ABSTRACT
<p><b>OBJECTIVE</b>To investigate the pro-angiogenic effects of several multiple myeloma (MM) cell line culture supernatants on human bone marrow endothelial cell (HBMEC) proliferation, migration, and capillary formation, and the anti-angiogenic effects of thalidomide.</p><p><b>METHODS</b>HBMEC was cultured in the presence of MM cell lines (IM9, XG1, U266 and MOLP-5) supernatants. Proliferation and migration of HBMEC were determined, capillary-like tubule formation of HBMEC was examined in fibrin and Matrigel. The inhibiting effect of thalidomide was investigated by adding it into myeloma cell line culture supernatants. Vascular endothelial growth factor (VEGF) was measured by ELISA.</p><p><b>RESULTS</b>(1) MM cell lines culture supernatants promoted HBMEC proliferation and migration. (2) In fibrin and Matrigel, capillary-like tubule network formation promoted by the supernatants. (3) All of these effects could be inhibited by thalidomide. (4) This effect was not related to VEGF in the supernatants.</p><p><b>CONCLUSIONS</b>MM cell line promote proliferation, migration and tubule formation by secreting VEGF or other several cytokines. Thalidomide can inhibit these effects.</p>
Subject(s)
Humans , Angiogenesis Inhibitors , Pharmacology , Bone Marrow , Cell Division , Cell Movement , Cells, Cultured , Culture Media, Conditioned , Chemistry , Pharmacology , Endothelial Growth Factors , Metabolism , Endothelium, Vascular , Cell Biology , Physiology , Enzyme-Linked Immunosorbent Assay , Intercellular Signaling Peptides and Proteins , Metabolism , Lymphokines , Metabolism , Multiple Myeloma , Pathology , Bodily Secretions , Neovascularization, Physiologic , Thalidomide , Pharmacology , Tumor Cells, Cultured , Vascular Endothelial Growth Factor A , Vascular Endothelial Growth FactorsABSTRACT
A new fibrinolytic enzyme, isolated from the haemolymph of Rhodnius prolixus Stal [Heteroptera, Reduviidae] has been disocovered. This enzyme does not act by activating plasminogen to plasmin. However the split products obtained with this new enzyme inhibit fibrin formation in normal plasma. This enzyme seems to act specifically on the proteins involved in blood coagulation. Its origin has induced us to name it prolixase