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Am J Physiol Lung Cell Mol Physiol 259: L270-L275, 1990;
1040-0605/90 $5.00
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AJP - Lung Cellular and Molecular Physiology, Vol 259, Issue 4 270-L275, Copyright © 1990 by American Physiological Society

ARTICLES

Enzymatic activity is necessary for thrombin-mediated increase in endothelial permeability

J. L. Aschner, J. M. Lennon, J. W. Fenton 2nd, M. Aschner and A. B. Malik
Department of Pediatrics, Albany Medical Center, New York 12208.

alpha-Thrombin causes a dose-dependent increase in endothelial permeability as measured by the clearance rate of 125I-albumin across a monolayer of bovine pulmonary artery endothelial cells. We determined if an active catalytic site is necessary for the thrombin-mediated increase in endothelial permeability. alpha-Thrombin was reacted with 10-fold excess D-phenylalanyl-prolyl-arginine chloromethyl ketone (PPACK), an irreversible inhibitor that forms a covalent bond with thrombin's active site, producing an enzymatically inactive thrombin. PPACK completely inhibited the alpha-thrombin-mediated increase in 125I-albumin permeability. Similar results were obtained with gamma-thrombin, an enzymatically active alpha-thrombin form with an altered fibrinogen recognition domain. PPACK alone and the active site-inhibited PPACK-alpha-thrombin had no effect on permeability. Diisopropylphospho (DIP)-alpha-thrombin was effective only in very high concentrations (10(-6)M), and this effect was abolished by the addition of PPACK. These studies demonstrate that binding alone is insufficient for the thrombin-mediated increase in endothelial monolayer permeability. Thrombin's active catalytic site is a requirement for the increase in transendothelial albumin permeability.


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