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Peretik, J. M.

Publications and source records attributed to Peretik, J. M..

2 recordsLinked to original sources

Integrin-Specific Signaling Drives ER Stress-Dependent Atherogenic Endothelial Activation

Atherogenic endothelial activation arises from both the local arterial microenvironment--characterized by altered extracellular matrix composition and disturbed blood flow--and soluble proinflammatory stimuli such as oxidized low-density lipoprotein (oxLDL). Fibronectin, a provisional extracellular matrix protein enriched at atheroprone sites, enhances endothelial activation and inflammation triggered by oxLDL and disturbed flow. Although endoplasmic reticulum (ER) stress contributes to vascular dysfunction, the role of matrix composition in regulating ER stress remains unknown. We show that oxLDL and disturbed flow induce ER stress selectively in endothelial cells adhered to fibronectin, whereas both stimuli fail to induce ER stress in cells on basement membrane proteins. This matrix-specific ER stress response requires integrin activation, as endothelial cells deficient for integrin activation (talin1 L325R mutation) fail to activate ER stress in response to disturbed flow and oxLDL and direct stimulation of integrin activation using CHAMP peptides is sufficient to trigger ER stress. Blunting endothelial expression of fibronectin-binding integrins (5, v) using siRNA prevents ER stress in response to atherogenic stimuli in vitro, whereas endothelial 5 and v deletion reduces ER stress at atheroprone sites in vivo. The mechanisms driving integrin-dependent ER stress remain unclear, since matrix composition does not affect protein translation, unfolded protein accumulation, or superoxide production, and scavenging superoxide (TEMPOL) does not reduce integrin-dependent ER stress. Inhibiting ER stress with TUDCA reduces proinflammatory and metabolic gene expression (bulk RNAseq) but does not prevent NF-{kappa}B activation, a classic proinflammatory transcription factor. Rather, TUDCA prevents activation of c-jun N-terminal kinase (JNK) and c-jun activation, and blocking JNK (SP600126) or c-Jun activity (TAM67) prevents proinflammatory gene expression following both stimuli. Together, these findings offer new insight into how the arterial microenvironment contributes to atherogenesis, with fibronectin-binding integrin signaling promotes ER stress in response to mechanical and metabolic stressors, thereby amplying proinflammatory endothelial activation through JNK-c-Jun signaling. HighlightsO_LIFibronectin promotes endothelial ER stress in response to oxLDL and disturbed flow via integrin 5{beta}1 and v{beta}3 signaling. C_LIO_LIMatrix-specific ER stress occurs independently of oxidative stress or misfolded protein accumulation, indicating a non-canonical UPR activation. C_LIO_LIER stress amplifies proinflammatory gene expression through JNK-c-Jun signaling, without activating NF-{kappa}B. C_LIO_LITargeting the integrin-ER stress-JNK axis may offer new therapeutic strategies for early atherosclerosis. C_LI O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=109 SRC="FIGDIR/small/654582v1_ufig1.gif" ALT="Figure 1"> View larger version (31K): org.highwire.dtl.DTLVardef@ed7ca3org.highwire.dtl.DTLVardef@191c238org.highwire.dtl.DTLVardef@660f3dorg.highwire.dtl.DTLVardef@7287a4_HPS_FORMAT_FIGEXP M_FIG Graphical Abstract C_FIG

pathology↗

Integrin Affinity Modulation Critically Regulates Atherogenic Endothelial Activation in vitro and in vivo

While vital to platelet and leukocyte adhesion, the role of integrin affinity modulation in adherent cells remains controversial. In endothelial cells, atheroprone hemodynamics and oxidized lipoproteins drive an increase in the high affinity conformation of 5{beta}1 integrins in endothelial cells in vitro, and 5{beta}1 integrin inhibitors reduce proinflammatory endothelial activation to these stimuli in vitro and in vivo. However, the importance of 5{beta}1 integrin affinity modulation to endothelial phenotype remains unknown. We now show that endothelial cells (talin1 L325R) unable to induce high affinity integrins initially adhere and spread, but show significant defects in nascent adhesion formation. In contrast, overall focal adhesion number, area, and composition in stably adherent cells are similar between talin1 wildtype and talin1 L325R endothelial cells. However, talin1 L325R endothelial cells fail to induce high affinity 5{beta}1 integrins, fibronectin deposition, and proinflammatory responses to atheroprone hemodynamics and oxidized lipoproteins. Inducing the high affinity conformation of 5{beta}1 integrins in talin1 L325R cells partially restores fibronectin deposition, whereas NF-{kappa}B activation and maximal fibronectin deposition require both integrin activation and other integrin-independent signaling. In endothelial-specific talin1 L325R mice, atheroprone hemodynamics fail to promote inflammation and macrophage recruitment, demonstrating a vital role for integrin activation in regulating endothelial phenotype.

cell biology↗