Anticoagulant, cationic protein (CAP) isolated from granulocytes: Endotoxin-binding property of CAP.:Endotoxin-binding property of CAP

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Prior incubation of endotoxin with cationic protein (CAP) from mouse bone marrow or spleen cells has been shown to inhibit some endotoxin activities such as tissue factor generation in spleen cells and lethality in mice.In this study, the binding mechanism of CAP isolated from rabbit granulocytes to endotoxin was investigated.1) CAP significantly prolonged the clotting time (prothrombin time) of human plasma in proportion to the amount of CAP added. 2) Binding of CAP to Reendotoxin was shown to form an insoluble complex since addition of CAP solution to Reendotoxin increased turbidity. 3) The binding of CAP to Re-endotoxin was optimal under the condition of low ionic strength. About 50% of the binding was inhibited by the addition of 200mM-NaCl. 4) The binding of CAP to Re-endotoxin or to lipid A was best expressed at pH 6.0 to 7.0. 5) Rapid increase of turbidity was observed in the mixture of CAP and Re-endotoxin or lipid A. 6) Binding of CAP to Re-endotoxin was reversible.These findings suggest that CAP binds to endotoxin through the ionic and hydrophobic bonds, and results in the inactivation of endotoxin. DIC manifestation in endotoxemia may be regulated by CAP.
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