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

FEBS Letters

Le, Y²  Kon, O.L²  Lu, J²  Lee, S.H¹ 

[1]Department of Pathology, National University of Singapore, 10 Kent Ridge Crescent, Singapore 119260, Singapore

[2]National University Medical Institute, Blk MD11, #02-01 Clinical Research Centre, National University of Singapore, 10 Kent Ridge Crescent, Singapore 119260, Singapore

关键词: Ficolin;    Fibrinogen-like domain;    Collagen-like;    Lectin;    Collectin;    C1q;    FBG;    fibrinogen β/γ C-terminal;    GlcNAc;    N-acetyl-d-glucosamine;    GalNAc;    N-acetyl-d-galactosamine;    CRD;    carbohydrate recognition domain;   

DOI  :  10.1016/S0014-5793(98)00267-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown