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Arteriosclerosis, Thrombosis, and Vascular Biology. 1991;11:530-539

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Arteriosclerosis and Thrombosis, Vol 11, 530-539, Copyright © 1991 by American Heart Association

ARTICLES

Antithrombin III-beta associates more readily than antithrombin III- alpha with uninjured and de-endothelialized aortic wall in vitro and in vivo

MR Witmer and MW Hatton
Department of Pathology, McMaster University Health Sciences Centre, Hamilton, Ontario, Canada.

The properties of two isoforms, alpha and beta, of rabbit antithrombin III (ATIII) were compared in the presence of undamaged or de- endothelialized rabbit aortic wall. Similar quantities of ATIII-alpha and ATIII-beta bound to and rapidly saturated the endothelium in vitro, but the rate of transendothelial passage of ATIII-beta exceeded that of ATIII-alpha by 22%. Furthermore, ATIII-beta was adsorbed approximately twice as rapidly as ATIII-alpha by the subendothelium of the de- endothelialized aorta. Binding of both isoforms was decreased (ATIII- beta more than ATIII-alpha) by pretreating the subendothelial surface with heparitinase. Also, subendothelium-bound ATIII-beta was desorbed more readily than bound ATIII-alpha by thrombin. In vivo, the rate of uptake of iodine-131-labeled ATIII-beta from the circulation by the aortic wall and the major organs was 30-50% faster than that of iodine- 125-labeled ATIII-alpha. In contrast, the uptake of 131I-ATIII-beta by the de-endothelialized aorta in vivo was three times faster than that of 125I-ATIII-alpha. By these criteria, ATIII-beta is the more active of the two isoforms. We surmise that plasma and, consequently, vessel wall levels of ATIII-beta may be vital for controlling thrombogenic events caused by injury to the vascular wall.


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