N-glycosylation profile of recombinant human soluble Fcγ receptor III
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چکیده
N-glycans of human Fcγ receptor III (FcγR 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 FcγRIII (rhsFcγRIII), which is produced in baby hamster kidney (BHK) cells, has been shown to interact with CR3 in a manner similar to native FcγRIII. We elucidated the N-glycosylation profiles of rhsFcγRIII by the 3D high-performance liquid chromatography mapping technique. It was revealed that the N-glycans of rhsFcγRIII 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 sFcγRII, notwithstanding close structural similarity of polypeptide chains between the two sFcγRs. Particularly, high-mannose type oligosaccharides are specifically expressed on rhsFcγRIII.
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تاریخ انتشار 2002