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A linear amino acid sequence involved in the interaction of t-PA with its
endothelial cell receptor
DP Beebe, LA Miles and EF Plow
Center for Drugs and Biologics Evaluation and Research, Food and Drug
Administration, Bethesda, MD.
Endothelial cell receptors for tissue plasminogen activator (t-PA) have
been demonstrated recently, and we have sought to identify a region of the
t-PA molecule involved in its interaction with these receptors on human
umbilical vein endothelial cells. Of three monoclonal antibodies against
various regions of t-PA, one directed against the finger region inhibited
125I-t-PA binding to the cells. Synthetic peptides corresponding in amino
acid sequences to segments from within the finger region were constructed,
and one of these inhibited t-PA binding. This peptide corresponded to
residues 7 through 17 of t-PA. The inhibition by this peptide was specific
as other peptides from the finger region were inactive. The inhibitory
peptide also did not affect the binding of another fibrinolytic ligand,
urokinase, to the cells. Although a role for other regions of t-PA in
binding to endothelial cells cannot be excluded, the results implicate a
short span of linear amino acid sequence within the finger region in the
interaction of t-PA with endothelial cells.
Volume 74,
Issue 6,
pp. 2034-2037,
11/01/1989
Copyright © 1989 by The American Society of Hematology
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