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Characterization of mammalian synemin, an intermediate filament protein present in all four classes of muscle cells and some neuroglial cells: co-localization and interaction with type III intermediate filament proteins and keratins

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Abstract

Using a monoclonal antibody, we have detected a high molecular weight muscle protein, co-localized and co-isolating with desmin. Searching a human cDNA database with partial amino acid sequences of the protein, we found a cDNA clone encoding a 1565-amino-acid polypeptide, identified as a mammalian (human) synemin, a member of the intermediate filament (IF) protein family. Immunoblotting showed the presence of a 180-kDa polypeptide in skeletal muscle and 180- and 200-kDa polypeptides in cardiac and smooth muscles. Interestingly, synemin was also found in myoepithelial cells, which have keratin filaments instead of desmin. Moreover, synemin was also found in astrocytes of optic nerves and non-myelin-forming Schwann cells, together with glial fibrillary acidic protein (GFAP) and vimentin. Blot overlays pointed to molecular interactions of synemin with desmin, vimentin, GFAP and keratin 5 and 6, but not with keratin 14. The experimental data also suggested a possible link with nebulin, a skeletal muscle protein. Purified synemin was coassembled with desmin in different molar ratios, and at 1:25, as typically found in vivo, IFs were formed which were comparable in length to desmin filaments. However, at molar ratios of 3:25 and 6:25, much shorter and irregular shaped filamentous polymers were generated. The fact that synemin is present in all four classes of muscle cells and a specific type of glial cells is indicative of important functions. Its incorporation may give structural and functional versatility to the IF cytoskeleton.

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Acknowledgements

We thank Dr. R. Kamiya (School of Science, University of Tokyo, Tokyo, Japan) and Dr. A. Kusumi (School of Science, Nagoya University, Nagoya, Japan) for their encouragement.

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Authors and Affiliations

  1. Unit of Biosystems, Graduate School of Human Informatics, Nagoya University, Nagoya, Japan

    Yoshiaki Hirako, Yuki Tsujimura, Masayo Okumura & Katsushi Owaribe

  2. Department of Human Gene Research, Kazusa DNA Research Institute, Kisarazu, Chiba, Japan

    Hisashi Yamakawa & Osamu Ohara

  3. Department of Anatomy, School of Medicine , Nagoya University, Nagoya, Japan

    Yuji Nishizawa & Jiro Usukura

  4. Department of Biochemistry and Molecular Biology, Health Sciences Center, The University of Oklahoma, Oklahoma City, Oklahoma, USA

    Hiroyuki Matsumoto

  5. The Molecular Biology Resource Facility, Health Sciences Center, The University of Oklahoma, Oklahoma City, Oklahoma, USA

    Kenneth W. Jackson

  6. Department of Dermatology, University of Würzburg, Josef-Schneider-Strasse 2, 97080, Würzburg, Germany

    Yoshiaki Hirako

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  1. Yoshiaki Hirako
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  2. Hisashi Yamakawa
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  10. Osamu Ohara
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Correspondence to Yoshiaki Hirako.

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This work was supported by grants from the Ministry of Education, Science, and Culture of Japan.

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Hirako, Y., Yamakawa, H., Tsujimura, Y. et al. Characterization of mammalian synemin, an intermediate filament protein present in all four classes of muscle cells and some neuroglial cells: co-localization and interaction with type III intermediate filament proteins and keratins. Cell Tissue Res 313, 195–207 (2003). https://doi.org/10.1007/s00441-003-0732-2

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  • DOI: https://doi.org/10.1007/s00441-003-0732-2

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