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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 04276naa a2200697 4500 | |
| 001 | oai:DiVA.org:uu-417592 | |
| 003 | SwePub | |
| 008 | 200821s2003 | |||||||||||000 ||eng| | |
| 009 | oai:DiVA.org:uu-66091 | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-4175922 URI |
| 024 | 7 | a https://doi.org/10.1074/jbc.M3044992002 DOI |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-660912 URI |
| 040 | a (SwePub)uu | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a art2 swepub-publicationtype |
| 100 | 1 | a Dixelius, Johanu Uppsala universitet,Institutionen för genetik och patologi4 aut0 (Swepub:uu)jdi21046 |
| 245 | 1 0 | a Ligand-induced vascular endothelial growth factor receptor-3 (VEGFR-3) heterodimerization with VEGFR-2 in primary lymphatic endothelial cells regulates tyrosine phosphorylation sites |
| 264 | 1 | c 2003 |
| 338 | a print2 rdacarrier | |
| 520 | a Vascular endothelial growth factors (VEGFs) regulate the development and growth of the blood and lymphatic vascular systems. Of the three VEGF receptors (VEGFR), VEGFR-1 and -2 are expressed on blood vessels; VEGFR-2 is found also on lymphatic vessels. VEGFR-3 is expressed mainly on lymphatic vessels but it is also up-regulated in tumor angiogenesis. Although VEGFR-3 is essential for proper lymphatic development, its signal transduction mechanisms are still incompletely understood. Trans-phosphorylation of activated, dimerized receptor tyrosine kinases is known to be critical for the regulation of kinase activity and for receptor interaction with signal transduction molecules. In this study, we have identified five tyrosyl phosphorylation sites in the VEGFR-3 carboxyl-terminal tail. These sites were used both in VEGFR-3 overexpressed in 293 cells and when the endogenous VEGFR-3 was activated in lymphatic endothelial cells. Interestingly, VEGF-C stimulation of lymphatic endothelial cells also induced the formation of VEGFR-3/VEGFR-2 heterodimers, in which VEGFR-3 was phosphorylated only at three of the five sites while the two most carboxyl-terminal tyrosine residues appeared not to be accessible for the VEGFR-2 kinase. Our data suggest that the carboxyl-terminal tail of VEGFR-3 provides important regulatory tyrosine phosphorylation sites with potential signal transduction capacity and that these sites are differentially used in ligand-induced homo- and heterodimeric receptor complexes. | |
| 650 | 7 | a MEDICIN OCH HÄLSOVETENSKAPx Medicinska och farmaceutiska grundvetenskaper0 (SwePub)3012 hsv//swe |
| 650 | 7 | a MEDICAL AND HEALTH SCIENCESx Basic Medicine0 (SwePub)3012 hsv//eng |
| 653 | a Animals | |
| 653 | a Endothelium | |
| 653 | a Vascular | |
| 653 | a Humans | |
| 653 | a Signal Transduction | |
| 653 | a Vascular Endothelial Growth Factor Receptor-2 | |
| 653 | a Mutation | |
| 653 | a Vascular Endothelial Growth Factor Receptor-3 | |
| 653 | a Cell Line | |
| 653 | a Neovascularization | |
| 653 | a Pathologic | |
| 653 | a Up-Regulation | |
| 653 | a Transfection | |
| 653 | a Ligands | |
| 653 | a Phosphorylation | |
| 653 | a Protein Structure | |
| 653 | a Tertiary | |
| 653 | a Tyrosine | |
| 653 | a Binding Sites | |
| 653 | a Dimerization | |
| 653 | a Electrophoresis | |
| 653 | a Polyacrylamide Gel | |
| 653 | a Immunoblotting | |
| 653 | a Peptides | |
| 653 | a Swine | |
| 700 | 1 | a Mäkinen, Taijau University of Helsinki4 aut0 (Swepub:uu)taima352 |
| 700 | 1 | a Wirzenius, Maria4 aut |
| 700 | 1 | a Karkkainen, Marika J.4 aut |
| 700 | 1 | a Wernstedt, Christeru Ludwiginstitutet för Cancerforskning4 aut0 (Swepub:uu)chrisws |
| 700 | 1 | a Alitalo, Kari4 aut |
| 700 | 1 | a Claesson-Welsh, Lenau Uppsala universitet,Institutionen för genetik och patologi4 aut0 (Swepub:uu)lcl04207 |
| 710 | 2 | a Uppsala universitetb Institutionen för genetik och patologi4 org |
| 773 | 0 | t Journal of Biological Chemistryg 278, s. 40973-q 278:42<40973-40979x 0021-9258x 1083-351X |
| 773 | 0 | t J Biol Chemg 278, s. 40973-q 278<40973- |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-417592 |
| 856 | 4 8 | u https://doi.org/10.1074/jbc.M304499200 |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-66091 |
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