PUBLICATION

Hypoxia-induced expression of phosducin-like 3 regulates expression of VEGFR-2 and promotes angiogenesis

Authors
Srinivasan, S., Chitalia, V., Meyer, R.D., Hartsough, E., Mehta, M., Harrold, I., Anderson, N., Feng, H., Smith, L.E., Jiang, Y., Costello, C.E., Rahimi, N.
ID
ZDB-PUB-150611-8
Date
2015
Source
Angiogenesis   18(4): 449-62 (Journal)
Registered Authors
Anderson, Nicole M., Feng, Hui, Harrold, Itrat
Keywords
Angiogenesis, VEGFR-2, PDCL3, Hypoxia, Protein ubiquitination, N-terminal methionine acetylation, Chaperone protein
MeSH Terms
  • Animals
  • Carrier Proteins/metabolism*
  • Gene Expression Regulation*
  • HEK293 Cells
  • Human Umbilical Vein Endothelial Cells/metabolism*
  • Human Umbilical Vein Endothelial Cells/pathology
  • Humans
  • Hypoxia/metabolism*
  • Hypoxia/pathology
  • Mice
  • Molecular Chaperones/metabolism*
  • Neovascularization, Physiologic*
  • Nerve Tissue Proteins/metabolism*
  • Protein Folding
  • Vascular Endothelial Growth Factor Receptor-2/biosynthesis*
PubMed
26059764 Full text @ Angiogenesis
Abstract
Expression and activation of vascular endothelial growth factor receptor 2 (VEGFR-2) by VEGF ligands are the main events in the stimulation of pathological angiogenesis. VEGFR-2 expression is generally low in the healthy adult blood vessels, but its expression is markedly increased in the pathological angiogenesis. In this report, we demonstrate that phosducin-like 3 (PDCL3), a recently identified chaperone protein involved in the regulation of VEGFR-2 expression, is required for angiogenesis in zebrafish and mouse. PDCL3 undergoes N-terminal methionine acetylation, and this modification affects PDCL3 expression and its interaction with VEGFR-2. Expression of PDCL3 is regulated by hypoxia, the known stimulator of angiogenesis. The mutant PDCL3 that is unable to undergo N-terminal methionine acetylation was refractory to the effect of hypoxia. The siRNA-mediated silencing of PDCL3 decreased VEGFR-2 expression resulting in a decrease in VEGF-induced VEGFR-2 phosphorylation, whereas PDCL3 over-expression increased VEGFR-2 protein. Furthermore, we show that PDCL3 protects VEGFR-2 from misfolding and aggregation. The data provide new insights for the chaperone function of PDCL3 in angiogenesis and the roles of hypoxia and N-terminal methionine acetylation in PDCL3 expression and its effect on VEGFR-2.
Genes / Markers
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Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping