Aberrant von Willebrand factor expression of sinusoidal endothelial cells and quiescence of hepatic stellate cells in nodular regenerative hyperplasia and obliterative portal venopathy

2020 ◽  
Vol 76 (7) ◽  
pp. 959-967
Author(s):  
Xuchen Zhang ◽  
Courtney Thomas ◽  
Thomas D Schiano ◽  
Swan N Thung ◽  
Stephen C Ward ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Von Willebrand Factor ◽  
Hepatic Stellate Cells ◽  
Stellate Cells ◽  
Nodular Regenerative Hyperplasia ◽  
Sinusoidal Endothelial Cells ◽  
Factor Expression ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Obliterative Portal Venopathy

scholarly journals Hypoxia Results in Upregulation and De Novo Activation of Von Willebrand Factor Expression in Lung Endothelial Cells

2013 ◽  
Vol 33 (6) ◽  
pp. 1329-1338 ◽  
Author(s):  
Anahita Mojiri ◽  
Maryam Nakhaii-Nejad ◽  
Wei-Lee Phan ◽  
Stephen Kulak ◽  
Aneta Radziwon-Balicka ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Von Willebrand Factor ◽  
De Novo ◽  
Factor Expression ◽  
Lung Endothelial Cells ◽  
Von Willebrand ◽  
Willebrand Factor

Endothelial cells of different organs exhibit heterogeneity in von Willebrand factor expression in response to hypoxia

2019 ◽  
Vol 282 ◽  
pp. 1-10 ◽  
Author(s):  
Anahita Mojiri ◽  
Parnian Alavi ◽  
Maria Areli Lorenzana Carrillo ◽  
Maryam Nakhaei-Nejad ◽  
Consolato M. Sergi ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Von Willebrand Factor ◽  
Factor Expression ◽  
Von Willebrand ◽  
Willebrand Factor

scholarly journals Chronic hypoxia in vivo increases von Willebrand factor expression in lung endothelial cells

2008 ◽  
Vol 22 (S1) ◽  
Author(s):  
Alice Huertas ◽  
Steven Greenberg ◽  
Maimaiti Yiming ◽  
Jahar Bhattacharya ◽  
Sunita Bhattacharya
Keyword(s):  
Endothelial Cells ◽  
Von Willebrand Factor ◽  
Chronic Hypoxia ◽  
Factor Expression ◽  
Lung Endothelial Cells ◽  
Von Willebrand ◽  
Willebrand Factor

Von Willebrand factor expression in endometrial endothelial cells in women with menorrhagia

2010 ◽  
Vol 94 (6) ◽  
pp. 2335-2337 ◽  
Author(s):  
Umber Agarwal ◽  
Soha El Sheikh ◽  
Ashwini Kulkarni ◽  
Donna Baff ◽  
Rezan A. Kadir
Keyword(s):  
Endothelial Cells ◽  
Von Willebrand Factor ◽  
Factor Expression ◽  
Von Willebrand ◽  
Willebrand Factor

Requirement for Both D Domains of the Propolypeptide in von Willebrand Factor Muitimerization and Storage

1993 ◽  
Vol 70 (06) ◽  
pp. 1053-1057 ◽  
Author(s):  
Agnès M Journet ◽  
Simin Saffaripour ◽  
Denisa D Wagner
Keyword(s):  
Endothelial Cells ◽  
Endoplasmic Reticulum ◽  
Von Willebrand Factor ◽  
Deletion Mutants ◽  
Relative Importance ◽  
D2 Domain ◽  
Constitutive Secretion ◽  
Von Willebrand ◽  
And Storage ◽  
Willebrand Factor

SummaryBiosynthesis of the adhesive glycoprotein von Willebrand factor (vWf) by endothelial cells results in constitutive secretion of small multimers and storage of the largest multimers in rodshaped granules called Weibel-Palade bodies. This pattern is reproduced by expression of pro-vWf in heterologous cells with a regulated pathway of secretion, that store the recombinant protein in similar elongated granules. In these cells, deletion of the vWf prosequence prevents vWf storage. The prosequence, composed of two homologous domains (D1 and D2), actively participates in vWf multimer formation as well. We expressed deletion mutants lacking either the D1 domain (D2vWf) or the D2 domain (D1vWf) in various cell lines to analyze the relative importance of each domain in vWf muitimerization and storage. Both proteins were secreted efficiently without being retained in the endoplasmic reticulum. Despite this, neither multimerized past the dimer stage and they were not stored. We conclude that several segments of the prosequence are jointly involved in vWf muitimerization and storage.

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