LIPOPOLYSACCHARIDE-INDUCED DIFFERENTIAL CELL SURFACE EXPRESSION OF INTERCELLULAR ADHESION MOLECULE-1 IN CULTURED HUMAN UMBILICAL CORD VEIN ENDOTHELIAL CELLS

Shock ◽  
1995 ◽  
Vol 3 (2) ◽  
pp. 96-101 ◽  
Author(s):  
Che-Hung Lee ◽  
Yvonne A. Reid ◽  
Julia S. Jong ◽  
Yuan-Hsu Kang
Keyword(s):  
Endothelial Cells ◽  
Cell Surface ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Intercellular Adhesion Molecule ◽  
Human Umbilical Cord ◽  
Intercellular Adhesion Molecule 1 ◽  
Differential Cell ◽  
Umbilical Cord Vein ◽  
Human Umbilical Cord Vein

scholarly journals Shiga Toxin Selectively Upregulates Expression of Syndecan-4 and Adhesion Molecule ICAM-1 in Human Glomerular Microvascular Endothelium

Toxins ◽  
2020 ◽  
Vol 12 (7) ◽  
pp. 435
Author(s):  
Elena B. Volokhina ◽  
Wouter J. C. Feitz ◽  
Lonneke M. Elders ◽  
Thea J. A. M. van der Velden ◽  
Nicole C. A. J. van de Kar ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Adhesion Molecule ◽  
Shiga Toxin ◽  
Alternative Pathway ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Intercellular Adhesion Molecule ◽  
Intercellular Adhesion Molecule 1 ◽  
Microvascular Endothelium ◽  
Protein Levels

Hemolytic uremic syndrome (HUS) is a severe renal disease that is often preceded by infection with Shiga toxin (Stx)-producing Escherichia coli (STEC). The exact mechanism of Stx-mediated inflammation on human glomerular microvascular endothelial cells (HGMVECs) during HUS is still not well understood. In this study, we investigated the effect of Stx1 on the gene expression of proteins involved in leucocyte-mediated and complement-mediated inflammation. Our results showed that Stx1 enhances the mRNA and protein expression of heparan sulfate proteoglycan (HSPG) syndecan-4 in HGMVECs pre-stimulated with tumor necrosis factor α (TNFα). CD44 was upregulated on mRNA but not on protein level; no effect on the mRNA expression of other tested HSPGs glypican-1 and betaglycan was observed. Furthermore, Stx1 upregulated the mRNA, cell surface expression, and supernatant levels of the intercellular adhesion molecule-1 (ICAM-1) in HGMVECs. Interestingly, no effect on the protein levels of alternative pathway (AP) components was observed, although C3 mRNA was upregulated. All observed effects were much stronger in HGMVECs than in human umbilical endothelial cells (HUVECs), a common model cell type used in endothelial studies. Our results provide new insights into the role of Stx1 in the pathogenesis of HUS. Possibilities to target the overexpression of syndecan-4 and ICAM-1 for STEC-HUS therapy should be investigated in future studies.

Action of cAMP on expression and release of adhesion molecules in human endothelial cells

1996 ◽  
Vol 270 (3) ◽  
pp. H807-H816 ◽  
Author(s):  
R. Morandini ◽  
G. Ghanem ◽  
A. Portier-Lemarie ◽  
B. Robaye ◽  
A. Renaud ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Adhesion Molecule ◽  
Umbilical Vein ◽  
Mrna Level ◽  
Phosphodiesterase Inhibitor ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Intercellular Adhesion Molecule ◽  
Intercellular Adhesion Molecule 1 ◽  
Soluble E Selectin

The expression of E-selectin induced by tumor necrosis factor (TNF) on the surface of human umbilical vein endothelial cells (HUVEC) was partially inhibited by an increase in the level of adenosine 3',5'-cyclic monophosphate (cAMP), produced by forskolin or cholera toxin combined with the type IV phosphodiesterase inhibitor rolipram and the protein kinase A agonist phosphorothioate analogue of cAMP SpcAMPS. The same agents had no significant effect on the constitutive and TNF-stimulated expression of intercellular adhesion molecule 1 (ICAM-1), whereas the effect on vascular cell adhesion molecule 1 (VCAM-1) expression was variable depending on cell culture conditions. The stimulatory effects of phorbol 12-myristate 13-acetate and bacterial lipopolysaccharide (LPS) on E-selectin expression were also downregulated by the forskolin-rolipram combination and by SpcAMPS. Inhibition of the surface expression of E-selectin was associated with a decrease of the total amount of the protein in the cell lysate and a reduced mRNA level, with no significant effect on mRNA stability. In anesthetized rats, the terbutaline-rolipram combination reduced the rolling of leukocytes induced by LPS in the mesenteric microcirculation. In addition to their partial inhibitory effect on the TNF-induced surface expression of E-selectin on HUVEC, the forskolin-rolipram combination and SpcAMPS strongly inhibited the release of soluble E-selectin from these cells; the release of soluble ICAM-1 and VCAM-1 was unaffected by these agents. Isoproterenol reduced the release of soluble E-selectin, whereas it had no significant effect on the cell surface expression of the protein. This study underscores the potential anti-inflammatory effect of a rise in the endothelial cAMP level.

scholarly journals Transcriptional Activation of mRNA of Intercellular Adhesion Molecule 1 and Induction of Its Cell Surface Expression in Normal Human Gingival Fibroblasts by Mycoplasma salivarium andMycoplasma fermentans

1999 ◽  
Vol 67 (6) ◽  
pp. 3061-3065 ◽  
Author(s):  
Li Dong ◽  
Ken-Ichiro Shibata ◽  
Yoshihiko Sawa ◽  
Akira Hasebe ◽  
Yuji Yamaoka ◽  
...  
Keyword(s):  
Cell Surface ◽  
Adhesion Molecule ◽  
Transcriptional Activation ◽  
Surface Expression ◽  
Intercellular Adhesion ◽  
Cell Surface Expression ◽  
Intercellular Adhesion Molecule ◽  
Gingival Tissue ◽  
Intercellular Adhesion Molecule 1 ◽  
Normal Human

ABSTRACT Lipoproteins in the cell membranes of both Mycoplasma salivarium and Mycoplasma fermentans were demonstrated to trigger the transcription of intercellular adhesion molecule-1 mRNA in normal fibroblasts isolated from human gingival tissue and to induce its cell surface expression by a mechanism distinct from that of Escherichia coli lipopolysaccharide. The lipid moiety of the lipoproteins was suggested to play a key role in the expression of the activity.

Intrinsic ICAM-1/LFA-1 activation mediates altered responsiveness of atopic asthmatic airway smooth muscle

2000 ◽  
Vol 278 (6) ◽  
pp. L1154-L1163 ◽  
Author(s):  
Michael M. Grunstein ◽  
Hakon Hakonarson ◽  
Neil Maskeri ◽  
Cecilia Kim ◽  
Sing Chuang
Keyword(s):  
Smooth Muscle ◽  
Airway Smooth Muscle ◽  
Constitutive Expression ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Intercellular Adhesion Molecule ◽  
Lymphocyte Function ◽  
Intercellular Adhesion Molecule 1 ◽  
Blocking Antibody ◽  
Asthmatic Patients

Cell adhesion molecules (CAMs) have been importantly implicated in the pathobiology of the airway responses in allergic asthma, including inflammatory cell recruitment into the lungs and altered bronchial responsiveness. To elucidate the mechanism of CAM-related mediation of altered airway responsiveness in the atopic asthmatic state, the expressions and actions of intercellular adhesion molecule-1 (ICAM-1) and its counterreceptor ligand lymphocyte function-associated antigen-1 (LFA-1; i.e., CD11a/CD18) were examined in isolated rabbit airway smooth muscle (ASM) tissues and cultured human ASM cells passively sensitized with sera from atopic asthmatic patients or nonatopic nonasthmatic (control) subjects. Relative to control tissues, the atopic asthmatic sensitized ASM exhibited significantly enhanced maximal contractility to acetylcholine and attenuated relaxation responses to isoproterenol. These proasthmatic changes in agonist responsiveness were ablated by pretreating the atopic sensitized tissues with a monoclonal blocking antibody (MAb) to either ICAM-1 or CD11a, whereas a MAb directed against the related β2-integrin Mac-1 had no effect. Moreover, relative to control tissues, atopic asthmatic sensitized ASM cells displayed an autologously upregulated mRNA and cell surface expression of ICAM-1, whereas constitutive expression of CD11a was unaltered. Extended studies further demonstrated that 1) the enhanced expression and release of soluble ICAM-1 by atopic sensitized ASM cells was prevented when cells were pretreated with an interleukin (IL)-5-receptor-α blocking antibody and 2) administration of exogenous IL-5 to naive (nonsensitized) ASM cells induced a pronounced soluble ICAM-1 release from the cells. Collectively, these observations provide new evidence demonstrating that activation of the CAM counterreceptor ligands ICAM-1 and LFA-1, both of which are endogenously expressed in ASM cells, elicits autologously upregulated IL-5 release and associated changes in ICAM-1 expression and agonist responsiveness in atopic asthmatic sensitized ASM.

ErbB2 Expression on Left Ventricular Epicardial Endothelial Cells and CD105+ Cells is Decreased in Patients with Diabetes Mellitus.

2021 ◽  
Author(s):  
Joanne T. deKay ◽  
Joshua Carver ◽  
Bailey Shevenell ◽  
Angela M. Kosta ◽  
Sergey Tsibulnikov ◽  
...  
Keyword(s):  
Diabetes Mellitus ◽  
Endothelial Cells ◽  
Cell Surface ◽  
High Glucose ◽  
Artery Bypass ◽  
Surface Expression ◽  
Left Ventricular ◽  
Cell Surface Expression ◽  
Erbb Receptors ◽  
Diabetic Patients

Abstract Background We investigated the cell surface expression of ErbB receptors on left ventricular (LV) epicardial endothelial cells and CD105+ cells obtained from cardiac biopsies of patients undergoing coronary artery bypass grafting surgery (CABG). Methods Endothelial cells and CD105+ non-endothelial cells were freshly isolated from LV epicardial biopsies obtained from 15 subjects with diabetes mellitus (DM) and 8 controls. The expression of ErbB recepotrs was examined using multiparametric flow cytometry. Human microvascular endothelial cells (HMEC-1) and LV epicardial CD105+ non-endothelial cells were used to determine the effect of high glucose on ADAM10-dependent cleavage of ErbB receptors. Results We found that diabetes mellitus (DM) and high levels of hemoglobin A1C are associated with reduced expression of ErbB2 on both endothelial cells and CD105+ non-endothelial cells. To determine if the expression of ErbB2 receptors is regulated by glucose levels, we examined the effect of high glucose in HMEC-1 and LV epicardial CD105+ non-endothelial cells, using a novel flow cytometric approach to simultaneously determine the total level, cell surface expression, and phosphorylation of ErbB2. Incubation of cells in the presence of 25 mM D-glucose resulted in decreased cell surface expression of ErbB2. We also found high expression of a disintegrin and metalloproteinase domain-containing protein 10 (ADAM10) on both endothelial cells and CD105+ non-endothelial cells. Inhibition of ADAM10 prevented the high glucose-dependent decrease in the cell surface expression of ErbB2. Conclusions We suggest that high glucose depresses ErbB receptor signaling in endothelial cells and cardiac progenitor cells via the promotion of ADAM10-dependent cleavage of ErbB2 at the cell surface, thus contributing to vascular dysfunction and adverse remodeling seen in diabetic patients.

Oncostatin M regulates endothelin-1 production in human endothelial cells

1998 ◽  
Vol 275 (2) ◽  
pp. H662-H667 ◽  
Author(s):  
Outi Saijonmaa ◽  
Tuulikki Nyman ◽  
Päivi Pacek ◽  
Frej Fyhrquist
Keyword(s):  
Endothelial Cells ◽  
Tyrosine Kinase ◽  
Kinase Inhibitors ◽  
Oncostatin M ◽  
Human Umbilical Cord ◽  
Kinase Activation ◽  
Endothelin 1 ◽  
Umbilical Cord Vein ◽  
Pkc Activation ◽  
Human Umbilical Cord Vein

The effect of the macrophage- and T-lymphocyte-derived cytokine oncostatin M (OSM) on endothelin-1 (ET-1) production in cultured human umbilical cord vein endothelial cells (HUVEC) was studied. OSM (2.5–10 ng/ml) stimulated ET-1 production and the expression of preproendothelin-1 mRNA. The stimulatory effect of OSM was reversed by anti-interleukin (IL)-6 IgG (33 μg/ml). IL-6 (10 ng/ml) was shown to stimulate ET-1 production. The tyrosine kinase inhibitors herbimycin (250–500 ng/ml) and genistein (1–4 μg/ml) suppressed basal ET-1 production and reversed the stimulatory effect of OSM, whereas daidzein (1–8 μg/ml), a less active analog of genistein, had no effect on basal ET-1 production and only partly reversed the stimulatory effect of OSM. The phorbol ester phorbol 12-myristate 13-acetate (PMA) inhibited ET-1 production. Downregulation of protein kinase C (PKC) with PMA (1 μM) preincubation potentiated OSM-induced ET-1 production. In summary, OSM stimulated ET-1 production in cultured HUVEC. The stimulation was probably mediated by IL-6. Furthermore, the present data suggest that tyrosine kinase activation was involved in ET-1 stimulation and that PKC activation leads to suppression of basal and OSM-stimulated ET-1 production.

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