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  • Articles  (6)
  • Cellulose microfibril  (4)
  • *Signal Transduction  (2)
  • 2020-2020
  • 1995-1999  (6)
  • 1955-1959
  • 1920-1924
  • 1
    Electronic Resource
    Electronic Resource
    Evidence for the role of the glomerulocyte in cellulose synthesis in the tunicate,Metandrocarpa uedai (1995)
    Springer
    Protoplasma 186 (1995), S. 24-33 
    Details
    ISSN: 1615-6102
    Keywords: Cellulose microfibril ; Electron diffraction ; Glomerulocyte ; Metandrocarpa uedai ; Tunic ; Vacuole-like structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The tunicate,Metandrocarpa uedai, contains a large quantity of cellulose; however, it is not known how and where the cellulose is synthesized. Based on evidence from electron diffraction and conventional thin-sectioning for electron microscopy, this study shows that the glomerulocyte is involved in the synthesis of cellulose. The bundles of microfibrils in the glomerulocyte as well as the tunic were identified as cellulose I using selected area electron diffraction analysis. The diffraction pattern of cellulose in the glomerulocyte was similar to that from the tunic, suggesting that the crystallization of cellulose already is initiated in the glomerulocyte. The diameter of cellulose microfibrils, both in the glomerulocyte and the tunic was the same, about 16 nm. These results suggest that the glomerulocyte is the most probable site for the synthesis of cellulose in the tunic ofM. uedai. Using thin-sectioning techniques, a series of observations showed that individual microfibrils are primarily assembled in structures tentatively identified as vacuole-like structures, then they are bundled by a tapering region within the vacuole-like structures. These bundles of microfibrils are deposited in a continuously circular arrangement. The microtubules are oriented parallel to the bundles of microfibrils at the tapering vacuole-like structure, and they may be involved in the tapering of these structures (perhaps controlling the shape). This study also provides the first account for the involvement of a vacuole-like structure in the synthesis of cellulose microfibrils among living organisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01276931
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  • 2
    Electronic Resource
    Electronic Resource
    New cellulose synthesizing complexes (terminal complexes) involved in animal cellulose biosynthesis in the tunicateMetandrocarpa uedai (1996)
    Springer
    Protoplasma 194 (1996), S. 151-163 
    Details
    ISSN: 1615-6102
    Keywords: Cellulose microfibril ; Freeze-fracture ; Terminal complex ; Tunic ; Tunicate ; Ascidian
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Cellulose synthesizing enzyme complexes (terminal complexes, TCs) have been found in the plasma membrane of epidermal cells in the tunicateMetandrocarpa uedai by using freeze-fracture replication techniques for electron microscopy. Assembly of cellulose microfibrils by TCs is a universal phenomenon in the biological kingdoms. The TCs are locally distributed in the plasma membrane of the epidermal cells facing the tunic, and no TCs are observed on the lateral membranes bordered by tight junctions. The TCs consist of two types of membrane subunits: large particles (14.5 nm in diameter) on the periphery and small subunit particles (7.2 nm) filling the center; the latter are hypothesized to be involved in cellulose synthesis. The TCs are the linear type (ca. 195 nm in length and 78 nm in width). Direct connections of TCs with the termini of microfibrils were observed. Amorphous regions, which were hypothesized the nascent microfibrils, were associated with the depressions of the TCs. The distortion of microfibrils on their terminus indicates that the crystallization may occur at the margin of TCs from which the microfibrils are discharged. This report provides evidence that: (1) The outer cell membrane of epidermis is the site for the assembly of cellulose microfibrils in the tunic; (2) a new type of TC is involved in the biosynthesis of cellulose microfibrils in the tunicates; (3) disorganized glucan chains may be synthesized in the depression of TCs and crystallized outside the E-surface of the epidermal cell membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01882023
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  • 3
    Electronic Resource
    Electronic Resource
    High-resolution electron microscopy on ultrathin sections of cellulose microfibrils generated by glomerulocytes inPolyzoa vesiculiphora (1998)
    Springer
    Protoplasma 203 (1998), S. 84-90 
    Details
    ISSN: 1615-6102
    Keywords: Cellulose microfibril ; Cross-sectional shape ; Lattice image ; Lattice orientation ; Glomerulocyte
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Glomerulocyte cellulosic bundles ofPolyzoa vesiculiphora were investigated by microdiffraction and high-resolution electron microscopy. In each bundle, hundreds of cellulose microfibrils, having a rectangular cross-sectional shape, are packed regularly with their 0.6 nm lattice planes parallel to each other. Lattice images reveal that the 0.6 nm plane is parallel to the longer edge of the cross section which is similar to the lattice organization of cellulose with a squarish cross section inValonia spp. More interestingly, all the microfibrils in a bundle have the same directionality of crystallographic c-axis, which suggests that the biosynthesis of the microfibrils within particular bundle occurs unidirectionally.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01280590
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  • 4
    Electronic Resource
    Electronic Resource
    A new cellulosic structure, the tunic cord in the ascidianPolyandrocarpa misakiensis (1998)
    Springer
    Protoplasma 204 (1998), S. 94-102 
    Details
    ISSN: 1615-6102
    Keywords: Ascidian ; Cellulose microfibril ; Hemocoel ; Polyandrocarpa misakiensis ; Tunic cord
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A specialized structure of tunic cord inPolyandrocarpa misakiensis is investigated by electron microscopy. The tunic cord is a cord-like coiled structure of 5–30 μm in diameter and 0.1–9.0 mm in length. The tunic cords originate and elongate from the dorsal tunic, and their termini have a swollen and ornamented structure. Scanning and transmission electron micrographs and the electron diffractogram show that the tunic cords are composed of bundled microfibrils of cellulose I with high crystallinity. The tunic cord is completely surrounded by single-layered epidermal cells, which have been found as the site of cellulose biosynthesis. A number of tunic cords are connected to the internal tunic of the siphon by forming “eyelet” structures at their termini. These observations suggest that the tunic cords act as a connector between dorsal and internal tunic of the siphon.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01282297
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  • 5
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    Synergistic signaling in fetal brain by STAT3-Smad1 complex bridged by p300 (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-04-16
    Description: The cytokines LIF (leukemia inhibitory factor) and BMP2 (bone morphogenetic protein-2) signal through different receptors and transcription factors, namely STATs (signal transducers and activators of transcription) and Smads. LIF and BMP2 were found to act in synergy on primary fetal neural progenitor cells to induce astrocytes. The transcriptional coactivator p300 interacts physically with STAT3 at its amino terminus in a cytokine stimulation-independent manner, and with Smad1 at its carboxyl terminus in a cytokine stimulation-dependent manner. The formation of a complex between STAT3 and Smad1, bridged by p300, is involved in the cooperative signaling of LIF and BMP2 and the subsequent induction of astrocytes from neural progenitors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakashima, K -- Yanagisawa, M -- Arakawa, H -- Kimura, N -- Hisatsune, T -- Kawabata, M -- Miyazono, K -- Taga, T -- New York, N.Y. -- Science. 1999 Apr 16;284(5413):479-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Cell Biology, Cell Fate Modulation Research Unit, Medical Research Institute, Tokyo Medical and Dental University, Tokyo 101-0062, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10205054" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Astrocytes/cytology ; Bone Morphogenetic Protein 2 ; Bone Morphogenetic Protein Receptors ; Bone Morphogenetic Proteins/metabolism/pharmacology ; COS Cells ; Cell Differentiation ; Cell Nucleus/metabolism ; Cells, Cultured ; Cytokines/*pharmacology ; DNA-Binding Proteins/*metabolism ; E1A-Associated p300 Protein ; Glial Fibrillary Acidic Protein/genetics ; Growth Inhibitors/metabolism/pharmacology ; *Interleukin-6 ; Leukemia Inhibitory Factor ; Leukemia Inhibitory Factor Receptor alpha Subunit ; Lymphokines/metabolism/pharmacology ; Mice ; Nuclear Proteins/*metabolism ; Promoter Regions, Genetic ; Receptors, Cell Surface/metabolism ; Receptors, Cytokine/metabolism ; *Receptors, Growth Factor ; Receptors, OSM-LIF ; STAT3 Transcription Factor ; Sequence Deletion ; *Signal Transduction ; Smad Proteins ; Smad1 Protein ; Stem Cells/cytology/metabolism ; Telencephalon/embryology/metabolism ; Trans-Activators/*metabolism ; *Transcriptional Activation ; *Transforming Growth Factor beta
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 6
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    Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-02
    Description: The substrate-specific protein chaperone Hsp90 (heat shock protein 90) from Saccharomyces cerevisiae functions in diverse signal transduction pathways. A mutation in YDJ1, a member of the DnaJ chaperone family, was recovered in a synthetic-lethal screen with Hsp90 mutants. In an otherwise wild-type background, the ydj1 mutation exerted strong and specific effects on three Hsp90 substrates, derepressing two (the estrogen and glucocorticoid receptors) and reducing the function of the third (the tyrosine kinase p60v-src). Analysis of one of these substrates, the glucocorticoid receptor, indicated that Ydj1 exerts its effects through physical interaction with Hsp90 substrates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kimura, Y -- Yahara, I -- Lindquist, S -- New York, N.Y. -- Science. 1995 Jun 2;268(5215):1362-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Cell Biology, University of Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7761857" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Fungal Proteins/genetics/*physiology ; HSP40 Heat-Shock Proteins ; HSP90 Heat-Shock Proteins/genetics/*physiology ; *Heat-Shock Proteins ; Molecular Chaperones/genetics/*physiology ; Molecular Sequence Data ; Oncogene Protein pp60(v-src)/metabolism ; Point Mutation ; Protein Conformation ; Receptors, Estrogen/metabolism ; Receptors, Glucocorticoid/metabolism ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins ; *Signal Transduction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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