Mannose Binding Proteins in the Liver and Blood

  • John A. Summerfield
Part of the NATO ASI Series book series (NSSA, volume 113)


The survival of glycoproteins in the circulation is determined by the nature of the terminal non-reducing sugar on their oligosaccharides. Glycoproteins terminating in sialic acid have plasma half-lives measured in days whereas those terminating in other sugars are cleared rapidly from the blood (a few minutes) mainly by the liver. The first mechanism to be defined was the hepatocyte galactose receptor which mediated the clearance of galactose-terminated glycoproteins from the blood (Ashwell & Morell, 1974). Around this time, groups interested in enzyme replacement for lyso-somal storage disorders noted that various rat lysosomal enzymes (e.g. β -glucuronidase) administered intravenously were also rapidly cleared by the liver (Achord et al., 1977a; Stahl et al., 1976a,b; Schlesinger et al, 1976). Uptake was carbohydrate mediated since it was abolished by periodate treatment of the lysosomal enzymes. However in the case of lysosomal enzymes hepatic uptake was inhibited, not by galactose, but both by mannan (a mannose-terminated proteoglycan from yeast cell walls) and agalactoorosomucoid (N-acetylglucosamine-terminated) (Stahl et al., 1976c; Achord et al., 1977b). Thus this novel receptor (in this paper referred to as the mannose receptor) recognised glycoproteins terminating in two sugars, either mannose (Man) or N-acetylglucosamine (GlcNAc).


Kupffer Cell Lysosomal Enzyme Hepatic Uptake Mannose Receptor Sinusoidal Cell 
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Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • John A. Summerfield
    • 1
  1. 1.Department of MedicineRoyal Free Hospital School of MedicineLondonUK

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