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Tissue Factor-Dependent Vascular Endothelial Growth Factor
Production by Human Fibroblasts in Response to Activated Factor VII
Véronique Ollivier,
Stéphane Bentolila,
Jacques Chabbat,
Jacques Hakim, and
Dominique de Prost
From INSERM U479 and Service d'Hématologie et d'Immunologie,
CHU Xavier Bichat, Paris, France; and LFB Recherche et
Développement, Les Ulis, France.
The transmembrane protein tissue factor (TF) is the cell surface
receptor for coagulation factor VII (FVII) and activated factor VII
(FVIIa). Recently, TF has been identified as a regulator of
angiogenesis, tumor growth, and metastasis. This study was designed to
link the binding of FVII(a) to its receptor, TF, with the subsequent
triggering of angiogenesis through vascular endothelial growth factor
(VEGF) production by human lung fibroblasts. We report that incubation
of fibroblasts, which express constitutive surface TF, with FVII(a)
induces VEGF synthesis. FVII(a)-induced VEGF secretion, assessed by a
specific enzyme-linked immunosorbent assay, was time- and
concentration-dependent. VEGF secretion was maximal after 24 hours of
incubation of the cells with 100 nmol/L FVII(a) and represented a
threefold induction of the basal VEGF level. Reverse
transcriptase-polymerase chain reaction analysis of VEGF detected three
mRNA species of 180, 312, and 384 bp corresponding, respectively, to
VEGF121, VEGF165, and VEGF189. A
2.5- to 3.5-fold increase was observed for the 180- and 312-bp
transcripts at 12 and 24 hours, respectively. FVII(a)-dependent VEGF
production was inhibited by a pool of antibodies against TF, pointing
to the involvement of this receptor. On specific active-site inhibition with dansyl-glutamyl-glycinyl-arginyl chloromethyl ketone, FVIIa lost
70% of its capacity to elicit VEGF production. Consistent with this,
the native form (zymogen) of FVII only had a 1.8-fold stimulating
effect. Protein tyrosine kinase and protein kinase C are
involved in signal transduction leading to VEGF production, as shown by
the inhibitory effects of genistein and GF 109203X. The results of this
study indicate that TF is essential for VIIa-induced VEGF production by
human fibroblasts and that its role is mainly linked to the proteolytic
activity of the TF-VIIa complex.
Blood, Vol. 91 No. 8 (April 15), 1998:
pp. 2698-2703
© 1998 by The American Society of Hematology.
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