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The immunoglobulin is a glycoprotein consisting of heavy and light chains on which the carbohydrate chains are located, normally in the heavy chain constant region. Although immunoglobulin light chains usually lack carbohydrates, some light chains contain carbohydrate chains in their variable region. In this mini review we will discuss the structure, role and modification of carbohydrates on immunoglobulin light chains. We have found an N-glycosylated carbohydrate chain on the light chain-hypervariable region of a human monoclonal antibody which is reactive to lung adenocarcinoma and is produced by a human hybridoma. A carbohydrate chain linked to one of the light chain glycoforms is characterized as hybrid-type, which is rare for any immunoglobulin isotype. To clarify the role of carbohydrates in the light chain variable region, we attempted to modify the glycosylation on this particular light chain. Carbohydrate moiety changes on this light chain produced in concanavalin A-resistant hybridoma clones and the following treatment of these variant light chains with various glycosidases leads to an alteration in the antigen binding activity. To modify the antigen-binding activity of the antibody by altering glycosylation on the light chain, we examined the effects of varying availability of glucose and other monosaccharides in the culture medium. Appropriate Nglycosylation on the light chain, which leads to higher antigenbinding, can be accomplished by modulating monosaccharide availability in the culture medium. Cell clones lacking sensitivity to a glucose level change for light chain glycosylation were screened from the lectin-resistant variants to obtain clones which produce glycoforms reproducibly in various culture environments. A. Introduction Immunoglobulin molecules are glycoproteins of which the carbohydrates are usually located in the constant regions of their heavy chain (1). Such carbohydrates have been indicated to be of significant importance for complement activation and secretion of immunoglobulin molecules (2, 3). Studies on a large number of human myeloma proteins have revealed that 要 約 免疫グロブリンは重鎖及び軽鎖からなる糖 タンパク質であ り、その糖鎖は重鎖の定常領域に存在 している。通常、軽鎖には 糖鎖は存在しないが、なかにはその可変領域に糖鎖が結合 してい るものがある。本総説では免疫グロブリン軽鎖に結合した糖鎖の 構造、機能及びその改変について述べる。我々はそうした軽鎖を ハイブリドーマの産生するヒトモノクローナル抗体の中に見いだ した。この抗体は肺腺がんと反応 し、その軽鎖の超可変領域に糖 鎖が結合 していた。この軽鎖のグリコフオームの一つに、ヒト免 疫グロブリンでは稀なハイブリッド型糖鎖が結合 していた。こう した可変領域に結合した糖鎖の役割を明らかにするために、軽鎖 に結合する糖鎖の修飾を試みた。コンカナバリンA耐 性ハイブリ ドーマで産生された軽鎖の糖鎖変異、およびそのグリコシダーゼ 処理は、抗体の抗原結合性に変化をもたらした。軽鎖の糖鎖を改 変することで、抗体の抗原結合性を修飾すべ く、培地中のグル コース利用性の影響を検討 した。ハイブリドーマの培地中での単 糖利用性を制御することで、産生抗体の抗原結合性が増大した。 、動物細胞による糖タンパク質の糖鎖修飾はその培養環境の 影響を受けるので、その糖 タンパク質糖鎖の正真性、均一性を維 持することは特に重要である。軽鎖の糖鎖修飾において培地中の グルコースレベルの変動に寛容な細胞株 をレクチン耐性変異細胞

Structure and Role of Oligosaccharide on Antibody Light Chains and Their Modification with Glycosylation-based Cytotechnology.