology 114, no. 5 (September 1, 1991): 893–904. http://dx.doi.org/10.1083/jcb.114.5.893.

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Peroxisomes, glyoxysomes, glycosomes, and hydrogenosomes have each been classified as microbodies, i.e., subcellular organelles with an electron-dense matrix that is bound by a single membrane. We investigated whether these organelles might share a common evolutionary origin by asking if targeting signals used for translocation of proteins into these microbodies are related. A peroxisomal targeting signal (PTS) consisting of the COOH-terminal tripeptide serine-lysine-leucine-COOH has been identified in a number of peroxisomal proteins (Gould, S.J., G.-A. Keller, N. Hosken, J. Wilkinson, and S. Subramani. 1989. J. Cell Biol. 108:1657-1664). Antibodies raised to a peptide ending in this sequence (SKL-COOH) recognize a number of peroxisomal proteins. Immunocryoelectron microscopy experiments using this anti-SKL antibody revealed the presence of proteins containing the PTS within glyoxysomes of cells from Pichia pastoris, germinating castor bean seeds, and Neurospora crassa, as well as within the glycosomes of Trypanosoma brucei. Western blot analysis of purified organelle fractions revealed the presence of many proteins containing this PTS in both glyoxysomes and glycosomes. These results indicate that at least one of the signals, and therefore the mechanism, for protein translocation into peroxisomes, glyoxysomes, and glycosomes has been conserved, lending support to a common evolutionary origin for these microbodies. Hydrogenosomes, the fourth type of microbody, did not contain proteins that cross-reacted with the anti-PTS antibody, suggesting that this organelle is unrelated to microbodies.
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Dissertations / Theses on the topic "Microbodies"

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Nyisztor, Michael. "The Leishmania donovani peroxin 14 N-terminal region is important for glycosomal localization." Thesis, McGill University, 2007. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=100200.

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Glycosomes are subcellular organelles that are evolutionarily related to the peroxisomes of higher eukaryotes. The Leishmania glycosome performs various metabolic processes that are essential for the survival of these parasites, such as the glycolytic process. Proteins that are destined for import into the glycosome interact selectively with specific cytosolic receptors peroxin 5(PEX5) or PEX7. The PEX5-protein complex migrates toward the glycosomal membrane where it interacts with PEX14, a vital step for protein important into the glycosome.
This project investigated the interaction mechanism of Leishmania donovani PEX14 with the glycosomal membrane. The regions responsible for PEX14 interaction with the glycosomal membrane are established in higher eukaryotes. LdPEX14 is poorly conserved with respect to the other PEX14 homologues. In Leishmania the interaction of LdPEX14 with the glycsomal membrane has been shown to be unique in terms of its lack of insertion in the glycosomal membrane. Using LdPEX14 mutants it was determined that the first 63 amino acids are important for the interaction of LdPEX14 with the glycosomal membrane. Results further suggest that LdPEX14 is a homopolymer forming a complex of 20S in size which is vital for the proper functioning of the glycosome.
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Tiao, Jim Yu-Hsiang. "The neuregulin-3 intracellular domain is biologically active : molecular and functional characterisation of protein interactions." University of Western Australia. School of Medicine and Pharmacology, 2006. http://theses.library.uwa.edu.au/adt-WU2006.0083.

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[Truncated abstract] Neuregulins (NRG’s) are pleiotropic growth factors that participate in a wide range of biological processes. The family of membrane-bound growth factors bind to and activate ErbB receptors on adjacent target cells, mediating multiple biological processes. NRG-1, NRG-2 and NRG-3 are all highly expressed in the nervous system, where it has been shown that NRG-1 is important for neuronal development, migration, synapse formation and glial cell proliferation. Little is known, however, on the specific roles of NRG-2 and NRG-3, although it is apparent that despite similar expression patterns and overlapping receptor specificity, NRG-2 and NRG-3 do not compensate for the loss of NRG-1 and mediate their own distinct activities. … Subcellular localisation experiments showed that this domain is important for trafficking of the fulllength protein to various intracellular compartments in an activity dependent manner. In addition, the ICD is required to elicit a cell death response in cultured cells and provoke an elevated α-amino-3-hydroxyl-5-methylisoxazole-4-propionate (AMPA) response in organotypic neuronal cultures following transient expression of NRG-3. A yeast two-hybrid screen identified 14-3-3ζ and PICK1 as two proteins that interacte with the human NRG-3 ICD. These interactions were confirmed both in vitro and in vivo, and were further characterised at a molecular level. This study demonstrates the ability of NRG-3 to mediate signal transduction through a biologically active ICD; a conclusion supported by identifying cytoplasmic proteins that interact with the ICD. These observations point to an additional layer of complexity where bi-directional signalling contributes to the full repertoire of NRG-3 functions.
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Managadze, David [Verfasser]. "Biogenesis of microbodies in the filamentous fungus Neurospora crassa / submitted by David Managadze." 2007. http://d-nb.info/986308900/34.

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Books on the topic "Microbodies"

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Angermüller, Sabine. Peroxisomal oxidases: Cytochemical localization and biological relevance. Stuttgart: G. Fischer, 1989.

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1933-, Fahimi H. Dariush, Sies H. 1942-, European Cell Biology Organization, and International Symposium on Peroxisomes in Biology and Medicine (1986 : Heidelberg, Germany), eds. Peroxisomes in biology and medicine. Berlin: Springer-Verlag, 1987.

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Brian, Dunford H., and Dunford H. Brian, eds. Peroxidases and catalases: Biochemistry, biophysics, biotechnology, and physiology. 2nd ed. Hoboken, N.J: John Wiley & Sons, 2010.

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K, Reddy Janardan, ed. Peroxisomes: Biology and role in toxicology and disease. New York, N.Y: New York Academy of Sciences, 1996.

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Alison, Baker, and Graham Ian A, eds. Plant peroxisomes: Biochemistry, cell biology, and biotechnological applications. Dordrecht: Kluwer Academic Publishers, 2002.

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Denis, Crane, ed. The peroxisome: A vital organelle. Cambridge: Cambridge University Press, 1995.

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Symposium, Society for the Study of Inborn Errors of Metabolism. Inborn errors of cellular organelles: Peroxisomes and mitochondria : proceedings of the 24th Annual Symposium of the SSIEM, Amersfoort, the Netherlands, September 1986. Lancaster, England: MTP Press, 1987.

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M, Meyers Kenneth, and Barnes Charles D, eds. The Platelet amine storage granule. Boca Raton: CRC Press, 1992.

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Graziella, Uziel, Wanders Ronald J. A, and Cappa Marco, eds. Adrenoleukodystrophy and other peroxisomal disorders: Clinical, biochemical, genetic, and therapeutic aspects : proceedings of the International Workshop on Adrenoleukodystrophy and Peroxisomal Disorders, Rome, 10-11 November 1989. Amsterdam: Excerpta Medica, 1990.

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X, Caddick M., ed. Microbial responses to light and time: Fifty-sixth Symposium of the Society for General Microbiology : held at the University of Nottingham, March 1998. Cambridge: Cambridge University Press, 1998.

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Book chapters on the topic "Microbodies"

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Donaldson, Robert. "Microbodies." In Plant Cells and their Organelles, 88–109. Chichester, UK: John Wiley & Sons, Ltd, 2016. http://dx.doi.org/10.1002/9781118924846.ch5.

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Schmoldt, Hans-Ulrich, Matin Daneschdar, Harald Kolmar, and Michael Blind. "Microbodies™." In Methods in Molecular Biology, 361–72. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-557-2_20.

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Hock, B., C. Gietl, and C. Sautter. "Biogenesis of Plant Microbodies." In Proceedings in Life Sciences, 417–25. Berlin, Heidelberg: Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-71325-5_45.

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Opperdoes, F. R. "Biogenesis of Glycosomes (Microbodies) in the Trypanosomatidae." In Proceedings in Life Sciences, 426–35. Berlin, Heidelberg: Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-71325-5_46.

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Veenhuis, M., and W. Harder. "Metabolic Significance and Biogenesis of Microbodies in Yeasts." In Proceedings in Life Sciences, 436–58. Berlin, Heidelberg: Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-71325-5_47.

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"Microbodies." In Encyclopedia of Parasitology, 1641. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-43978-4_1939.

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"Microbodies." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics, 1206. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_10326.

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Wang, Qiuyu, Chris Smith, and Emma Davis. "Microbodies." In Thrive in Cell Biology. Oxford University Press, 2013. http://dx.doi.org/10.1093/hesc/9780199697328.003.0012.

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This chapter identifies microbodies as globular-shaped organelles surrounded by a single biological membrane. It highlights three types of microbodies that are recognizable in different types of cells: peroxisomes, glyoxysomes, and glycosomes. It also describes peroxisomes as roughly spherical organelles that are widely distributed in eukaryotes and enriched in urate and d-amino acid oxidases and catalase activities. The chapter examines glyoxysomes, which are specialized peroxisomes found particularly in plant lipid storage structures, such as the endosperm or the cotyledons of germinating seeds and occur in filamentous fungi. It considers glycosomes as membrane-enclosed organelles which occur in a relatively few species of protozoa called trypanosomes.
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Merrett, Michael J. "MICROBODIES, LYSOSOMES, AND AUTOPHAGIC VACUOLES." In Subcellular Biochemistry and Molecular Biology, 315–33. Elsevier, 1989. http://dx.doi.org/10.1016/b978-0-12-139904-7.50010-5.

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Ghadially, Feroze N. "Microbodies (peroxisomes, microperoxisomes and catalosomes)." In Ultrastructural Pathology of the Cell and Matrix, 767–86. Elsevier, 1988. http://dx.doi.org/10.1016/b978-0-407-01572-2.50009-5.

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Conference papers on the topic "Microbodies"

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Lui, Bonny Gaby, Joycelyn Wüstehube-Lausch, Hans-Ulrich Schmoldt, Matin Daneschdar, and Ugur Sahin. "Process Development for the Identification of Novel Microbodies against NSCLC Related Targets." In The 2nd World Congress on Recent Advances in Nanotechnology. Avestia Publishing, 2017. http://dx.doi.org/10.11159/nddte17.117.

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