%0 Journal Article %1 Rahimi.2009 %A Rahimi, N. %A Golde, T. E. %A Meyer, R. D. %D 2009 %J Cancer Res. %K Amyloid B-Cell C Cell Cells Cytoplasm Diffuse Endothelial Factor Growth Humans Hypertension Kinase Large Ligands Lymphoma Membrane Necrosis Phosphorylation Precursor Protein Receptor-1 Research Secretases Signal Structure Tertiary Transduction Tyrosine Vascular biosynthesis cells enzymology metabolism pathology protein %N 6 %P 2607-2614 %T Identification of ligand-induced proteolytic cleavage and ectodomain shedding of VEGFR-1/FLT1 in leukemic cancer cells %U PM:19276374 %V 69 %X Vascular endothelial growth factor receptor-1/fms-related tyrosine kinase 1 (VEGFR-1/FLT1) is expressed as a membrane-bound receptor tyrosine kinase and as an alternatively spliced soluble protein (sVEGFR-1) containing the 1-6 IgG-like domain of its ectodomain. sVEGFR-1 is known as a naturally occurring inhibitor of angiogenesis and as a surrogate marker for cancer progression; it is also linked to pregnancy-induced hypertension called preeclampsia and to avascularity of normal cornea. It remains an open question whether alternative mRNA splicing is the only mechanism by which sVEGFR-1 is generated. In this study, we show that in leukemic cancer cells, PlGF and VEGF-A both induce tyrosine phosphorylation of VEGFR-1 and render it susceptible to ectodomain shedding, resulting in the generation of sVEGFR-1 and an intracellular cytoplasmic fragment. Activation of protein kinase C and tumor necrosis factor-alpha-converting enzyme family metalloproteases are critically required for the occur

@article{Rahimi.2009, abstract = {Vascular endothelial growth factor receptor-1/fms-related tyrosine kinase 1 (VEGFR-1/FLT1) is expressed as a membrane-bound receptor tyrosine kinase and as an alternatively spliced soluble protein (sVEGFR-1) containing the 1-6 IgG-like domain of its ectodomain. sVEGFR-1 is known as a naturally occurring inhibitor of angiogenesis and as a surrogate marker for cancer progression; it is also linked to pregnancy-induced hypertension called preeclampsia and to avascularity of normal cornea. It remains an open question whether alternative mRNA splicing is the only mechanism by which sVEGFR-1 is generated. In this study, we show that in leukemic cancer cells, PlGF and VEGF-A both induce tyrosine phosphorylation of VEGFR-1 and render it susceptible to ectodomain shedding, resulting in the generation of sVEGFR-1 and an intracellular cytoplasmic fragment. Activation of protein kinase C and tumor necrosis factor-alpha-converting enzyme family metalloproteases are critically required for the occur}, added-at = {2010-02-05T11:28:39.000+0100}, author = {Rahimi, N. and Golde, T. E. and Meyer, R. D.}, biburl = {https://www.bibsonomy.org/bibtex/25a47ea780da22e7f86a3cef06ec574cb/kanefendt}, interhash = {ab0820afabce041f8530b6a3fe32bab7}, intrahash = {5a47ea780da22e7f86a3cef06ec574cb}, journal = {Cancer Res.}, keywords = {Amyloid B-Cell C Cell Cells Cytoplasm Diffuse Endothelial Factor Growth Humans Hypertension Kinase Large Ligands Lymphoma Membrane Necrosis Phosphorylation Precursor Protein Receptor-1 Research Secretases Signal Structure Tertiary Transduction Tyrosine Vascular biosynthesis cells enzymology metabolism pathology protein}, number = 6, pages = {2607-2614}, timestamp = {2010-02-05T11:28:53.000+0100}, title = {Identification of ligand-induced proteolytic cleavage and ectodomain shedding of VEGFR-1/FLT1 in leukemic cancer cells}, url = {PM:19276374}, volume = 69, year = 2009 }