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Blood, Vol. 92 No. 9 (November 1), 1998:
pp. 3277-3285
Three Complement-Type Repeats of the Low-Density Lipoprotein
Receptor-Related Protein Define a Common Binding Site for RAP,
PAI-1, and Lactoferrin
Brian Vash,
Neil Phung,
Sima Zein, and
Dianne DeCamp
The low-density lipoprotein receptor-related protein
(LRP) is a 600-kD scavenger receptor that binds a number
of protein ligands with high affinity. Although some ligands do not
compete with each other, binding of all is uniformly blocked by the
39-kD receptor-associated protein (RAP). RAP is normally found in the
endoplasmic reticulum and seems to function as a chaperone for LRP. To
identify the binding sites for RAP, lactoferrin, and plasminogen
activator inhibitor-1 (PAI-1), a bacterial expression system has been
developed to produce soluble LRP fragments spanning residues 783-1399. These residues overlap most of the CNBr fragment
containing the second cluster of complement-type repeats (C). Solid
phase binding assays show that 125I-RAP binds to fragments
containing three successive complement-type repeats: C5-C7. PAI-1 and
lactoferrin bind to the same fragments. A fragment containing C5-C7
also blocks uptake and degradation of 125I-RAP by
fibroblasts in a concentration-dependent manner. Binding competition
experiments show that RAP, PAI-1, and lactoferrin each inhibit the
binding of the others, suggesting that at this site in LRP, RAP acts as
a competitive, rather than an allosteric, inhibitor of PAI-1 and
lactoferrin binding.
© 1998 by The American Society of Hematology.
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