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Glycobiology, 2002, Vol. 12, No. 8 507-515
© 2002 Oxford University Press

N-glycosylation profile of recombinant human soluble Fc{gamma} receptor III

Noriko Takahashi2, Joel Cohen-Solal3, Annie Galinha3, Wolf Herman Fridman3, Catherine Sautès-Fridman3 and Koichi Kato1,2

2 Graduate School of Pharmaceutical Sciences, Nagoya City University, Mizuho-ku, Nagoya 467-8603, Japan; and 3 INSERM Unité 255, Centre de Recherches Biomedicales des Cordeliers, 15 rue de I’Ecole de Medecine, 75270 Paris, France

N-glycans of human Fc{gamma} receptor III (Fc{gamma}R III) are believed to be involved in the interaction with complement receptor type 3 (CR3) (Sehgal et al. [1993] J. Immunol., 150, 4571–4580). Recombinant human soluble Fc{gamma}RIII (rhsFc{gamma}RIII), which is produced in baby hamster kidney (BHK) cells, has been shown to interact with CR3 in a manner similar to native Fc{gamma}RIII. We elucidated the N-glycosylation profiles of rhsFc{gamma}RIII by the 3D high-performance liquid chromatography mapping technique. It was revealed that the N-glycans of rhsFc{gamma}RIII are much more divergent (consisting of 20 neutral, 7 monosialyl, 4 disialyl, 5 trisialyl, and 1 tetrasialyl oligosaccharides) than those previously determined for BHK-expressed mouse sFc{gamma}RII, notwithstanding close structural similarity of polypeptide chains between the two sFc{gamma}Rs. Particularly, high-mannose type oligosaccharides are specifically expressed on rhsFc{gamma}RIII.

1 To whom correspondence should be addressed; E-mail: kkato@phar.nagoya-u.ac.jp


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