Antithrombin III-/J Associates More Readily Than Antithrombin Ill-or With Uninjured and De-endothelialized Aortic Wall In Vitro and In Vivo

نویسندگان

  • Michael R. Witmer
  • Mark W.C. Hatton
چکیده

The properties of two isoforms, or and fi, of rabbit antithrombin III (ATIII) were compared in the presence of undamaged or de-endothelialized rabbit aortic wall. Similar quantities of ATIII-tt and ATUI-fi bound to and rapidly saturated the endothelium in vitro, but the rate of transendothelial passage of ATIII-/3 exceeded that of ATIII-a by 22%. Furthermore, ATIII-0 was adsorbed approximately twice as rapidly as ATlII-a by the subendothelium of the de-endothelialized aorta. Binding of both isoforms was decreased (ATIII-/3 more than Al'lU-or) by pretreating the subendothelial surface with heparitinase. Also, subendothelium-bound ATIII-/J was desorbed more readily than bound ATlII-aby thrombin. In vivo, the rate of uptake of iodine-131-labeled ATI1I-/3 from the circulation by the aortic wall and the major organs was 30-50% faster than that of iodine-125-labeled ATIII-o: In contrast, the uptake of I-ATIII-0 by the de-endothelialized aorta in vivo was three times faster than that of '"I-ATlII-a. By these criteria, ATIII-^ is the more active of the two isoforms. We surmise that plasma and, consequently, vessel wall levels of ATIII-/3 may be vital for controlling thrombogenic events caused by injury to the vascular wall. (Arteriosclerosis and Thrombosis 1991;ll:530-539)

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

On the Interaction of Rabbit Antithrombin Ill With the Luminal Surface of the Normal and Deendothelialized Rabbit Thoracic Aorta In Vitro

Pure rabbit antithrombin Ill was isotope labeled (with 125I or 3H by two different methods; neither procedure caused a loss of antithrombin activity although both methods affected the affinity of the protein for Sepharose-heparin. From segments from freshly excised rabbit aorta, the uptake of isotope-labeled antithrombin Ill by the endothehum was rapid and saturable, although relatively small c...

متن کامل

Familial thrombosis due to antithrombin 3 deficiency.

A large kindred from eastern Kentucky, with extensive history of recurrent venous thrombasis and pulmonary embolism, was studied. Low antithrombin III titers, ranging from 26% to 49% of normal values, were found in plasma of nine members in three consecutive generations; another five members, four of whom were not available for study, are suspected of having the biochemical defect. There was a ...

متن کامل

On the interaction of rabbit antithrombin III with the luminal surface of the normal and deendothelialized rabbit thoracic aorta in vitro.

Pure rabbit antithrombin III was isotope labeled (with 125I or 3H) by two different methods; neither procedure caused a loss of antithrombin activity although both methods affected the affinity of the protein for Sepharose-heparin. From segments from freshly excised rabbit aorta, the uptake of isotope-labeled antithrombin III by the endothelium was rapid and saturable, although relatively small...

متن کامل

Formation of the antithrombin heterodimer in vivo and the onset of thrombosis.

Antithrombin is shown to undergo a slow spontaneous conversion to its inactive latent conformation with readily discernible amounts present in plasma on incubation at 37 degrees C for 72 hours. More rapid conversion occurs on incubation of isolated antithrombin at 41 degrees C or 50 degrees C, but the appearance on electrophoresis of free latent antithrombin is preceded by the formation, in rec...

متن کامل

Histidine-rich glycoprotein does not interfere with interactions between antithrombin III and heparin-like compounds on vascular endothelial cells.

The role of histidine-rich glycoprotein in controlling heparin-like compounds on the endothelial cell surface is still unclear. The effects of this heparin-neutralizing protein on the interaction between antithrombin III and cultured porcine aortic endothelial cells were examined. Displacement of 125I-labeled antithrombin III specifically bound to endothelial cells by unlabeled histidine-rich g...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2005