Human L-ficolin: plasma levels, sugar specificity, and assignment of its lectin activity to the fibrinogen-like (FBG) domain

被引:111
作者
Le, Y
Lee, SH
Kon, OL
Lu, J
机构
[1] Natl Univ Singapore, Clin Res Ctr 02 01, Natl Univ Med Inst, Singapore 119260, Singapore
[2] Natl Univ Singapore, Dept Pathol, Singapore 119260, Singapore
来源
FEBS LETTERS | 1998年 / 425卷 / 02期
关键词
ficolin; fibrinogen-like domain; collagen-like; lectin; collectin; Clq;
D O I
10.1016/S0014-5793(98)00267-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Ficolins are characterised by the presence of collagen-like and fibrinogen-like (FBG) sequences. Human L-ficolin is synthesised in the liver and secreted into blood circulation. In previous studies, it was shown to bind to N-acetyl-D-glucosamine (GlcNAc). In the present study, its detailed sugar specificity and binding site have been investigated. It was found to bind to GlcNAc and GalNAc (N-acetyl-D-galactosamine) while showing no significant affinity for the precursor sugars. The structure in these molecules which is recognised by L-ficolin has been deduced to include an amide (-CO-NH-) or similar group. L-Ficolin was digested with collagenase and the collagenase resistant FBG domain was shown to bind to GlcNAc. Its levels in adult and cord blood-derived human plasma were also determined and showed that adult plasma contains approximately three times more L-ficolin than that of newborn babies. (C) 1998 Federation of European Biochemical Societies.
引用
收藏
页码:367 / 370
页数:4
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