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Endocrinology, Vol 137, 3871-3876, Copyright © 1996 by Endocrine Society

ARTICLES

The insulin-like growth factor II/mannose 6-phosphate receptor is required for proliferin-induced angiogenesis

O Volpert, D Jackson, N Bouck and DI Linzer
Department of Microbiology-Immunology, Northwestern University Medical School, Chicago, Illinois 60611, USA. Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA.

Proliferin stimulates endothelial cell migration in culture and neovascularization in vivo. Previous studies have demonstrated that proliferin can bind to the insulin-like growth factor II/mannose 6- phosphate receptor, and that binding can be blocked by mannose 6- phosphate. We have now found that this receptor plays an essential role in proliferin-induced angiogenesis. Proliferin binding to endothelial cells is blocked by the addition of mannose 6-phosphate, as is the ability of both recombinant and placental-derived proliferin to stimulate the migration of capillary endothelial cells in vitro and to induce neovascularization in the rat cornea. Consistent with a direct role of this receptor in angiogenesis, insulin-like growth factor II, as well as a mutant form of insulin-like growth factor II that binds to the insulin-like growth factor II/mannose 6-phosphate receptor but not to the insulin-like growth factor I receptor, also stimulate endothelial cell migration and neovascularization.


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