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Primary Structure and Functional Expression of the Inositol 1,4,5-Trisphosphate Receptor, P400

  • Katsuhiko Mikoshiba
  • Teiichi Furuichi
  • Nobuaki Maeda
  • Shingo Yoshikawa
  • Atsushi Miyawaki
  • Michio Niinobe
  • Kentaro Wada
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 287)

Abstract

There are several signal transduction pathways inside the cell/ such as the C-kinase/ A-kinase/ and calmodulin dependent protein kinase Systems. These Systems exert physioI09icat func-tions through phosphoryIation. However/ it is well known that calcium ions play an important role in physi0IogicaI functions/ and recently/ it has been demonstrated that inositol trisphos-phate/ a counterpart of diacy I g I ycer01 (DG) hydrolysed from phosphatidyl inositol di-Phosphates/ mobil izes calcium ions from calcium storage sites inside the cell (Berridge* 1987). Although many researchers have been working on calcium mobili-zation/ no detailed mechanism was known. Many questions have arisen/ for example/ do putative lnsP3 receptors have both lnsP3 binding sites and calcium Channels or not/ is the calcium Channel a different molecule from the lnsP3 receptor or not.

Keywords

Purkinje Cell P400 Protein Ryanodine Receptor Inositol Trisphosphate Mouse Cerebellum 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1991

Authors and Affiliations

  • Katsuhiko Mikoshiba
    • 1
    • 2
  • Teiichi Furuichi
    • 2
  • Nobuaki Maeda
    • 1
  • Shingo Yoshikawa
    • 2
  • Atsushi Miyawaki
    • 2
  • Michio Niinobe
    • 1
  • Kentaro Wada
    • 1
  1. 1.Division of Regulation of Macromolecular Function, Institute for Protein ResearchOsaka UniversitySuita, Osaka 565Japan
  2. 2.Division of Behavior and NeurobiologyNational Institute for Basic BiologyMyodaijicho, Okazaki 444Japan

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