Proceedings of the Japan Academy, Series B
Online ISSN : 1349-2896
Print ISSN : 0386-2208
ISSN-L : 0386-2208
Volume 90, Issue 3
Displaying 1-3 of 3 articles from this issue
Review
  • Koji TANABE, Kazutoshi TAKAHASHI, Shinya YAMANAKA
    2014 Volume 90 Issue 3 Pages 83-96
    Published: March 11, 2014
    Released on J-STAGE: March 11, 2014
    JOURNAL FREE ACCESS FULL-TEXT HTML
    The “reversion of cell fate from differentiated states back into totipotent or pluripotent states” has been an interest of many scientists for a long time. With the help of knowledge accumulated by those scientists, we succeeded in converting somatic cells to a pluripotent cell lineage by the forced expression of defined factors. These established induced pluripotent stem (iPS) cells have similar features to embryonic stem (ES) cells, including pluripotency and immortality. The iPS cell technology provides unprecedented opportunities for regenerative medicine and drug discovery.
Original Articles
  • Shun-ichiro KARATO
    2014 Volume 90 Issue 3 Pages 97-103
    Published: March 11, 2014
    Released on J-STAGE: March 11, 2014
    JOURNAL FREE ACCESS FULL-TEXT HTML
    One of the difficulties of the current giant impact model for the origin of the Moon is to explain the marked similarity in the isotopic compositions and the substantial differences in the major element chemistry. Physics of shock heating is analyzed to show that the degree of heating is asymmetric between the impactor and the target, if the target (the proto-Earth) had a magma-ocean but the impactor did not. The magma ocean is heated much more than the solid impactor and the vapor-rich jets come mainly from the magma-ocean from which the Moon might have been formed. In this scenario, the similarity and differences in the composition between the Moon and Earth would be explained as a natural consequence of a collision in the later stage of planetary formation. Including the asymmetry in shock heating is the first step toward explaining the chemical composition of the Moon.
  • Naoki KANEKO, Rie YAMAMOTO, Taka-Aki SATO, Koichi TANAKA
    2014 Volume 90 Issue 3 Pages 104-117
    Published: March 11, 2014
    Released on J-STAGE: March 11, 2014
    JOURNAL FREE ACCESS FULL-TEXT HTML
    Proteolytic processing of the amyloid precursor protein (APP) by β-secretase and γ-secretase leads to the generation and deposition of amyloid β (Aβ) in Alzheimer’s disease (AD). N-terminally or C-terminally truncated Aβ variants have been found in human cerebrospinal fluid and cultured cell media using immunoprecipitation and mass spectrometry. Unfortunately, the profile of plasma Aβ variants has not been revealed due to the difficulty of isolating Aβ from plasma. We present here for the first time studies of Aβ and related peptides in human plasma. Twenty-two Aβ-related peptides including novel peptides truncated before the β-secretase site were detected in human plasma and 20 of the peptides were identified by tandem mass spectrometry. Using an internal standard, we developed a quantitative assay for the Aβ-related peptides and demonstrated plasma dilution linearity and the precision required for their quantitation. The present method should enhance the understanding of APP processing and clearance in AD progression.
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