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Article Dans Une Revue Proceedings of the National Academy of Sciences of the United States of America Année : 1989

Specific binding of angiogenin to calf pulmonary artery endothelial cells

Résumé

Specific binding of angiogenin (ANG) to calf pulmonary artery endothelial cells was demonstrated. Cellular binding at 4TC of 125-Ilabeled human recombinant ANG was time and concentration dependent, reversible, and saturable in the presence of increasing amounts of the unlabeled molecules. The interaction was shown to be specific since a large excess of unlabeled ANG reduced labeled ANG binding by >80%, whereas similar doses of RNase A, a structurally related protein, had no effect. Scatchard analyses of binding data revealed two apparent components. High-affinity sites with an apparent dissociation constant of 5 x 10-9 M were shown to represent cell-specific interactions. The second component, comprising low-affinity/high-capacity sites with an apparent dissociation constant of 0.2 x 10-6 M, was essentially associated with pericellular components. High-affinity ANG binding sites varied with cell density and were found on other endo-thelial cells from bovine aorta, cornea, and adrenal cortex capillary but not on Chinese hamster lung fibroblasts. Divalent copper, a modulator of angiogenesis, was found to induce a severalfold increase in specific cell-bound radioactivity. Pla-cental ribonuclease inhibitor, a tight-binding inhibitor of both ribonucleolytic and angiogenic activities of ANG, abolished 1251-labeled human recombinant ANG binding only in the absence of copper.

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Biotechnologies
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hal-01880423 , version 1 (24-09-2018)

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  • HAL Id : hal-01880423 , version 1

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Josette Badet, Fabrice Soncin, Jean-Dominique Guitton, Olivier Lamare, Terence Cartwright, et al.. Specific binding of angiogenin to calf pulmonary artery endothelial cells. Proceedings of the National Academy of Sciences of the United States of America, 1989, 86, pp.8427 - 8431. ⟨hal-01880423⟩

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