Elements of the Endomucin Extracellular Domain Essential for VEGF-Induced VEGFR2 Activity.

Cells
Zhengping HuPatricia A D'Amore

Abstract

Endomucin (EMCN) is the type I transmembrane glycoprotein, mucin-like component of the endothelial cell glycocalyx. We have previously shown that EMCN is necessary for vascular endothelial growth factor (VEGF)-induced VEGF receptor 2 (VEGFR2) internalization and downstream signaling. To explore the structural components of EMCN that are necessary for its function and the molecular mechanism of EMCN in VEGF-induced endothelial functions, we generated a series of mouse EMCN truncation mutants and examined their ability to rescue VEGF-induced endothelial functions in human primary endothelial cells (EC) in which endogenous EMCN had been knocked down using siRNA. Expression of the mouse full-length EMCN (FL EMCN) and the extracellular domain truncation mutants ∆21-81 EMCN and ∆21-121 EMCN, but not the shortest mutant ∆21-161 EMCN, successfully rescued the VEGF-induced EC migration, tube formation, and proliferation. ∆21-161 EMCN failed to interact with VEGFR2 and did not facilitate VEGFR2 internalization. Deletion of COSMC (C1GalT1C1) revealed that the abundant mucin-type O-glycans were not required for its VEGFR2-related functions. Mutation of the two N-glycosylation sites on ∆21-121 EMCN abolished its interaction with VEGFR2 and ...Continue Reading

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Citations

Feb 4, 2021·Animal Models and Experimental Medicine·Guoxin ZhangRan Gao

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Methods Mentioned

BETA
GTPase
nucleotide exchange
transfection
Protein Assay
Gene Knockout
co-immunoprecipitation
co-IP
glycosylation

Software Mentioned

GraphPad
Image Studio
EVOS Cell Imaging System
Image J Angiogenesis Analyzer
VectorBuilder
mEMCN
NetOGlyc
NetNGlyc
Prism
Image J

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