• Search Research Projects
  • Search Researchers
  • How to Use
  1. Back to project page

1991 Fiscal Year Final Research Report Summary

Functional Modification of Calcium Dependent Proteins by Phosphorylation

Research Project

Project/Area Number 02680156
Research Category

Grant-in-Aid for General Scientific Research (C)

Allocation TypeSingle-year Grants
Research Field 代謝生物化学
Research InstitutionNagoya University

Principal Investigator

KOBAYASHI Ryoji  Nagoya Univ., School of Med., associate professor, 医学部, 助教授 (00020917)

Co-Investigator(Kenkyū-buntansha) HAGIWARA Masatoshi  Nagoya Univ., School of Med., assistant professor, 医学部, 助手 (10208423)
Project Period (FY) 1990 – 1991
KeywordsCalcium Signaling / Annexin / EF-hand protein / Calcium binding protein / Calcium signal network
Research Abstract

It is generally accepted that intracellular calcium is involved in regulation various biochemical events in excitable cells. These events mediated by a family of homologous calcium-binding proteins. In this research, we focuse of EF-hand type calcium binding proteins and calcium dependent phospholipid binding proteins (Annexin family) in the many families of calcium binding proteins and tried to identify the new members of these family proteins and to reveal the function of these proteins. Firstly, we identified three proteins from smooth muscle, lens and spleen as family proteins of Annexin. Physicochemical properties of three proteins were accordance with those of Annexin family proteins such as calcium dependent phospholipid binding inhibitory action of phospholipase A_2 and actin binding. We revealed the tissue distribution using polyclonal antibodies. In the second course of this research, we purified four EF-hand type calcium binding proteins from lung, smooth muscle, aortic tissue and placenta. All these four proteins had two Ef-hand structures in those molecules and belonged to S100 protein family. In the four calcium binding proteins, calcyclin purified from rabbit lung had 50 kDa target protein in the same tissue. We identified that this protein, named CAP-50 (calcyclin associate protein with 50 kDa of molecular mass), was a family protein of Annexin. This result suggests that in intracellular calcium signalling system, different calcium binding protein had different pathways of signal and those pathways had interaction each other at the same time.

  • Research Products

    (12 results)

All Other

All Publications (12 results)

  • [Publications] R.Kobayashi et al.: "Purification,biological properties and partial sequence analysis of 67-kDa calcimedin and its 34-kDa fragment frim chicken gizzard." Eur.J.Biochem.188. 447-453 (1990)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] R.Kobayashi et al.: "Isolation and characterization of three distinct 34 kDa EDTA-extractable proteins from bovine lens." Biochim.Biophys.Acta. 1034. 4-10 (1990)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] R.Kobayashi et al.: "Purification,characterization and partial sequence analysis of 32-dDa calcimedin from chicken gizzard." Arch.Biochem.Biophys.277. 203-210 (1990)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] H.Tokumitsu et al.: "A calcium-binding protein from rabbit lung cytosol identified as the product of growth-regulated gene (2A9) and its binding proteins." Arch.Biochem.Biophys.288. 202-207 (1991)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] H.Todoroki et al.: "Purificaton,characterization and partial sequence analysis of a newly identified EF-hand type 13 kDa Ca-binding protein from smooth muscle and non-muscletissues." J.Biol.Chem.266. 18668-18673 (1991)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] H.Tokumitsu et al.: "A calcyclin-associated protein is a newly identified member of the Ca^<2+>/phospholipid-binding proteins,annexin family." J.Biol.Chem.

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] R. Kobayashi et al.: "Purification, biological properties and partial sequence analysis of 67-kDa calcimedin and its 34-kDa fragment firm chicken gizzard." Eur. J. Biochem.188. 447-453 (1990)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] R. Kobayashi et al.: "Isolation and characterization of three distinct 34 kDa EDTA-extractable proteins from bovine lens." Biochim. Biophys. Acta. 1034. 4-10 (1990)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] R. Kobayashi et al.: "Purification, characterization and partial sequence analysis of 32-kDa calcimedin from chicken gizzard." Arch. Biochem. Biophys.277. 203-210 (1990)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] H. Tokumitsu et al.: "A calcium-binding protein from rabbit lung cytosol identified as the product of growth-regulated gene (2A9) and is binding proteins." Arch. Biochem. Biophys.288. 202-207 (1991)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] H. Todoroki et al.: "Purification, characterization and partial sequence analysis of a newly identified EF-hand type 13 kDa Ca-binding protein from smooth muscle and non-muscletissues." J. Biol. Chem.266. 18668-18673 (1991)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] H. Tokumitsu et al.: "A calcyclin-associated protein is a newly identified member of the Ca^<2+>/phospholipid-binding proteins, annexin family." J. Biol. Chem.

    • Description
      「研究成果報告書概要(欧文)」より

URL: 

Published: 1993-03-16  

Information User Guide FAQ News Terms of Use Attribution of KAKENHI

Powered by NII kakenhi