GRP78 translocation to the cell surface and O-GlcNAcylation of VE-Cadherin contribute to ER stress-mediated endothelial permeability

Increased O-GlcNAcylation, a well-known post-translational modification of proteins causally linked to various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR). Previously we have shown that endothelial activation induced by inflammation and hyperglycemia...

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Veröffentlicht in:	Scientific reports 2019-07, Vol.9 (1), p.10783-14, Article 10783
Hauptverfasser:	Lenin, Raji, Nagy, Peter G., Jha, Kumar Abhiram, Gangaraju, Rajashekhar
Format:	Artikel
Sprache:	eng
Schlagworte:	14 14/19 38 38/77 631/378/2613/1786 631/80/458/1524 82 82/1 96 96/1 96/109 Antigens, CD - metabolism Blood-Retinal Barrier - cytology Blood-Retinal Barrier - metabolism Cadherins Cadherins - metabolism Capillary Permeability Cell Membrane - metabolism Cell Movement Cell surface Cells, Cultured Diabetes mellitus Diabetic retinopathy Endoplasmic reticulum Endoplasmic Reticulum - drug effects Endoplasmic Reticulum - metabolism Endoplasmic Reticulum Stress Endothelial Cells - metabolism Glycosylation Heat-Shock Proteins - metabolism Humanities and Social Sciences Humans Hyperglycemia Leukocyte migration Monocytes Monocytes - physiology multidisciplinary O-GlcNAcylation Permeability Post-translation Protein Transport Retina Retinopathy Science Science (multidisciplinary) Taurochenodeoxycholic Acid - pharmacology Tauroursodeoxycholic acid Therapeutic applications Transgenic mice Translocation Tumor necrosis factor-α
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