scholarly journals Dopamine modulates von Willebrand factor secretion in endothelial cells via D2-D4 receptors

2006 ◽  
Vol 4 (7) ◽  
pp. 1588-1595 ◽  
Author(s):  
S. ZAREI ◽  
M. FRIEDEN ◽  
B. RUBI ◽  
P. VILLEMIN ◽  
B. R. GAUTHIER ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Von Willebrand Factor ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Factor Secretion

scholarly journals Weibel-Palade Body Localized Syntaxin-3 Modulates Von Willebrand Factor Secretion From Endothelial Cells

2018 ◽  
Vol 38 (7) ◽  
pp. 1549-1561 ◽  
Author(s):  
Maaike Schillemans ◽  
Ellie Karampini ◽  
Bart L. van den Eshof ◽  
Anastasia Gangaev ◽  
Menno Hofman ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Von Willebrand Factor ◽  
Syntaxin 3 ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Factor Secretion

scholarly journals Vasopressin-induced von Willebrand factor secretion from endothelial cells involves V2 receptors and cAMP

2000 ◽  
Vol 106 (1) ◽  
pp. 107-116 ◽  
Author(s):  
Jocelyne E. Kaufmann ◽  
Alexander Oksche ◽  
Claes B. Wollheim ◽  
Gabriele Günther ◽  
Walter Rosenthal ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Von Willebrand Factor ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Factor Secretion

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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