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Blood, 15 April 2001, Vol. 97, No. 8, pp. 2342-2350
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Expression and colocalization of cytokeratin 1 and
urokinase plasminogen activator receptor on endothelial cells
Fakhri Mahdi,
Zia Shariat-Madar,
Robert F. Todd III,
Carlos D. Figueroa, and
Alvin H. Schmaier
From the Hematology and Oncology Division, Department
of Internal Medicine and Pathology, University of Michigan, Ann Arbor,
MI, and Institute of Histology and Pathology, Austral University,
Valdivia, Chile.
The cellular localization of human cytokeratin 1 (CK1), urokinase
plasminogen activator receptor (uPAR), and gC1qR, high-molecular-weight kininogen (HK)-binding proteins on endothelial cells, was determined. CK1 was found on the external membrane of nonpermeabilized endothelial cells by immunoperoxidase staining, immunofluorescence, and
transmission electron microscopy using immunogold. Human umbilical vein
endothelial cells (HUVECs) had 7.2 ± 0.2 × 104
specific CK1 membrane sites/cell by
125I-F(ab')2 anti-CK1 antibody binding. Flow
cytometry studies confirmed the presence of CK1, uPAR, and gC1qR on
HUVECs. On laser scanning confocal microscopy and transmission
electron microscopy, CK1 and uPAR, but not gC1qR, colocalized on the
cell surface of HUVECs. The HUVEC surface distribution of these
proteins was distinctly different from that for von Willebrand factor.
In competitive inhibition experiments, anti-CK1, anti-uPAR, or
anti-gC1qR blocked both biotin-HK binding and prekallikrein (PK)
activation on HUVECs with an inhibitory concentration of 50%
(IC50) of 300 to 350 nM, 50 to 60 nM, or 35 to 100 nM,
respectively. Also, antibodies to uPAR and gC1qR each inhibited 86% of
kallikrein-mediated, 2-chain urokinase plasminogen activation, whereas
antibodies to CK1 only inhibited 24% of plasminogen activation. On
HUVECs, CK1 and uPAR, but not gC1qR, colocalized to be a
multiprotein receptor complex for HK binding, PK activation, and
2-chain urokinase plasminogen activation.
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