Seibutsu Butsuri
Online ISSN : 1347-4219
Print ISSN : 0582-4052
ISSN-L : 0582-4052
Volume 39, Issue 4
Issue 224
Displaying 1-11 of 11 articles from this issue
Overview
  • Mitsuhiro MORITA, Yoshihisa KUDO
    1999 Volume 39 Issue 4 Pages 211-216
    Published: July 25, 1999
    Released on J-STAGE: April 12, 2000
    JOURNAL FREE ACCESS
    The properties of glial cells are overviewed. The word of glia covers all the non-excitable cells in nervus system and consists of astrocyte, oligodendrocyte, Schwann's cell and microglia. The physiological function of glial cells has been considered to be restricted to long term neuronal function such as physical protection of neurons and metabolism, but recent development of Ca imaging technology revealed the dynamic change of glial ghysiology and the relationship of glial cells to the central problems in neuroscience such as synaptic transmission and its plasticity. Cell culture system has been the main approach to glial cell function, but the development of technology to access the glial cell property in neuronal tissue is in progress.
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  • Satoshi B. SATO
    1999 Volume 39 Issue 4 Pages 217-222
    Published: July 25, 1999
    Released on J-STAGE: April 12, 2000
    JOURNAL FREE ACCESS
    Endocytosis is involved in information-processing in many cell types. Recent research efforts revealed its regulatory mechanism at the synaptic terminus and regulated internalization of many G-protein coupled receptors and cell adhesion molecules. Moreover, an important break-through has been brought about by establishment of the usage of actin-dependent mechanisms. The drasitic advance in understanding of the molecular mechanism is now widening its biological significance as the global linkage among membrane traffic, cytoskeletal dynamics and signal transduction.
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Review
  • So-ichiro NISHIYAMA, Michio HOMMA, Ikuro KAWAGISHI
    1999 Volume 39 Issue 4 Pages 223-228
    Published: July 25, 1999
    Released on J-STAGE: April 12, 2000
    JOURNAL FREE ACCESS
    Thermotaxis in Escherichia coli as a model system for studying thermosensing mechanisms. All the components involved in the signal transduction circuit have been indentified. Thermosensors are the transmembrane proteins that were originally indentified as chemoreceptors. They regulate the activity of the cytoplasmic histidine kinase CheA. Recent studies revealed some unique and unexpected features of these "thermometer proteins", including effects of receptor covalent modification on thermosensing properties, and uncoupling of intra- and extracellular domains under some conditions. Investigation of thermosensing properties of the sensors should also be required for understanding their chemosensing mechanisms.
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  • Ken SEKIMOTO
    1999 Volume 39 Issue 4 Pages 229-234
    Published: July 25, 1999
    Released on J-STAGE: April 12, 2000
    JOURNAL FREE ACCESS
    The energetics in the world of fluctuation is prerequisit for understanding the fundamental mechanism of a single motor protein, since the average and macroscopic descriptions in terms of thermodynamics, statistical mechanics or reaction rate are inadequate. We try to reconstruct the macroscopic concepts such as heat, chemical potential, and control in the world of fluctuation.
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  • Yohko TANAKA-TAKIGUCHI, Tomohiko J. ITOH, Hirokazu HOTANI
    1999 Volume 39 Issue 4 Pages 235-239
    Published: July 25, 1999
    Released on J-STAGE: April 12, 2000
    JOURNAL FREE ACCESS
    To examine the relationship between the growth polarity of microtubules and guanine nucleotide dependence, we polymerized microtubules from axonemes either with GTP or with GTP and GDP, and observed individual microtubules by dark-field microscopy. We used a perfusion chamber to monitor the growth polarity of microtubules from the same axoneme. Exchanging a solution containing only GTP for one containing GTP and GDP elicited a switch in the growth polarity of microtubules from the plus ends to the minus ends. These results suggest that GDP directly affects microtubule polymerization and inverts growth polarity, probably by inhibiting growth at the plus ends.
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  • Naotaka HAMASAKI
    1999 Volume 39 Issue 4 Pages 240-245
    Published: July 25, 1999
    Released on J-STAGE: April 12, 2000
    JOURNAL FREE ACCESS
    The current prevalent consensus of membrane proteins is that the transmembrane peptide portions have always been regarded as being surrounded by boundary lipids, interacting with hydrophobic surfaces of the peptide portions. It is true for all single-spanning bitopic membrane proteins. For multi-spanning polytopic membrane proteins, however, some transmembrane peptide portions could remain in the membrane lipid bilayer without having to associate with boundary lipids: instead, they art stabilized by the rest of peptide portions of the molecules.
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Experimental techniques
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