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J. Biol. Chem., Vol. 268, Issue 29, 22046-22054, Oct, 1993
I Warshawsky, G Bu and AL Schwartz
The low density lipoprotein receptor-related protein/alpha 2- macroglobulin
receptor (LRP/alpha 2MR) binds and internalizes several plasma proteins
including tissue-type plasminogen activator (t-PA) and alpha
2-macroglobulin-protease complexes (alpha 2M*). A 39-kDa protein that
copurifies with LRP/alpha 2MR inhibits the binding and uptake of ligands by
LRP/alpha 2MR, including t-PA and alpha 2M*. To define domains on the
39-kDa protein which are essential for inhibition of t- PA and alpha 2M*
binding to LRP/alpha 2MR, we have generated bacterial expression constructs
encoding discrete regions of the 39-kDa protein as fusion proteins with
glutathione S-transferase. Inhibition of t-PA and alpha 2M* binding to
LRP/alpha 2MR on rat hepatoma MH1C1 cells are shown to require amino acid
residues 18-24 and 100-107 on the 39-kDa protein. Inhibition of t-PA but
not alpha 2M* binding to LRP/alpha 2MR is also mediated by residues 200-225
and 311-319. The same 39-kDa protein constructs that inhibit alpha 2M* and
t-PA binding to MH1C1 cells are able to bind directly to purified LRP/alpha
2MR immobilized on nitrocellulose. Thus, our studies demonstrate several
specific regions on the 39-kDa protein which are required for the
inhibition of t-PA and alpha 2M* binding to LRP/alpha 2MR.
Identification of domains on the 39-kDa protein that inhibit the binding of ligands to the low density lipoprotein receptor-related protein
Edward Mallinckrodt Department of Pediatrics, Washington University School of Medicine, St. Louis, Missouri 63110.
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