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Background  Immobilized recombinant perlecan domain I (PlnDI) binds and modulates the activity of heparin-binding growth factors,  in vitro . However, activities for PlnDI, in solution, have not been reported. In this study, we assessed the ability of soluble forms to modulate vascular endothelial growth factor-165 (VEGF 165 ) enhanced capillary tube-like formation, and VEGF receptor-2 phosphorylation of human bone marrow endothelial cells,  in vitro .    Results  In solution, PlnDI binds VEGF 165  in a heparan sulfate and pH dependent manner. Capillary tube-like formation is enhanced by exogenous PlnDI; however, PlnDI/VEGF 165  mixtures combine to enhance formation beyond that stimulated by either PlnDI or VEGF 165  alone. PlnDI also stimulates VEGF receptor-2 phosphorylation, and mixtures of PlnDI/VEGF 165  reduce the time required for peak VEGF receptor-2 phosphorylation (Tyr-951), and increase Akt phosphorylation. PlnDI binds both immobilized neuropilin-1 and VEGF receptor-2, but has a greater affinity for neuropilin-1. PlnDI binding to neuropilin-1, but not to VEGF receptor-2 is dependent upon the heparan sulfate chains adorning PlnDI. Interestingly, the presence of VEGF 165  but not VEGF 121  significantly enhances PlnDI binding to Neuropilin-1 and VEGF receptor-2.    Conclusions  Our observations suggest soluble forms of PlnDI are biologically active. Moreover, PlnDI heparan sulfate chains alone or together with VEGF 165  can enhance VEGFR-2 signaling and angiogenic events,  in vitro . We propose PlnDI liberated during basement membrane or extracellular matrix turnover may have similar activities,  in vivo .

Soluble perlecan domain i enhances vascular endothelial growth factor-165 activity and receptor phosphorylation in human bone marrow endothelial cells