Binding of human angiogenin inhibits actin polymerization.

Binding of human angiogenin inhibits actin polymerization.
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DOI:
10.1016/j.abb.2009.12.024
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发表时间:
2010-03-01
影响因子:
3.9
通讯作者:
Kostyukova AS
Kostyukova AS
中科院分区:
生物学3区
文献类型:
--
作者:
Pyatibratov MG;Tolkatchev D;Plamondon J;Xu P;Ni F;Kostyukova AS

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Angiogenin is a potent inducer of angiogenesis, a process of blood vessel formation. It interacts with endothelial and other cells and elicits a wide range of cellular responses including migration, proliferation, and tube formation. One important target of angiogenin is endothelial cell-surface actin and their interaction might be one of essential steps in angiogenin-induced neovascularization. Based on earlier indications that angiogenin promotes actin polymerization, we studied the binding interactions between angiogenin and actin in a wide range of conditions. We showed that at subphysiological KCl concentrations, angiogenin does not promote, but instead inhibits polymerization by sequestering G-actin. At low KCl concentrations angiogenin induces formation of unstructured aggregates, which, as shown by NMR, may be caused by angiogenin's propensity to form oligomers. Binding of angiogenin to preformed F-actin does not cause depolymerization of actin filaments though it causes their stiffening. Binding of tropomyosin and angiogenin to F-actin is not competitive at concentrations sufficient for saturation of actin filaments. These observations suggest that angiogenin may cause changes in the cell cytoskeleton by inhibiting polymerization of G-actin and changing the physical properties of F-actin.
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