Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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High-yield Expression and Characterization of Syndecan-4 Extracellular, Transmembrane and Cytoplasmic Domains

  • Choi, Sung-Sub (Department of Chemistry and Protein Research Center for Bio-Industry, Hankuk University of Foreign Studies) ;
  • Kim, Ji-Sun (Department of Chemistry and Protein Research Center for Bio-Industry, Hankuk University of Foreign Studies) ;
  • Song, Jooyoung (Department of Chemistry and Protein Research Center for Bio-Industry, Hankuk University of Foreign Studies) ;
  • Kim, Yongae (Department of Chemistry and Protein Research Center for Bio-Industry, Hankuk University of Foreign Studies)
  • Received : 2012.12.27
  • Accepted : 2013.01.21
  • Published : 2013.04.20
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Abstract

The syndecan family consists of four transmembrane heparan sulfate proteoglycans present in most cell types and each syndecan shares a common structure containing a heparan sulfate modified extracellular domain, a single transmembrane domain and a C-terminal cytoplasmic domain. To get a better understanding of the mechanism and function of syndecan-4 which is one of the syndecan family, it is crucial to investigate its three-dimensional structure. Unfortunately, it is difficult to prepare the peptide because it is membrane-bound protein that transverses the lipid bilayer of the cell membrane. Here, we optimize the expression, purification, and characterization of transmembrane, cytoplasmic and short extracellular domains of syndecan4 (syndecan-4 eTC). Syndecan-4 eTC was successfully obtained with high purity and yield from the M9 medium. The structural information of syndecan-4 eTC was investigated by MALDI-TOF mass (MS) spectrometry, circular dichroism (CD) spectroscopy, and nuclear magnetic resonance (NMR) spectroscopy. It was confirmed that syndecan-4 eTC had an ${\alpha}$-helical multimeric structure like transmembrane domain of syndecan-4 (syndecan-4 TM) in membrane environments.

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References

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