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Prepublished online as a Blood First Edition Paper on May 15, 2003; DOI 10.1182/blood-2003-01-0166.
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Blood, 1 September 2003, Vol. 102, No. 5, pp. 1723-1731
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Regulation of plasminogen activation: a role for melanotransferrin (p97) in cell migration
Michel Demeule,
Yanick Bertrand,
Jonathan Michaud-Levesque,
Julie Jodoin,
Yannève Rolland,
Reinhard Gabathuler, and
Richard Béliveau
From the Laboratoire de Médecine Moléculaire, Centre
d'Hémato-Oncologie, Hôpital Ste-Justine-Université du
Québec à Montréal, Montréal, QC, Canada; and
Biomarin Pharmaceutical, Novato, CA.
We recently reported that human recombinant melanotransferrin (p97)
presents a high transport rate across the blood-brain barrier that might
involve the low-density lipoprotein receptor–related protein (LRP). We
now report new interactions between p97 and another LRP ligand, the urokinase
plasminogen activator (uPA) complex. By using biospecific interaction
analysis, both pro-uPA and plasminogen are shown to interact with immobilized
p97. Moreover, the activation of plasminogen by pro-uPA is increased by
soluble p97. Because the uPA system plays a crucial role in cell migration,
both in cancer and in angiogenesis, we also measured the impact of both
endogenous membrane-bound and exogenous p97 on cell migration. The monoclonal
antibody L235 (which recognizes a conformational epitope on p97) inhibited the
migration of human microvascular endothelial cells (HMECs-1) and of human
melanoma SK-MEL-28 cells, indicating that endogenous membrane-bound p97 could
be associated with this process. In addition, low concentrations of exogenous
p97 (10 and 100 nM) inhibited HMEC-1 and SK-MEL28 cell migration by more than
50%. These results indicate that membrane-bound and soluble p97 affect the
migration capacity of endothelial and melanoma cells and suggest that p97
could be involved in the regulation of plasminogen activation by interacting
with pro-uPA and plasminogen.
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