Characterization of tissue plasminogen activator binding proteins isolated from endothelial cells and other cell types

Thrombosis Research
D P BeebeM Moos

Abstract

Human tissue plasminogen activator (t-PA) was shown to bind specifically to human osteosarcoma cells (HOS), and human epidermoid carcinoma cells (A-431 cells). Crosslinking studies with DTSSP demonstrated high molecular weight complexes (130,000) between 125I-t-PA and cell membrane protein on human umbilical vein endothelial cells (HUVEC), HOS, and A-431 cells. A 48-65,000 molecular weight complex was demonstrated after crosslinking t-PA peptide (res. 7-20) to cells. Ligand blotting of cell lysates which had been passed over a t-PA affinity column revealed binding of t-PA to 54,000 and 95,000 molecular weight proteins. Several t-PA binding proteins were identified in immunopurified cell lysates, including tubulin beta chain, plasminogen activator inhibitor type 1 and single chain urokinase.

Citations

Oct 5, 2010·Journal of Biomedicine & Biotechnology·Fatemeh DavamiFereidoun Mahboudi
Feb 18, 2010·Blood Coagulation & Fibrinolysis : an International Journal in Haemostasis and Thrombosis·Chikako IshidaOsamu Matsuo
Sep 1, 1991·Progress in Cardiovascular Diseases·J HenkinH C Yang
Jun 1, 1995·Baillière's Clinical Haematology·A Redlitz, E F Plow

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