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J. Biol. Chem., Vol. 262, Issue 16, 7451-7454, Jun, 1987
K Ikeda, T Sannoh, N Kawasaki, T Kawasaki and I Yamashina
Serum mannan-binding protein (MBP), a lectin specific for mannose and N-
acetylglucosamine, was revealed to activate the complement system as
measured by passive hemolysis using sheep erythrocytes coated with yeast
mannan. In contrast, rat liver MBP, which shares many properties in common
with serum MBP, could not activate complement at all. The activation by
serum MBP was inhibited effectively by the presence of haptenic sugars and
dependent absolutely upon the presence of C4, indicating that the
activation is initiated by the sugar binding activity of MBP and proceeds
through the classical pathway. The 25 NH2- terminal amino acid sequence of
rat serum MBP determined in this study was completely matched with that of
MBP-A deduced from cDNA sequence by Drickamer et al. (Drickamer, K.,
Dordal, M. S., and Reynolds, L. (1986) J. Biol. Chem. 261, 6878-6887),
revealing that MBP-A is in fact identical with serum MBP. On the basis of
the knowledge of primary structures and physicochemical properties of rat
serum and liver MBPs, a possible mechanism of the complement activation by
serum MBP is discussed with reference to close similarity in the gross
structures of serum MBP and C1q.
Serum lectin with known structure activates complement through the classical pathway
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