On the interaction of bovine seminal RNase with actin in vitro

Simm, Franz C.; Krietsch, Wolfgang K. G.; Isenberg, G.

doi:10.1111/j.1432-1033.1987.tb13482.x

Cited by 11 publications

(15 citation statements)

References 25 publications

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“…This region is relatively well conserved among the angiogenins from various species but differs markedly from the pancreatic RNases. It is notable that none of these RNases is angiogenic and only bovine seminal RNase, a dimeric protein with a number of unusual biological properties, has been reported to be an actin-binding protein, a property that is lost on monomerization (23).…”

Section: I25-labeled Actin Binds Other Angioge Factors Thementioning

confidence: 99%

Actin is a binding protein for angiogenin.

Strydom

Fett

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

123

127

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The 42-kDa angiogenin binding protein isolated previously has been purified to electrophoretic homogeneity. It has been identified as a member of the actin family by peptide mapping and partial amino acid sequencing. The interaction of bovine muscle actin with angiogenin is similar to that of the angiogenin binding protein. Angiogenin induces the polymerization of actin below the critical concentration for spontaneous polymerization. The interaction occurs both in solution and on a poly(vinylidene difluoride) membrane. It is inhibited by excess unlabeled angiogenin and also by platelet factor 4 and protamine, which are known inhibitors of angiogenesis. Two other angiogenic molecules, basic fibroblast growth factor and tumor necrosis factor a, bind to 125I-labeled actin and can be crosslinked by a water-soluble carbodilmide. Both actin and an anti-actin antibody inhibit the angiogenic activity of angiogenin in the chicken embryo chorioallantoic membrane assay. The results indicate that the angiogenin binding protein is a cell surface actin and suggest that the reaction between angiogenin and this actin is an essential step in the angiogenesis process induced by angiogenin.Angiogenin is a 14-kDa protein purified initially from serumfree supernatants of an established human adenocarcinoma cell line, HT-29 (1). It was the first human tumor-derived angiogenic protein to be isolated based on its in vivo activity. It stimulates endothelial cells to produce diacylglycerol (2) and secrete prostacyclin (3) by phospholipase activation. It supports endothelial and fibroblast cell adhesion (4) and modulates a mitogenic effect in certain cells (5). An angiogenin binding protein (AngBP), which has properties consistent with its being a component of a cellular receptor for angiogenin, has been identified and isolated from a transformed endothelial cell line, GM7373 (6). It is a cell-surface protein with an apparent molecular mass of 42 kDa and is released from endothelial cells by exposure to heparnn, heparan sulfate, or angiogenin itself.We report here the further purification and characterization of AngBP. Tryptic peptide mapping and amino acid sequence analysis indicate that AngBP is a member of the actin family. The binding of angiogenin to bovine muscle actin and the inhibitory effect of actin and anti-actin antibodies on angiogenin-induced neovascularization on the chicken embryo chorioallantoic membrane (CAM) are also reported. The mechanism by which AngBP is released from the cell surface and the physiological significance of its presence and displacement remain to be elucidated.

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Section: I25-labeled Actin Binds Other Angioge Factors Thementioning

confidence: 99%

Actin is a binding protein for angiogenin.

Strydom

Fett

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

123

127

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“…Our results thus suggest models where either all three proteins bind together or where eEF1A acts as an intermediate between the S-RNase and actin. It must be noted that several reports in the literature suggest a possible binding between actin and mammalian or fungal ribonucleases such as bovine seminal RNase [54], angiogenin [55] or ACTIBIND [56]. The nature of this binding is unclear, however, as the native structure and activity of at least the fungal enzyme is not required [56].…”

Section: Discussionmentioning

confidence: 99%

eEF1A Is an S-RNase Binding Factor in Self-Incompatible Solanum chacoense

et al. 2014

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Self-incompatibility (SI) is a genetic mechanism that allows flowering plants to identify and block fertilization by self-pollen. In the Solanaceae, SI is controlled by a multiallelic S-locus encoding both S-RNases and F-box proteins as female and male determinants, respectively. S-RNase activity is essential for pollen rejection, and a minimum threshold value of S-RNases in the style is also required. Here we present biochemical evidence that eEF1A is a novel S-RNase-binding partner in vitro. We further show that the normal actin binding activity of eEF1A is enhanced by the presence of S-RNase. Lastly, we find that there is a co-localization of S-RNase and actin in the incompatible pollen tubes in structures reminiscent of the actin bundles formed by eEF1A. We propose that increased binding of eEF1A to actin in the presence of S-RNase could help explain the disruption of the actin cytoskeleton observed during SI reactions.

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“…5.1A). It is notable that none of these RNases is angiogenic and only dimeric RNase from bovine seminal plasma (RNase BS) binds to G-actin (Simm et al, 1987). …”

Section: Interaction Of Angiogenin With Actin In Vivo and In Vitromentioning

confidence: 99%

“…RNase BS (D’Alessio et al, 1972) interacts with skeletal muscle actin with an apparent binding constant of 9.2×l0 4 M −1 in 0.1M KC1 (Simm et al, 1987). According to the viscosimetric data, it induces the polymerization of actin below the critical concentration in a depolymerization buffer and accelerates the salt-induced polymerization of actin even at a molar ratio of RNase to actin below l/l00.…”

Section: Interaction Of Angiogenin With Actin In Vivo and In Vitromentioning

confidence: 99%

“…RNase BS consists of two identical subunits cross-linked by disulfide bridges, and it was concluded that the dimeric structure is responsible for the bundling activity and the accelerating effect on the polymerization of actin (Simm et al, 1987). A monomeric form of RNase BS does not cross-link actin filaments and has a much smaller effect on actin polymerization (Simm et al, 1987).…”

Section: Interaction Of Angiogenin With Actin In Vivo and In Vitromentioning

confidence: 99%

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New Insights into the Role of Angiogenin in Actin Polymerization

Pyatibratov¹,

Kostyukova²

2012

International Review of Cell and Molecular Biology

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Angiogenin is a potent stimulator of angiogenesis. It interacts with endothelial cells and induces a wide range of cellular responses initiating a process of blood vessel formation. One important target of angiogenin is endothelial cell-surface actin, and their interaction might be one of crucial steps in angiogenin-induced neovascularization. Recently, it was shown that angiogenin inhibits polymerization of G-actin and changes the physical properties of F-actin. These observations suggest that angiogenin may cause changes in the cell cytoskeleton. This chapter reviews the current state of the literature regarding angiogenin structure and function and discusses the relationship between the angiogenin and actin and possible functional roles of their interaction.

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On the interaction of bovine seminal RNase with actin in vitro

Cited by 11 publications

References 25 publications

Actin is a binding protein for angiogenin.

Actin is a binding protein for angiogenin.

eEF1A Is an S-RNase Binding Factor in Self-Incompatible Solanum chacoense

New Insights into the Role of Angiogenin in Actin Polymerization

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