1988
DOI: 10.1159/000463036
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Inhibition of Clq Functions by RHP, a Protein Elevated in Sera from Patients with Rheumatoid Arthritis

Abstract: We have previously shown that serum levels of Clq, unbound to Clr X Cls, are elevated in rheumatoid arthritis. We have also shown that RHP, a newly described serum protein which affects the Clq-anti Clq precipitin reaction, is also present at elevated levels in rheumatoid arthritis. We now show that RHP inhibits the hemolytic activity of Clq, disaggregates Cl, and inhibits the ability of Clq bound to latex beads or to aggregated IgG to enhance the oxidative metabolism of neutrophils.

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Cited by 5 publications
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“…The inhibitor, described as a 60 kDa glycoprotein, exerts its effect by binding to immunoglobulin and inhibits complement activation through an effect on C1 binding. Yet another protein, designated RHP, with a molecular weight of 135 kDa, has also been isolated and purified from rheumatoid sera [22]. It is capable of inhibiting haemolytic activity initiated via the classical pathway, but at present it is not known whether this protein has inhibitory activity.…”
Section: Discussionmentioning
confidence: 99%
“…The inhibitor, described as a 60 kDa glycoprotein, exerts its effect by binding to immunoglobulin and inhibits complement activation through an effect on C1 binding. Yet another protein, designated RHP, with a molecular weight of 135 kDa, has also been isolated and purified from rheumatoid sera [22]. It is capable of inhibiting haemolytic activity initiated via the classical pathway, but at present it is not known whether this protein has inhibitory activity.…”
Section: Discussionmentioning
confidence: 99%