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Secretion of N-terminal domain of α-dystroglycan in cerebrospinal fluid

  • Fumiaki Saito
  • , Yuko Saito-Arai
  • , Ayami Nakamura-Okuma
  • , Miki Ikeda
  • , Hiroki Hagiwara
  • , Toshihiro Masaki
  • , Teruo Shimizu
  • , Kiichiro Matsumura
  • Teikyo University
  • Teikyo University of Science

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

Abstract

α-Dystroglycan (α-DG) plays crucial roles in maintaining the stability of cells. We demonstrated previously that the N-terminal domain of α-DG (α-DG-N) is secreted by cultured cells into the culture medium. In the present study, to clarify its function in vivo, we generated a monoclonal antibody against α-DG-N and investigated the secretion of α-DG-N in human cerebrospinal fluid (CSF). Interestingly, we found that a considerable amount of α-DG-N was present in CSF α-DG-N in CSF was a sialylated glycoprotein with both N- and O-linked glycan. These observations suggest that secreted α-DG-N may be transported via CSF and have yet unidentified effects on the nervous system.

Original languageEnglish
Pages (from-to)365-369
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume411
Issue number2
DOIs
StatePublished - 29 Jul 2011

Keywords

  • Cerebrospinal fluid
  • Dystroglycan
  • Glycosylation
  • Muscular dystrophy
  • Processing of protein
  • Proprotein convertase

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