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Regulation of complement functional efficiency by histidine-rich
glycoprotein
NS Chang, RW Leu, JA Rummage, JK Anderson and JE Mole
Guthrie Research Institute, Sayre, PA 18840.
The modulation of complement functional efficiency by serum histidine- rich
glycoprotein (HRG) was investigated. Addition of exogenous HRG to prewarmed
diluted serum, followed immediately by sensitized sheep erythrocytes (EA),
resulted in enhanced hemolysis. However, when HRG was incubated with
diluted serum for 10 minutes at 37 degrees C, inhibition of hemolysis
occurred. The biphasic modulation of complement function was also obtained
with the complement alternative pathway when HRG was added to diluted serum
for hemolysis of rabbit erythrocytes. Partial reduction of complement
functional activity was shown when serum was absorbed by an HRG-Sepharose
6MB column. Western blot analysis showed that complement C8, C9, factor D,
and S-protein in diluted serum were bound by nylon membrane-immobilized
HRG. However, by immunoprecipitation of relatively undiluted serum with
anti-HRG IgG beads, HRG was found to coprecipitate with S-protein and
plasminogen, which suggested that HRG may complex with these proteins in
serum. In functional tests, HRG inhibited C8 hemolytic activity, probably
by preventing C8 binding to EAC1-7 cells. HRG also enhanced polymerization
of purified C9 as well as the generation of a 45-Kd C9 fragment. Such an
effect was even more pronounced in the presence of divalent cations with
the reaction mixtures of C9 and HRG. Partial dimerization of C9 was shown
when exogenous HRG was added to normal serum. In contrast, polymerization
of serum C9 was inhibited by exogenous HRG during poly I:C activation of
serum or incubation under low ionic strength conditions. HRG was further
shown to inhibit factor D-mediated cleavage of factor B when bound by cobra
venom factor. The molecular basis by which HRG regulates serum complement
function is not clear. Hypothetically, the tandem repetitions of a
consensus histidine-rich penta-peptide sequence in HRG may provide a highly
charged area that interacts with complement components.
Volume 79,
Issue 11,
pp. 2973-2980,
06/01/1992
Copyright © 1992 by The American Society of Hematology
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