Induction of nitric oxide by erythropoietin is mediated by the β common receptor and requires interaction with VEGF receptor 2
Copyright policy )Induction of nitric oxide by erythropoietin is mediated by the β common receptor and requires interaction with VEGF receptor 2
AbstractVascular endothelial growth factor (VEGF) and erythropoietin (EPO) have profound effects on the endothelium and endothelial progenitor cells (EPCs), which originate from the bone marrow and differentiate into endothelial cells. Both EPO and VEGF have demonstrated an ability to increase the number and performance properties of EPCs. EPC behavior is highly dependent on nitric oxide (NO), and both VEGF and EPO can stimulate intracellular NO. EPO can bind to the homodimeric EPO receptor (EPO-R) and the heterodimeric receptor, EPO-R and the common β receptor (βC-R). Although VEGF has several receptors, VEGF-R2 appears most critical to EPC function. We demonstrate that EPO induction of NO is dependent on the βC-R and VEGF-R2, that VEGF induction of NO is dependent on the expression of the βC-R, and that the βC-R and VEGF-R2 interact. This is the first definitive functional and structural evidence of an interaction between the 2 receptors and has implications for the side effects of EPO.
- Florida Southern College United States
Mice, Knockout, Vascular Endothelial Growth Factor A, Nitric Oxide Synthase Type III, Reverse Transcriptase Polymerase Chain Reaction, Receptor Cross-Talk, Hematopoietic Stem Cells, Nitric Oxide, Transfection, Vascular Endothelial Growth Factor Receptor-2, Mice, Inbred C57BL, Mice, Protein Subunits, Receptors, Erythropoietin, Animals, Humans, Phosphorylation, Dimerization, Erythropoietin, Proto-Oncogene Proteins c-akt, Cells, Cultured
Mice, Knockout, Vascular Endothelial Growth Factor A, Nitric Oxide Synthase Type III, Reverse Transcriptase Polymerase Chain Reaction, Receptor Cross-Talk, Hematopoietic Stem Cells, Nitric Oxide, Transfection, Vascular Endothelial Growth Factor Receptor-2, Mice, Inbred C57BL, Mice, Protein Subunits, Receptors, Erythropoietin, Animals, Humans, Phosphorylation, Dimerization, Erythropoietin, Proto-Oncogene Proteins c-akt, Cells, Cultured
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