N-glycosylation profile of recombinant human soluble Fc receptor III
| Autor: | Joel Cohen-Solal, Catherine Sautès-Fridman, Annie Galinha, Noriko Takahashi, Wolf H. Fridman, Koichi Kato |
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| Rok vydání: | 2002 |
| Předmět: |
Glycosylation
Structural similarity Receptors IgG Complement receptor Biology Biochemistry Molecular biology Recombinant Proteins Cell Line law.invention Mice Solubility N-linked glycosylation Polysaccharides law Cricetinae Recombinant DNA Baby hamster kidney cell Animals Humans Receptor Chromatography High Pressure Liquid |
| Zdroj: | Glycobiology. 12:507-515 |
| ISSN: | 1460-2423 0959-6658 |
| DOI: | 10.1093/glycob/cwf063 |
| Popis: | N-glycans of human Fcgamma receptor III (FcgammaR 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 FcgammaRIII (rhsFcgammaRIII), which is produced in baby hamster kidney (BHK) cells, has been shown to interact with CR3 in a manner similar to native FcgammaRIII. We elucidated the N-glycosylation profiles of rhsFcgammaRIII by the 3D high-performance liquid chromatography mapping technique. It was revealed that the N-glycans of rhsFcgammaRIII 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 sFcgammaRII, notwithstanding close structural similarity of polypeptide chains between the two sFcgammaRs. Particularly, high-mannose type oligosaccharides are specifically expressed on rhsFcgammaRIII. |
| Databáze: | OpenAIRE |
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