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Blood, 15 June 2002, Vol. 99, No. 12, pp. 4562-4567
NEOPLASIA
Tissue factor is the receptor for plasminogen type 1 on 1-LN
human prostate cancer cells
Mario Gonzalez-Gronow,
Govind Gawdi, and
Salvatore V. Pizzo
From the Department of Pathology, Duke University
Medical Center, Durham, NC.
Tissue factor (TF), the initiator of the extrinsic pathway of
coagulation, binds plasminogen (Pg) with high affinity through an
interaction between kringles 1-3 of Pg and the extracellular domain of
TF. We investigated the binding of Pg type 1 (Pg 1) and Pg type 2 (Pg
2) to highly invasive, TF-expressing, 1-LN human prostate tumor cells
and to TF isolated from 1-LN cell membranes. Pg 1, containing both
N-linked and O-linked oligosaccharide chains, bound to isolated TF with
high affinity, whereas Pg 2, containing only one O-linked
oligosaccharide chain, did not bind to TF. Although Pg 1 and Pg 2 bind
to 1-LN cells, only anti-TF antibodies inhibited the binding of Pg 1, suggesting that TF functions as the receptor for Pg 1 on 1-LN cells.
Binding of Pg 1 to isolated TF was inhibited by 6-aminohexanoic acid
and  -methylmannoside, suggesting that Pg 1 L-lysine
binding sites and the biantennary, mannose-containing N-linked
oligosaccharide chain are involved in this interaction. Binding of Pg 1 to 1-LN cells promoted activation by receptor-bound urinary-type Pg
activator (u-PA) and initiated a Ca++ signaling cascade. In
previous studies we demonstrated that the Pg 2 O-linked carbohydrate
chain is essential for its binding to CD26 on 1-LN cells. The current
studies suggest that Pg oligosaccharide chains regulate the binding of
Pg 1 and Pg 2 to separate receptors on the cell surface.
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