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Inhibition by -Aminocaproic Acid of the Activation of the First Component of the Complement System¹

From the Departments of Dermatology and Medicine, Harvard Medical School, and the Division of Dermatology, Departments of Medicine, Peter Bent Brigham and Robert B. Brigham Hospitals, Boston, Massachusetts 02120

Abstract

The influence of EACA on C1 in whole human serum and on C1 and C as isolated molecules was assessed hemolytically. There was selective inhibition of C1 without effect on the levels of C4, C2, C3, and C9 in whole human serum that was reversed by dialysis. EACA was found to inhibit the intrinsic activation of C1 without inhibiting the already active molecule. This was confirmed by the capacity of trypsin to uncover C1 activity in cellular intermediates formed by C1 treated with EACA that did not evolve in the absence of this extrinsic activating mechanism. Inasmuch as the trypsin-dependent recovery of C1 was incomplete, an effect on binding cannot be excluded.

Footnotes

¹ This work was supported in part by Grants RR-05489, AI-07722, and AM-05577 from the National Institutes of Health.

² Dr. Soter is a Postgraduate Fellow of the Dermatology Foundation.

³ Dr. Gigli is the recipient of Research Career-Development Award AM-46409 from the National Institutes of Health.