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Ligand-induced vasc...
Ligand-induced vascular endothelial growth factor receptor-3 (VEGFR-3) heterodimerization with VEGFR-2 in primary lymphatic endothelial cells regulates tyrosine phosphorylation sites
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- Dixelius, Johan (författare)
- Uppsala universitet,Institutionen för genetik och patologi
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- Mäkinen, Taija (författare)
- University of Helsinki
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Wirzenius, Maria (författare)
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Karkkainen, Marika J. (författare)
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- Wernstedt, Christer (författare)
- Ludwiginstitutet för Cancerforskning
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Alitalo, Kari (författare)
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- Claesson-Welsh, Lena (författare)
- Uppsala universitet,Institutionen för genetik och patologi
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(creator_code:org_t)
- 2003
- 2003
- Engelska.
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Ingår i: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 278, s. 40973-
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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https://urn.kb.se/re...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine (hsv//eng)
Nyckelord
- Animals
- Endothelium
- Vascular
- Humans
- Signal Transduction
- Vascular Endothelial Growth Factor Receptor-2
- Mutation
- Vascular Endothelial Growth Factor Receptor-3
- Cell Line
- Neovascularization
- Pathologic
- Up-Regulation
- Transfection
- Ligands
- Phosphorylation
- Protein Structure
- Tertiary
- Tyrosine
- Binding Sites
- Dimerization
- Electrophoresis
- Polyacrylamide Gel
- Immunoblotting
- Peptides
- Swine
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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