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• W2023666947 abstract "SummaryGas6 is a novel member of the vitamin K-dependent family of γ-carboxylated proteins and is a ligand for the receptor tyrosine kinase Axl. Gas6–Axl interactions have been shown to mediate cell survival in vascular endothelium. Although the receptor-binding portion of gas6 lies in the C-terminus, the significance of the N-terminal γ-carboxylated residues (Gla domain) is not clear. To address this question, this study examines the role of the Gla domain in phospholipid binding as well as in the promotion of cell survival, especially in endothelial cells. The results show that carboxylated gas6 binds to phosphatidylserine-containing phospholipid membranes in an analogous manner to other γ-carboxylated proteins whereas decarboxylated gas6 does not. The γ-carboxylation inhibitor warfarin abrogates gas6-mediated protection of NIH3T3 fibroblasts from serum starvation-induced apoptosis. Furthermore, the role of γ-carboxylation in gas6's survival effect on endothelium is demonstrated directly in that only carboxylated, but not decarboxylated, gas6 protects endothelial cells from serum starvation-induced apoptosis. γ-carboxylation is also required for both Axl phosphorylation and PI3 kinase activation. Taken together, these findings demonstrate that γ-carboxylation is necessary not only for gas6 binding to phospholipid membranes, but also for gas6-mediated endothelial cell survival. Gas6 is a novel member of the vitamin K-dependent family of γ-carboxylated proteins and is a ligand for the receptor tyrosine kinase Axl. Gas6–Axl interactions have been shown to mediate cell survival in vascular endothelium. Although the receptor-binding portion of gas6 lies in the C-terminus, the significance of the N-terminal γ-carboxylated residues (Gla domain) is not clear. To address this question, this study examines the role of the Gla domain in phospholipid binding as well as in the promotion of cell survival, especially in endothelial cells. The results show that carboxylated gas6 binds to phosphatidylserine-containing phospholipid membranes in an analogous manner to other γ-carboxylated proteins whereas decarboxylated gas6 does not. The γ-carboxylation inhibitor warfarin abrogates gas6-mediated protection of NIH3T3 fibroblasts from serum starvation-induced apoptosis. Furthermore, the role of γ-carboxylation in gas6's survival effect on endothelium is demonstrated directly in that only carboxylated, but not decarboxylated, gas6 protects endothelial cells from serum starvation-induced apoptosis. γ-carboxylation is also required for both Axl phosphorylation and PI3 kinase activation. Taken together, these findings demonstrate that γ-carboxylation is necessary not only for gas6 binding to phospholipid membranes, but also for gas6-mediated endothelial cell survival." @default.
• W2023666947 created "2016-06-24" @default.
• W2023666947 creator A5021294238 @default.
• W2023666947 creator A5025889275 @default.
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• W2023666947 date "2005-12-01" @default.
• W2023666947 modified "2023-10-16" @default.
• W2023666947 title "The role of γ-carboxylation in the anti-apoptotic function of gas6" @default.
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• W2023666947 doi "https://doi.org/10.1111/j.1538-7836.2005.01662.x" @default.
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