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1992 Fiscal Year Final Research Report Summary

Molecular Pharmacology of Calcium Signal Transduction

Research Project

Project/Area Number 02454134
Research Category

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

Allocation TypeSingle-year Grants
Research Field General pharmacology
Research InstitutionMie University(School of Medicine)

Principal Investigator

TANAKA Toshio  Mie University school of medicine Department of molecular and cellular pharmacology:Professor, 医学部, 教授 (00135443)

Project Period (FY) 1990 – 1992
KeywordsCalcium ion / S100 protein / Calcium binding protein / Calmodulin / Inhibitor / Cytoskeleton / Kidney / Beart
Research Abstract

An increase in intracellular calcium ion triggers a variety of cellular responses and injury.The calcium ion is mediated by various calcium-binding proteins. We purifier a new calcium-binding protein from porcine heart and kidney by caloium-dependent hydrophobic and dye-affinity chromatography. It was an apparent molecular weight of llkDa on SDS-PAGE. Sequence analysis of the cloned cDNA showed that the protein was composed of 99 amino acid residues and its molecular weight was estimated to be 11,179 and contained two calcium-binding domains of EF-hand motif and suggested that this protein represented a new member of the S100 protein family. Homologies to calpactin light chain,S100alpha and beta protein were 41.1%,40.9% and 37.5%, respectively, polyolonal antibodies were raised against S100C protein and used to determine the tissue and subcellular distribution of this molecule.The S100C protein is expressed at high levels in porcine kidney and lung,low levels in brain and liver,and intermediate levels in heart and adrenal gland. The LLC-PK1 cell line derived from porcine kidney was found to contain S100C,S100ao and S100L. Immunofluorescence microscopy indicated that these isoforms of S100 protein have a different distribution in these cells. The S100 protein family possesses many properties such as regulation of cell differentiation and cell cycle. We studied S100C protein expression in synchronized cultued LLC-PK1 cells. Peak expression of S100C protein was found in the Go phase of the cell cycle. S100C protein levels decrease during Go to G1 cell cycle transition,These data suggest that S100C protein is closely associated with cell cycle and cell proliferation.

  • Research Products

    (8 results)

All Other

All Publications (8 results)

  • [Publications] H.Masuok,M.Ito,T.Nakano,M.naka and T.Tanaka: "Effects of ruthenium red on activation of ca2+-dependent cyclic nucleotide phosphodiesterase" Biochem.Biophys.Res.Commun.169. 315-322 (1990)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] M.Naka,Y.Kureishi,Y.Muroga,K.Takahashi,M.Ito and T.Tanaka: "Modulation of smooth muscle calponin by protein kinase C and calmodulin." Biochem.Biophys.Res.Commun.171. 933-937 (1990)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] H.Ohta,T.Sasaki,M.Naka,C.Miyamato,Y.Furuichi and T.Tanaka: "Molecular cloning and expression of the cDNA coding for a new member of the S100 protein family from porcine cardiac muscle." FEBS Lett.295. 93-96 (1991)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] T.Sasaki,M.Naka,F.Nakamura and T.Tanaka: "Rutheium red ingibits the binding of calcium to calmodulin required for enzyme activation." J.Biol.Chem.267. 21518-21523 (1992)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] H.Masuoka,M.Ito,T.Nakano,M.Naka and T.Tanaka: "Effects of ruthenium red on activation of Ca2+-dependent cyclic nucleotide phosphodiesterase" Biochem.Biophys.Res.Commun. 169. 315-322 (1990)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] M.Naka,Y.Kureishi,Y.Muroga,K.Takahashi,M.Ito and T.Tanaka: "Modulation of smooth muscle calponin by protein kinase C and calmodulin." Biochem.Biophys.Res Commun. 171. 933-937 (1990)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] H.Ohta,T.Sasaki,M.Naka,C.Miyamoto,Y.Furuichi and T.Tanaka: "Molecular cloning and expression of the cDNA coding for a new member of the S100 protein family from porcine cardiac muscle." FEBS Lett. 295. 93-96 (1991)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] T.Sasaki,M.Naka,F.Nakamura and T.Tanaka: "Ruthenium red inhibits the binding of caloium to calmodulin required for enzyme activation." J.Biol.Chem. 267. 21518-21523 (1992)

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

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Published: 1994-03-24  

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