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
2013 ◽  
Vol 33 (6) ◽  
pp. 1329-1338 ◽  
Author(s):  
Anahita Mojiri ◽  
Maryam Nakhaii-Nejad ◽  
Wei-Lee Phan ◽  
Stephen Kulak ◽  
Aneta Radziwon-Balicka ◽  
...  

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

2008 ◽  
Vol 22 (S1) ◽  
Author(s):  
Alice Huertas ◽  
Steven Greenberg ◽  
Maimaiti Yiming ◽  
Jahar Bhattacharya ◽  
Sunita Bhattacharya

1993 ◽  
Vol 70 (06) ◽  
pp. 1053-1057 ◽  
Author(s):  
Agnès M Journet ◽  
Simin Saffaripour ◽  
Denisa D Wagner

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.


1993 ◽  
Vol 70 (04) ◽  
pp. 707-711 ◽  
Author(s):  
Andrew D Blann ◽  
Charles N McCollum

SummaryThe effect of smoking on the blood vessel intima was examined by comparing indices of endothelial activity in serum from smokers with that from non-smokers. Serum from smokers contained higher levels of von Willebrand factor (p <0.01), the smoking markers cotinine (p <0.02) and thiocyanate (p <0.01), and was more cytotoxic to endothelial cells in vitro (p <0.02) than serum from non-smokers. The acute effects of smoking two unfiltered medium tar cigarettes was to briefly increase von Willebrand factor (p <0.001) and cytotoxicity of serum to endothelial cells in vitro (p <0.005), but lipid peroxides or thiocyanate were not increased by this short exposure to tobacco smoke. Although there were correlations between von Willebrand factor and smokers consumption of cigarettes (r = 0.28, p <0.02), number of years smoking (r = 0.41, p <0.001) and cotinine (r = 0.45, p <0.01), the tissue culture of endothelial cells with physiological levels of thiocyanate or nicotine suggested that these two smoking markers were not cytotoxic. They are therefore unlikely to be directly responsible for increased von Willebrand factor in the serum of smokers. We suggest that smoking exerts a deleterious influence on the endothelium and that the mechanism is complex.


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