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Departments of Pathology, and Microbiology and Immunology, Dalhousie University, Halifax, Nova Scotia, Canada
Mast cells accumulate in large numbers at angiogenic sites, where they have been shown to express a number of proangiogenic factors, including vascular endothelial growth factor (VEGF-A). PGE2 is known to strongly promote angiogenesis and is found in increased levels at sites of chronic inflammation and around solid tumors. The expression pattern of VEGF and the regulation of VEGF-A by PGE2 were examined in cord blood-derived human mast cells (CBMC). CBMC expressed mRNA for five isoforms of VEGF-A and other members of the VEGF family (VEGF-B, VEGF-C, and VEGF-D) with strong expression of the most potent secretory isoforms. PGE2 was a very strong inducer of VEGF-A121/165 production by CBMC and also elevated VEGF-A mRNA expression. The amount of VEGF-A121/165 protein production induced by PGE2 was 4-fold greater than that induced by IgE-mediated activation of CBMC. Moreover, the response to PGE2 as well as to other cAMP-elevating agents such as forskolin and salbutamol was observed under conditions that were not associated with mast cell degranulation. CBMC expressed substantial levels of the EP2 receptor, but not the EP4 receptor, when examined by flow cytometry. In contrast to other reported PGE2-mediated effects on mast cells, VEGF-A121/165 production occurred via activation of the EP2 receptor. These data suggest a role for human mast cells as a potent source of VEGF121/165 in the absence of degranulation, and may provide new opportunities to regulate angiogenesis at mast cell-rich sites.
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