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

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.

journal_name

Thromb Res

journal_title

Thrombosis research

authors

Beebe DP,Wood LL,Moos M

doi

10.1016/0049-3848(90)90136-z

subject

Has Abstract

pub_date

1990-07-15 00:00:00

pages

339-50

issue

2

eissn

0049-3848

issn

1879-2472

journal_volume

59

pub_type

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