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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MARC

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

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2003
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LIBRIS-ID:oai:DiVA.org:uu-417592
https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-417592URI
https://doi.org/10.1074/jbc.M304499200DOI
https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-66091URI

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Language:English
Summary in:English

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Subject category:ref swepub-contenttype
Subject category:art swepub-publicationtype

Notes

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.

Subject headings and genre

MEDICIN OCH HÄLSOVETENSKAP Medicinska och farmaceutiska grundvetenskaper hsv//swe
MEDICAL AND HEALTH SCIENCES Basic Medicine hsv//eng
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

Added entries (persons, corporate bodies, meetings, titles ...)

Mäkinen, TaijaUniversity of Helsinki(Swepub:uu)taima352 (author)
Wirzenius, Maria (author)
Karkkainen, Marika J. (author)
Wernstedt, ChristerLudwiginstitutet för Cancerforskning(Swepub:uu)chrisws (author)
Alitalo, Kari (author)
Claesson-Welsh, LenaUppsala universitet,Institutionen för genetik och patologi(Swepub:uu)lcl04207 (author)
Uppsala universitetInstitutionen för genetik och patologi (creator_code:org_t)

Related titles

In:Journal of Biological Chemistry278, s. 40973-0021-92581083-351X
In:J Biol Chem278, s. 40973-

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By the author/editor: Dixelius, Johan; Mäkinen, Taija; Wirzenius, Maria; Karkkainen, Mari ...; Wernstedt, Chris ...; Alitalo, Kari; show more...; Claesson-Welsh, ...; show less...

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MEDICAL AND HEALTH SCIENCES: MEDICAL AND HEAL ...; and Basic Medicine

Articles in the publication: Journal of Biolo ...; J Biol Chem

By the university: Uppsala University

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