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Research Article Free access | 10.1172/JCI113790

Endothelial cell-mediated conversion of Glu-plasminogen to Lys-plasminogen. Further evidence for assembly of the fibrinolytic system on the endothelial cell surface.

K A Hajjar and R L Nachman

Department of Pediatrics, Cornell University Medical College, New York 10021.

Find articles by Hajjar, K. in: PubMed | Google Scholar

Department of Pediatrics, Cornell University Medical College, New York 10021.

Find articles by Nachman, R. in: PubMed | Google Scholar

Published November 1, 1988 - More info

Published in Volume 82, Issue 5 on November 1, 1988
J Clin Invest. 1988;82(5):1769–1778. https://doi.org/10.1172/JCI113790.
© 1988 The American Society for Clinical Investigation
Published November 1, 1988 - Version history
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Abstract

Lysine-plasminogen (Lys-PLG), the plasmin-modified form of native glutamic acid-plasminogen (Glu-PLG), displays enhanced binding affinity for fibrin and also enhanced activation by urokinase and tissue plasminogen activator. We previously demonstrated high-affinity, specific, and functional binding of Glu-PLG as well as tissue plasminogen activator to cultured human umbilical vein endothelial cells (HUVEC). In the present study, we demonstrate binding of Lys-PLG to HUVEC, as well as conversion of Glu-PLG to Lys-PLG at the cell surface. Binding of Lys-PLG to HUVEC was saturable, reversible, epsilon-aminocaproic acid-sensitive, and involved two saturable sites with Kd's of 142 pM and 120 nM, respectively. Upon incubation with Glu-PLG, HUVEC, as well as endothelium in situ, partially converted the ligand to a Lys-PLG-like species. Conversion by HUVEC was blocked by diisopropyl-fluorophosphate, but not by other serine protease inhibitors, including alpha 2-plasmin inhibitor. Eluates of intact umbilical cord vessels contained Lys-PLG by immunoblot analysis. Lys-PLG was also identified immunohistochemically on the endothelial surface of vessels from a variety of normal and inflamed tissues. Thus, endothelial cells appear to actively modify circulating Glu-PLG, bind Lys-PLG to their surface, and thus enhance the fibrinolytic potential of the blood vessel wall.

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