Effect of selective proteasome inhibitors on TNF-induced  activation of primary and transformed endothelial cells

Kalogeris, Theodore J.; Laroux, F. Stephen; Cockrell, Adam S.; Ichikawa, Hiroshi; Okayama, Naotsuka; Phifer, Travis J.; Alexander, J. Steven; Grisham, Matthew B.

doi:10.1152/ajpcell.1999.276.4.c856

Cited by 72 publications

(43 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…6A). These data are in agreement with a previous report that lactacystin inhibits EC NF-B activation assayed by an electrophoretic mobility shift (69).…”

Section: Caspase Inhibition Blocks Lps-induced Apoptosis But Fails Tosupporting

confidence: 93%

A Constitutive Cytoprotective Pathway Protects Endothelial Cells from Lipopolysaccharide-induced Apoptosis

Bannerman

Tupper²,

Ricketts

et al. 2001

Journal of Biological Chemistry

105

111

View full text Add to dashboard Cite

“…6A). These data are in agreement with a previous report that lactacystin inhibits EC NF-B activation assayed by an electrophoretic mobility shift (69).…”

Section: Caspase Inhibition Blocks Lps-induced Apoptosis But Fails Tosupporting

confidence: 93%

A Constitutive Cytoprotective Pathway Protects Endothelial Cells from Lipopolysaccharide-induced Apoptosis

Bannerman

Tupper²,

Ricketts

et al. 2001

Journal of Biological Chemistry

105

111

View full text Add to dashboard Cite

“…We hypothesized that PS-341 treatment should impair IAV replication as a consequence of preventing NF-B activity through inhibition of IB␣ degradation. This inhibitory effect on the NF-B pathway has already been shown for other cells, such as human primary umbilical vein endothelial cells (HUVEC), renal carcinoma cell lines, multiple myeloma cell lines, mantle cell lymphoma cell lines, and pancreatic adenocarcinoma cell lines (3,15,24,29,60,65). Indeed, we could show that PS-341 leads to reduced viral titers.…”

supporting

confidence: 78%

The Clinically Approved Proteasome Inhibitor PS-341 Efficiently Blocks Influenza A Virus and Vesicular Stomatitis Virus Propagation by Establishing an Antiviral State

Dudek

Luig

Pauli³

et al. 2010

J Virol

View full text Add to dashboard Cite

Recently it has been shown that the proinflammatory NF-B pathway promotes efficient influenza virus propagation. Based on these findings, it was suggested that NF-B blockade may be a promising approach for antiviral intervention. The classical virus-induced activation of the NF-B pathway requires proteasomal degradation of the inhibitor of NF-B, IB. Therefore, we hypothesized that inhibition of proteasomal IB degradation should impair influenza A virus (IAV) replication. We chose the specific proteasome inhibitor PS-341, which is a clinically approved anticancer drug also known as

show abstract

“…Thus, to confidently study the TACE-dependent ectodomainshedding, we decided to generate an endothelial cell line that stably expresses human TNF-α. The effect of proteasome inhibition on NF-κB activation was previously shown to be comparable in HUVECs and in the human endothelial cell line ECV-304 (Kalogeris et al, 1999), making this cell line a suitable model to match our criteria.…”

Section: Proteasome Inhibition Increases the Release Of Tnfrsmentioning

confidence: 82%

Proteasome inhibition activates the transport and the ectodomain shedding of TNF-α receptors in human endothelial cells

Peiretti

Canault

Bernot

et al. 2005

Journal of Cell Science

View full text Add to dashboard Cite

Binding of tumor necrosis factor-α (TNF-α) to its transmembrane receptors (TNFRs) mediates proinflammatory, apoptotic and survival responses in several cell types including vascular endothelial cells. Because ectodomain shedding of cell surface molecules can be modified by proteasome activity, we studied in human endothelial cells whether the TNF-α–TNFRs axis can be regulated by the cleavage of their transmembrane forms in a proteasome-dependent manner. We show that proteasome inhibition increases the release of TNF-α and TNFRs from human endothelial cells and decreases their cellular and cell surface expression. This phenomenon involves the transient activation of mitogen-activated protein kinase p42/p44 that triggers the dispersion of TNF-α and TNFRs from their intracellular Golgi-complex-associated pool towards the plasma membrane. This results in their enhanced cleavage by TNF-α converting enzyme (TACE) because it is reduced by synthetic metalloprotease inhibitors, recombinant TIMP-3 and by a dominant negative form of TACE. In the presence of TACE inhibitor, proteasome inhibition increases the cell surface expression of TNFRs and enhances the sensitivity of these cells to the proapoptotic effect of recombinant TNF-α. In conclusion, our data provide evidence that proteasome inhibitors increase TACE-dependent TNFR-shedding in endothelial cells, supporting the use of these molecules in inflammatory disorders. In association with TACE inhibitor, proteasome inhibitors increase the amount of TNFRs at the cell surface and enhance the sensitivity to the proapoptotic effect of TNF-α, which might be of interest in the antitumor therapy.

show abstract

Effect of selective proteasome inhibitors on TNF-induced activation of primary and transformed endothelial cells

Cited by 72 publications

References 29 publications

A Constitutive Cytoprotective Pathway Protects Endothelial Cells from Lipopolysaccharide-induced Apoptosis

A Constitutive Cytoprotective Pathway Protects Endothelial Cells from Lipopolysaccharide-induced Apoptosis

The Clinically Approved Proteasome Inhibitor PS-341 Efficiently Blocks Influenza A Virus and Vesicular Stomatitis Virus Propagation by Establishing an Antiviral State

Proteasome inhibition activates the transport and the ectodomain shedding of TNF-α receptors in human endothelial cells

Contact Info

Product

Resources

About