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DOI: 10.1055/s-0038-1661281
A Role for Pericellular Proteoglycan in the Binding of Thrombin or Antithrombin III by the Blood Vessel Endothelium? – The Effects of Proteoglycan-Degrading Enzymes and Glycosaminoglycan-Binding Proteins on 125I-Thrombin Binding by the Rabbit Thoracic Aorta In Vitro
Publication History
Received 16 October 1984
Accepted 15 January 1985
Publication Date:
18 July 2018 (online)
![](https://www.thieme-connect.de/media/10.1055-s-00035024/198502/lookinside/thumbnails/10-1055-s-0038-1661281-1.jpg)
Summary
Rabbit thoracic aorta segments were treated with either proteoglycan-degrading enzymes or with glycosaminoglycan- binding proteins to examine the nature of the endothelial and subendothelial binding sites of 125I-thrombin. Treatment (5-30 min) with enzymes (heparitinase, chondroitinases AC or ABC) caused a decrease in 125I-thrombin binding by the endothelium (30-70%) and by the subendothelial (intima-media) layer (20-50%); a low- specificity protease destroyed endothelial binding almost entirely and reduced binding to the subendothelium by approximately 60% over a similar period. Of the glycosaminoglycan-binding proteins, pretreatment of the aorta wall with protamine caused a 30% decrease in thrombin binding to the endothelium whereas lipoprotein lipase (present during 125I-thrombin uptake) decreased binding by up to 40%. Pretreatment with antithrombin III did not significantly affect binding of either 125I-thrombin or 125I-FPR-inactivated thrombin. In contrast to thrombin, 125I- antithrombin III was not readily uptaken by the aorta segments. These observations indicate that, whereas the minimal binding by 125I-antithrombin III probably does not involve endothelial proteoglycan, a strong case can be made for endothelial and subendothelial proteoglycan binding sites for thrombin..
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