Chemokine and chemoattractant receptor expression on human endothelial cells

1997 ◽  
Vol 56 (1-3) ◽  
pp. 101
Author(s):  
C Murdoch
Keyword(s):  
Endothelial Cells ◽  
Receptor Expression ◽  
Human Endothelial Cells

scholarly journals Coronary arterial development is regulated by a Dll4-Jag1-EphrinB2 signaling cascade

2019 ◽  
Author(s):  
Stanislao Igor Travisano ◽  
Vera Lucia Oliveira ◽  
Belén Prados ◽  
Joaquim Grego-Bessa ◽  
Vanesa Bou ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Heart Function ◽  
Receptor Expression ◽  
Cell Maturation ◽  
Signaling Cascade ◽  
Human Endothelial Cells ◽  
Perivascular Cell ◽  
Capillary Growth ◽  
Arterial Development ◽  
Notch1 Receptor

AbstractCoronaries are essential for myocardial growth and heart function. Notch is crucial for mouse embryonic angiogenesis, but its role in coronary development remains uncertain. We show Jag1, Dll4 and activated Notch1 receptor expression in sinus venosus (SV) endocardium. Endocardial Jag1 removal blocks SV capillary sprouting, while Dll4 inactivation stimulates excessive capillary growth, suggesting that ligand antagonism regulates coronary primary plexus formation. Later endothelial ligand removal, or forced expression of Dll4 or the glycosyltransferase MFng, blocks coronary plexus remodeling, arterial differentiation, and perivascular cell maturation. Endocardial deletion of Efnb2 phenocopies the coronary arterial defects of Notch mutants. Angiogenic rescue experiments in ventricular explants, or in primary human endothelial cells, indicate that EphrinB2 is a critical effector of antagonistic Dll4 and Jag1 functions in arterial morphogenesis. Thus, coronary arterial precursors are specified in the SV prior to primary coronary plexus formation and subsequent arterial differentiation depends on a Dll4-Jag1-EphrinB2 signaling cascade.

Chemokine and chemoattractant receptor expression on human endothelial cells

1997 ◽  
Vol 56 ◽  
pp. 101 ◽  
Author(s):  
C. Murdoch ◽  
P.N. Monk ◽  
J.E. Pease ◽  
M.D. Barker ◽  
A. Finn
Keyword(s):  
Endothelial Cells ◽  
Receptor Expression ◽  
Human Endothelial Cells

Poliovirus permissivity and specific receptor expression on human endothelial cells

Virology ◽  
1990 ◽  
Vol 174 (1) ◽  
pp. 95-102 ◽  
Author(s):  
Thérèse Couderc ◽  
Thérèse Barzu ◽  
Florian Horaud ◽  
Radu Crainic
Keyword(s):  
Endothelial Cells ◽  
Receptor Expression ◽  
Human Endothelial Cells ◽  
Specific Receptor

Vascular Endothelial Growth Factor Enhances the Expression of Urokinase Receptor in Human Endothelial Cells via Protein Kinase C Activation

2001 ◽  
Vol 85 (02) ◽  
pp. 296-302 ◽  
Author(s):  
Marielle Kroon ◽  
Pieter Koolwijk ◽  
Mario Vermeer ◽  
Bea van der Vecht ◽  
Victor van Hinsbergh
Keyword(s):  
Vascular Endothelial Growth Factor ◽  
Endothelial Cells ◽  
Protein Kinase C ◽  
Growth Factor ◽  
Protein Kinase ◽  
Receptor Expression ◽  
Vascular Endothelial ◽  
Human Endothelial Cells ◽  
Kinase C ◽  
Endothelial Growth Factor

SummaryAmong other proteolytic enzymes, the urokinase-type plasminogen activator (u-PA)/plasmin cascade contributes to cell migration and the formation of capillary-like structures in a fibrinous exudate. The u-PA receptor (u-PAR) focuses proteolytical activity on the cell surface of the endothelial cell and hereby accelerates the pericellular matrix degradation. Vascular endothelial growth factor (VEGF) and fibroblast growth factor (FGF)-2 enhance u-PA receptor expression in human endothelial cells. In this paper we show that the protein kinase C (PKC) inhibitors Ro31-8220 and GF109203X inhibit VEGF165-induced u-PAR antigen expression in human endothelial cells, whereas PKC inhibition had no effect on FGF-2-induced u-PAR antigen enhancement. In addition, inhibition of PKC activity had no effect on VEGF165-or FGF-2-induced proliferation in human endothelial cells. We conclude that VEGF165 induces u-PAR via a PKC-dependent pathway, whereas proliferation is induced via a different pathway probably involving tyrosine phosphorylation of proteins downstream of the VEGF receptors.

Simvastatin modulates chemokine and chemokine receptor expression by geranylgeranyl isoprenoid pathway in human endothelial cells and macrophages

2006 ◽  
Vol 188 (1) ◽  
pp. 51-58 ◽  
Author(s):  
Niels R. Veillard ◽  
Vincent Braunersreuther ◽  
Claire Arnaud ◽  
Fabienne Burger ◽  
Graziano Pelli ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Chemokine Receptor ◽  
Receptor Expression ◽  
Human Endothelial Cells ◽  
Chemokine Receptor Expression ◽  
Isoprenoid Pathway

scholarly journals Tie2 Receptor Expression Is Stimulated by Hypoxia and Proinflammatory Cytokines in Human Endothelial Cells

2000 ◽  
Vol 87 (5) ◽  
pp. 370-377 ◽  
Author(s):  
Carsten Willam ◽  
Petra Koehne ◽  
Jan Steffen Jürgensen ◽  
Michael Gräfe ◽  
Kay Dietrich Wagner ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Proinflammatory Cytokines ◽  
Receptor Expression ◽  
Human Endothelial Cells ◽  
Tie2 Receptor

scholarly journals Regulation of Tie Receptor Expression on Human Endothelial Cells by Protein Kinase C-Mediated Release of Soluble Tie

Blood ◽  
1997 ◽  
Vol 90 (2) ◽  
pp. 706-715 ◽  
Author(s):  
Rachel Yabkowitz ◽  
Susanne Meyer ◽  
Donna Yanagihara ◽  
David Brankow ◽  
Tabitha Staley ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Surface ◽  
Extracellular Domain ◽  
Receptor Expression ◽  
Cell Surface Receptor ◽  
Soluble Form ◽  
Human Endothelial Cells ◽  
Kinase C

Abstract The expression and activity of receptor tyrosine kinases (RTK) at the cell surface can be modulated by several different pathways including the proteolytic release of the extracellular domain as a soluble receptor. We investigated the regulation of tie receptor expression, an orphan RTK restricted to cells of hematopoietic and endothelial lineages, on primary human endothelial cells and a stably transfected Chinese hamster ovary (CHO) cell line. Tie was expressed in cells as a doublet of 135 and 125 kD; the 135-kD band represented mature cell surface receptor containing sialic acid and N-linked oligosaccharide residues, whereas the 125-kD band represented an intracellular pool of immature receptor. Phorbol 12-myristate 13-acetate (PMA) had dramatic effects on tie expression at the cell surface. Within 15 minutes of PMA treatment, the 135-kD band disappeared from the cell surface and was accompanied by the appearance of a 100-kD band in cell supernatants. The 100-kD band continued to accumulate in the media throughout the duration of PMA treatment during which mature tie receptor was undetectable on the cell surface by fluorescence-activated cell sorting (FACS) or in cell lysates by immunoblot analysis. Using specific antibodies, this 100-kD species was shown to be a soluble form of the tie receptor containing the extracellular domain. PMA-dependent release of soluble tie was mediated through the activation of protein kinase C (PKC); soluble tie was not released in the presence of PKC inhibitors, an inactive PMA analog, or following the downregulation of PKC through chronic PMA treatment. These results indicate that tie receptor expression on endothelial cells is regulated by the release of a soluble extracellular fragment following activation of PKC. Parallel pathways regulating c-kit, tumor necrosis factor (TNF), and colony-stimulating factor (CSF) receptor expression suggest that the release of extracellular receptor fragments represents an alternative mechanism through which cells modulate responses to growth factors and cytokines.

Sign in / Sign up

Export Citation Format

Share Document