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2005 Fiscal Year Final Research Report Summary

Research on Dysferlin interacting proteins

Research Project

Project/Area Number 15590924
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Neurology
Research InstitutionNational Institute of Advanced Industrial Science and Technology

Principal Investigator

MATSUDA Chie  National Institute of Advanced Industrial Science and Technology, Neuroscience research Institute, Senior researcher, 脳神経情報研究部門, 主任研究員 (50344099)

Project Period (FY) 2003 – 2005
KeywordsDysferlin / Dystrophy / Affixin
Research Abstract

The dysferlin gene is defective in Miyoshi myopathy (MM) and limb girdle muscular dystrophy type 2B (LGMD2B). Dysferlin is a sarcolemmal protein that is implicated in calcium-dependent membrane repair. Affixin (beta-parvin) is a novel, integrin-linked kinase-binding protein that is involved in the linkage between integrin and the cytoskeleton. Here we show that affixin is a dysferlin binding protein that colocalizes with dysferlin at the sarcolemma of normal human skeletal muscle. The immunoreactivity of affixin was reduced in sarcolemma of MM and LGMD2B muscles, although the total amount of the affixin protein was normal. Altered immunoreactivity of affixin was also observed in other muscle diseases including LGMD1C, where both affixin and dysferlin showed quite similar changes with a reduction of sarcolemmal staining with or without cytoplasmic accumulations. Colocalization of dysferlin and affixin was confirmed by immunofluorescence analysis using dysferlin-expressing C2 myoblasts. Wild-type and mutant dysferlin colocalized with endogenous affixin. The interaction of dysferlin and affixin was confirmed by immunoprecipitation study using normal human and mouse skeletal muscles. Using immunoprecipitation with deletion mutants of dysferlin, we have identified that C-terminal region of dysferlin is an apparent binding site for affixin. We also found N-terminal calponin homology domain of affixin as a binding site for dysferlin. Our results suggest that affixin may participate in membrane repair with dysferlin

  • Research Products

    (4 results)

All 2006 2005

All Journal Article (4 results)

  • [Journal Article] The gamma-parvin-integrin-linked kinase complex is critically involved in leukocyte-substrate interaction.2006

    • Author(s)
      Yoshimi, R. et al.
    • Journal Title

      Journal of Immunology 176・6

      Pages: 3611-3624

    • Description
      「研究成果報告書概要(和文)」より
  • [Journal Article] The gamma-parvin-integrin-linked kinase complex is critically involved in leukocyte-substrate interaction.2006

    • Author(s)
      Yoshimi R, Yamaji S, Suzuki A, Mishima W, Okamura M, Obana T, Matsuda C, Miwa Y, Ohno S, Ishigatsubo Y.
    • Journal Title

      J Immunol. 176(6)

      Pages: 3611-3624

    • Description
      「研究成果報告書概要(欧文)」より
  • [Journal Article] Dysferlin interacts with affixin (β-parvin) at the salcolemma.2005

    • Author(s)
      Matuda, C. et al.
    • Journal Title

      Journal of Neuropathology and Experimental Neurology 64・4

      Pages: 334-340

    • Description
      「研究成果報告書概要(和文)」より
  • [Journal Article] Dysferlin interacts with affixin (beta-parvin) at the sarcolemma.2005

    • Author(s)
      Matsuda C, Kameyama K, Tagawa K, Ogawa M, Suzuki A, Yamaji S, Okamoto H, Nishino I, Hayashi YK.
    • Journal Title

      J.Neuropathol.Exp.Neurol. 64(4)

      Pages: 334-340

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

URL: 

Published: 2007-12-13  

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