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Ligand-induced vasc...
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Dixelius, JohanUppsala universitet,Institutionen för genetik och patologi
(author)
Ligand-induced vascular endothelial growth factor receptor-3 (VEGFR-3) heterodimerization with VEGFR-2 in primary lymphatic endothelial cells regulates tyrosine phosphorylation sites
- Article/chapterEnglish2003
Publisher, publication year, extent ...
Numbers
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LIBRIS-ID:oai:DiVA.org:uu-417592
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https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-417592URI
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https://doi.org/10.1074/jbc.M304499200DOI
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https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-66091URI
Supplementary language notes
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Language:English
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Summary in:English
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Classification
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Subject category:ref swepub-contenttype
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Subject category:art swepub-publicationtype
Notes
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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.
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Added entries (persons, corporate bodies, meetings, titles ...)
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Mäkinen, TaijaUniversity of Helsinki(Swepub:uu)taima352
(author)
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Wirzenius, Maria
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Karkkainen, Marika J.
(author)
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Wernstedt, ChristerLudwiginstitutet för Cancerforskning(Swepub:uu)chrisws
(author)
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Alitalo, Kari
(author)
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Claesson-Welsh, LenaUppsala universitet,Institutionen för genetik och patologi(Swepub:uu)lcl04207
(author)
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Uppsala universitetInstitutionen för genetik och patologi
(creator_code:org_t)
Related titles
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In:Journal of Biological Chemistry278, s. 40973-0021-92581083-351X
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In:J Biol Chem278, s. 40973-
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