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J Biol Chem, Vol. 275, Issue 20, 15541-15548, May 19, 2000
From the ** Hematology-Oncology Division, Case Western Reserve
University School of Medicine, Cleveland, Ohio 44106-4937, the
¶ Hematology-Oncology Division and the
§§ Department of Pediatrics, Weill Medical
College of Cornell University, New York, New York, and the
High Affinity Binding of
2-Glycoprotein I to Human
Endothelial Cells Is Mediated by Annexin II*
§,
,, Children's Hospital of Philadelphia,
Philadelphia, Pennsylvania
2-Glycoprotein I
(2GPI) is an abundant plasma phospholipid-binding
protein and an autoantigen in the antiphospholipid antibody syndrome.
Binding of 2GPI to endothelial cells targets them for activation by anti-2GPI antibodies, which circulate and
are associated with thrombosis in patients with the antiphospholipid
antibody syndrome. However, the binding of 2GPI to
endothelial cells has not been characterized and is assumed to result
from association of 2GPI with membrane phospholipid.
Here, we characterize the binding of 2GPI to endothelial
cells and identify the 2GPI binding site.
125I-2GPI bound with high affinity
(Kd ~18 nM) to human umbilical vein
endothelial cells (HUVECs). Using affinity purification, we isolated
2GPI-binding proteins of ~78 and ~36 kDa from HUVECs and EAHY.926 cells. Amino acid sequences of tryptic peptides from each
of these were identical to sequences within annexin II. A role for
annexin II in binding of 2GPI to cells was confirmed by
the observations that annexin II-transfected HEK 293 cells bound
~10-fold more 125I-2GPI than control cells
and that anti-annexin II antibodies inhibited the binding of
125I-2GPI to HUVECs by ~90%. Finally,
surface plasmon resonance studies revealed high affinity binding
between annexin II and 2GPI. These results demonstrate
that annexin II mediates the binding of 2GPI to
endothelial cells.
*
This work was supported by Grant HL50827, a grant from the
American Diabetes Foundation, and an Established Investigator Award from the American Heart Association (to K. R. M.). The W. M. Keck Biomedical Mass Spectrometry Laboratory, University of Virginia School
of Medicine, is funded by a grant from the W. M. Keck Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by Clinical Associate Physician Award M01RR00047
from the General Clinical Research Centers of the National Institutes of Health and a Junior Faculty Scholars Award from the American Society
of Hematology.
Recipient of a postdoctoral fellowship award from the Ohio
Valley Affiliate of the American Heart Association.
¶¶
To whom correspondence should be addressed:
Hematology-Oncology Division, BRB 3, Case Western Reserve Univ. School
of Medicine, 10900 Euclid Ave., Cleveland, Ohio 44106-4937. Tel.:
216-368-1175; Fax: 216-368-1166; E-mail: kxm71@po.cwru.edu.
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