Protein disulfide isomerase externalization in endothelial cells follows classical and unconventional routes

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• 作者：Thaí ; s L.S. Araujo^a ; Julianna D. Zeidler^a ; ¹ ; Percí ; llia V.S. Oliveira^a ; ¹ ; Matheus H. Dias^b ; ^c ; Hugo A. Armelin^b ; ^c ; Francisco R.M. Laurindo^a ; ^{francisco.laurindo@incor.usp.br}
• 关键词：PDI ; protein disulfide isomerase ; csPDI ; Cell surface PDI ; pecPDIA1 ; peri/epicellular PDIA1 ; ER ; endoplasmic reticulum ; BFA ; Brefeldin-A ; Mon ; Monensin ; CytD ; Cytochalasin-D ; Noc ; Nocodazole ; SC ; Sodium chlorate ; Neo ; Neomycin ; Baf ; bafilomycin ; NEM ; N-ethylmaleimide ; Methy ; methylamine ; Glyb ; glyburide ; DNP ; 2 ; 4-dinitrophenol ; Nyst ; nystatin ; GRASP ; Golgi-associated peripheral membrane protein
• 刊名：Free Radical Biology and Medicine
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：103
• 期：Complete
• 页码：199-208
• 全文大小：1056 K
• 卷排序：103

文摘

Protein disulfide isomerase (PDIA1) externalization in vascular cells supports injury-associated thrombosis or vascular remodeling. Cellular routes of PDIA1 externalization are unknown. We systematically screened PDIA1 secretion routes in endothelial cells. Golgi bypass supports PDIA1 secretion in endothelial cells, while classical pathway also contributes to cell-surface PDIA1. Laminar shear stress triggers PDIA1 secretion and alpha-5 integrin oxidation, suggesting a physiological role for this process.