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

FEBS Lett. 1998 Mar 27;425(2):367-70. doi: 10.1016/s0014-5793(98)00267-1.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Animals
  • Binding Sites
  • Carbohydrate Metabolism*
  • Carrier Proteins / blood
  • Carrier Proteins / chemistry
  • Carrier Proteins / metabolism*
  • Fibrinogen / chemistry*
  • Humans
  • Lectins / metabolism*
  • Molecular Structure
  • Rabbits

Substances

  • Carrier Proteins
  • Lectins
  • ficolin
  • Fibrinogen