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The Low-Density Lipoprotein Receptor-Related Protein (LRP) Mediates
Clearance of Coagulation Factor Xa In Vivo
Masaaki Narita,
Amy E. Rudolph,
Joseph P. Miletich, and
Alan L. Schwartz
From the Edward Mallinckrodt Departments of Pediatrics, Molecular
Biology, and Pharmacology, and the Departments of Medicine and
Pathology at the Washington University School of Medicine, St Louis,
MO.
Blood coagulation factor X plays a pivotal role in the clotting
cascade. When administered intravenously to mice, the majority of
activated factor X (factor Xa) binds to  2-macroglobulin
(2M) and is rapidly cleared from the circulation into
liver. We show here that the low-density lipoprotein receptor-related
protein (LRP) is responsible for factor Xa catabolism in vivo. Mice
overexpressing a 39-kD receptor-associated protein that binds to LRP
and inhibits its ligand binding activity displayed dramatically
prolonged plasma clearance of 125I-factor Xa.
Preadministration of 2M-proteinase complexes
(2M*) also diminished the plasma clearance of
125I-factor Xa in a dose-dependent fashion. The clearance
of preformed complexes of 125I-factor Xa and
2M was similar to that of 125I-factor Xa
alone and was also inhibited by mice overexpressing a 39-kD
receptor-associated protein. These results thus suggest that, in vivo,
factor Xa is metabolized via LRP after complex formation with
2M.
Blood, Vol. 91 No. 2 (January 15), 1998:
pp. 555-560
© 1998 by The American Society of Hematology.
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