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• W2044097637 abstract "The bioactive sphingolipid, ceramide 1-phosphate (C-1-P), has been implicated as an extracellular chemotactic agent directing cellular migration in hematopoietic stem/progenitor cells and macrophages. However, interacting proteins that could mediate these actions of C-1-P have, thus far, eluded identification. We have now identified and characterized interactions between ceramide 1-phosphate and the annexin a2-p11 heterotetramer constituents. This C-1-P-receptor complex is capable of facilitating cellular invasion. Herein, we demonstrate in both coronary artery macrovascular endothelial cells and retinal microvascular endothelial cells that C-1-P induces invasion through an extracellular matrix barrier. By employing surface plasmon resonance, lipid-binding ELISA, and mass spectrometry technologies, we have demonstrated that the heterotetramer constituents bind to C-1-P. Although the annexin a2-p11 heterotetramer constituents do not bind the lipid C-1-P exclusively, other structurally similar lipids, such as phosphatidylserine, sphingosine 1-phosphate, and phosphatidic acid, could not elicit the potent chemotactic stimulation observed with C-1-P. Further, we show that siRNA-mediated knockdown of either annexin a2 or p11 protein significantly inhibits C-1-P-directed invasion, indicating that the heterotetrameric complex is required for C-1-P-mediated chemotaxis. These results imply that extracellular C-1-P, acting through the extracellular annexin a2-p11 heterotetrameric protein, can mediate vascular endothelial cell invasion.Background: Extracellular ceramide 1-phosphate is presumed to interact with extracellular proteins to mediate cellular invasion. These proteins are unidentified.Results: C-1-P interacts with both annexin a2 and p11 proteins. C-1-P-mediated vascular endothelial cell invasion requires expression of these proteins.Conclusion: Extracellular C-1-P mediates invasion via an interaction with the annexin a2-p11 heterotetramer.Significance: Gradients of C-1-P may guide vascular endothelial cell invasion during wound healing. The bioactive sphingolipid, ceramide 1-phosphate (C-1-P), has been implicated as an extracellular chemotactic agent directing cellular migration in hematopoietic stem/progenitor cells and macrophages. However, interacting proteins that could mediate these actions of C-1-P have, thus far, eluded identification. We have now identified and characterized interactions between ceramide 1-phosphate and the annexin a2-p11 heterotetramer constituents. This C-1-P-receptor complex is capable of facilitating cellular invasion. Herein, we demonstrate in both coronary artery macrovascular endothelial cells and retinal microvascular endothelial cells that C-1-P induces invasion through an extracellular matrix barrier. By employing surface plasmon resonance, lipid-binding ELISA, and mass spectrometry technologies, we have demonstrated that the heterotetramer constituents bind to C-1-P. Although the annexin a2-p11 heterotetramer constituents do not bind the lipid C-1-P exclusively, other structurally similar lipids, such as phosphatidylserine, sphingosine 1-phosphate, and phosphatidic acid, could not elicit the potent chemotactic stimulation observed with C-1-P. Further, we show that siRNA-mediated knockdown of either annexin a2 or p11 protein significantly inhibits C-1-P-directed invasion, indicating that the heterotetrameric complex is required for C-1-P-mediated chemotaxis. These results imply that extracellular C-1-P, acting through the extracellular annexin a2-p11 heterotetrameric protein, can mediate vascular endothelial cell invasion. Background: Extracellular ceramide 1-phosphate is presumed to interact with extracellular proteins to mediate cellular invasion. These proteins are unidentified. Results: C-1-P interacts with both annexin a2 and p11 proteins. C-1-P-mediated vascular endothelial cell invasion requires expression of these proteins. Conclusion: Extracellular C-1-P mediates invasion via an interaction with the annexin a2-p11 heterotetramer. Significance: Gradients of C-1-P may guide vascular endothelial cell invasion during wound healing." @default.
• W2044097637 created "2016-06-24" @default.
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• W2044097637 date "2013-07-01" @default.
• W2044097637 modified "2023-09-30" @default.
• W2044097637 title "Ceramide 1-Phosphate Mediates Endothelial Cell Invasion via the Annexin a2-p11 Heterotetrameric Protein Complex" @default.
• W2044097637 cites W135648715 @default.
• W2044097637 cites W1542304810 @default.
• W2044097637 cites W1562745957 @default.
• W2044097637 cites W1605718906 @default.
• W2044097637 cites W1714325720 @default.
• W2044097637 cites W1772998384 @default.
• W2044097637 cites W1775924518 @default.
• W2044097637 cites W1932669647 @default.
• W2044097637 cites W1966223886 @default.
• W2044097637 cites W1972146443 @default.
• W2044097637 cites W1974377953 @default.
• W2044097637 cites W1978119458 @default.
• W2044097637 cites W1982277787 @default.
• W2044097637 cites W1983852016 @default.
• W2044097637 cites W1995721306 @default.
• W2044097637 cites W1996870265 @default.
• W2044097637 cites W2001687686 @default.
• W2044097637 cites W2002012958 @default.
• W2044097637 cites W2005162507 @default.
• W2044097637 cites W2009021880 @default.
• W2044097637 cites W2013690808 @default.
• W2044097637 cites W2019516160 @default.
• W2044097637 cites W2020158690 @default.
• W2044097637 cites W2031143643 @default.
• W2044097637 cites W2034384396 @default.
• W2044097637 cites W2034900417 @default.
• W2044097637 cites W2035353955 @default.
• W2044097637 cites W2036925454 @default.
• W2044097637 cites W2040620918 @default.
• W2044097637 cites W204511859 @default.
• W2044097637 cites W2046413878 @default.
• W2044097637 cites W2048031310 @default.
• W2044097637 cites W2048333374 @default.
• W2044097637 cites W2050254589 @default.
• W2044097637 cites W2054573680 @default.
• W2044097637 cites W2054878669 @default.
• W2044097637 cites W2058188594 @default.
• W2044097637 cites W2062880614 @default.
• W2044097637 cites W2063142068 @default.
• W2044097637 cites W2064013315 @default.
• W2044097637 cites W2065330589 @default.
• W2044097637 cites W2067701304 @default.
• W2044097637 cites W2069377492 @default.
• W2044097637 cites W2079227152 @default.
• W2044097637 cites W2082733405 @default.
• W2044097637 cites W2083762260 @default.
• W2044097637 cites W2084582881 @default.
• W2044097637 cites W2087281748 @default.
• W2044097637 cites W2088143728 @default.
• W2044097637 cites W2097512416 @default.
• W2044097637 cites W2101040824 @default.
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• W2044097637 cites W2121164372 @default.
• W2044097637 cites W2123811384 @default.
• W2044097637 cites W2128649422 @default.
• W2044097637 cites W2155000549 @default.
• W2044097637 cites W2167376541 @default.
• W2044097637 cites W2411685655 @default.
• W2044097637 cites W26705282 @default.
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• W2044097637 doi "https://doi.org/10.1074/jbc.m113.481622" @default.
• W2044097637 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3707677" @default.
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