N-Glycoform-dependent interactions of megalin with its ligands

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• 作者：Makoto Hirano^a ; ^b ; ¹ ; ^{mhirano@st.seikei.ac.jp} ; Kiichiro Totani^b ; Tomohiko Fukuda^c ; Jianguo Gu^c ; Akemi Suzuki^a ; ^c ; ²
• 关键词：DBP ; vitamin D-binding protein ; Fut8 ; α1 ; 6-fucosyltransferase ; JCGGDB ; Japan Consortium for Glycobiology and Glycotechnology Database ; Kan ; kanamycin ; LCA ; Lens culinaris agglutinin ; LRP ; LDL receptor-related protein ; MAS ; Matsunami Adhesive Silane ; NP-40 ; Nonidet P-40 ; OCT ; optimal cutting temperature ; PCTs ; proximal convoluted tubules ; PFA ; paraformaldehyde ; PNGase F ; peptide-N-glycanase F ; PSTs ; proximal straight tubules ; RAP ; receptor-associated protein ; RBP ; retinol-binding protein ; RBP-Cy5
• 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：1861
• 期：1
• 页码：3106-3118
• 全文大小：2413 K
• 卷排序：1861

文摘

Segment-specific N-glycoforms of megalin exist in a nephron. Megalin glycoforms exhibit different ligand-binding activities. Lack of core-fucose reduces the binding activity to retinol-binding protein. N-Glycosylation of megalin modulates the ligand-binding capacity.