title: Inhibition of the classical and alternative pathways by amino acids and their derivatives.
abstract: Effects of various aminoacids and their derivatives on the classical pathway and alternative pathway of the complement were studied. Leupeptin, acetyl-leucyl-leucyl-arginal, inhibited CH50 and Cl-esterase, but did not inhibit the alternative pathway. When aminoacids of carbon chains of the order of seven were used, arginine and lysine had stronger effects than trans-aminomethyl cyclohexane carboxylic acid (t-AMCHA), cis-aminomethyl cyclohexane carboxylic acid (cis-AMCHA) and epsilon aminocaproic acid (EACA). SH-compounds, cysteine, homocysteine and glutathione, had the strongest inhibitory effects among these aminoacids on both classical and alternative pathways. When effects on Cl esterase were compared, arginine, lysine, t-AMCHA, cis-AMCHA and EACA had weak inhibition while SH-compounds showed strong inhibition. Poly-L-lysine, which had extremely strong inhibition of CH50, had no inhibition of Cl esterase. The inhibitory effects of antifibrinolytic agents, EACA and t-AMCHA, were weak but when effects on early parts of the classical pathway, C(1,4,2)H50 were tested, some inhibitory activities were recognized. Thus inhibitory effects of these agents were due to their activities on the early parts of the classical pathway.
mesh_terms: D000596:Amino Acids / Q000494:pharmacology*; D015119:Aminocaproic Acid / Q000494:pharmacology; D003174:Complement C1 Inactivator Proteins; D003173:Complement C1s / Q000378:metabolism; D003169:Complement Inactivator Proteins; D006461:Hemolysis; D007976:Leupeptins / Q000494:pharmacology
chemical_list: D000596:Amino Acids; D003174:Complement C1 Inactivator Proteins; D003169:Complement Inactivator Proteins; D007976:Leupeptins; D003173:Complement C1s; D015119:Aminocaproic Acid