Characterization of the N-Oligosaccharides Attached to the Atypical Asn-X-Cys Sequence of Recombinant Human Epidermal Growth Factor Receptor.

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概要

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• The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGFinduced receptor activation. We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn32-X33-Cys34. The oligosaccharide structure at Asn32 is a mixture of the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide. Deletion of this atypical glycosylation site by replacement of Asn32 with lysine changed neither the expression nor function of the full length EGFR in CHO cells. The glycosylation at Asn32 in CHO sEGFR was incomplete: 20% of Asn32 remained unmodified. Thus, CHO sEGFR itself is heterogeneous with respect to the glycosylation at Asn32, which may cause problems in biophysical studies. An attempt to remove the oligosaccharide at Asn32 enzymatically did not succeed under nondenaturing conditions. Therefore, sEGFR with the mutation of Asn32→Lys32 is useful for biophysical and biochemical studies, and, particularly, for X-ray crystallography.

• 社団法人 日本生化学会の論文

著者

• Kohda Daisuke

  Department Of Molecular Physiology The Tokyo Metropolitan Institute Of Medical Science

• Kim Jae-hoon

  Yokoyama Cytologic Project Erato Japan Science And Technology Corporation

• Saito Kazuki

  Yokoyama Cytologic Project Erato Japan Science And Technology Corporation

• Sato Chiaki

  Department Of Public Health Faculty Of Veterinary Medicine Hokkaido University

• Yokoyama Shigeyuki

  Yokoyama Cytologic Project Erato Japan Science And Technology Corporation

• Abe Yoshito

  Department Of Archaeology Keio University

• Yokoyama Shigeyuki

  Yokoyama CytoLogic Project, ERATO, Japan Science and Technology Corporation, clo Tsuhuba Research Consortium

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