A novel seminal plasma glycoprotein of a teleost, the nile tilapia (Oreochromis niloticus), contains a partial von Willebrand factor type D domain and a zona pellucida-like domain

2002 ◽  
Vol 62 (1) ◽  
pp. 57-68 ◽  
Author(s):  
Kazuhiko Mochida ◽  
Takahiro Matsubara ◽  
Tadashi Andoh ◽  
Kazuhiro Ura ◽  
Shinji Adachi ◽  
...  
Keyword(s):  
Von Willebrand Factor ◽  
Seminal Plasma ◽  
Oreochromis Niloticus ◽  
Nile Tilapia ◽  
Type D ◽  
Nile Tilapia Oreochromis Niloticus ◽  
Plasma Glycoprotein ◽  
Factor Type ◽  
Von Willebrand ◽  
Willebrand Factor

scholarly journals Molecular Characterization of the Von Willebrand Factor Type D Domain of Vitellogenin from Takifugu flavidus

Marine Drugs ◽  
2021 ◽  
Vol 19 (4) ◽  
pp. 181
Author(s):  
Kun Qiao ◽  
Caiyun Jiang ◽  
Min Xu ◽  
Bei Chen ◽  
Wenhui Qiu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Von Willebrand Factor ◽  
Molecular Mechanisms ◽  
Protein Domain ◽  
Type D ◽  
Protein Toxin ◽  
Factor Type ◽  
Von Willebrand ◽  
Willebrand Factor

The von Willebrand factor type D (VWD) domain in vitellogenin has recently been found to bind tetrodotoxin. The way in which this protein domain associates with tetrodotoxin and participates in transporting tetrodotoxin in vivo remains unclear. A cDNA fragment of the vitellogenin gene containing the VWD domain from pufferfish (Takifugu flavidus) (TfVWD) was cloned. Using in silico structural and docking analyses of the predicted protein, we determined that key amino acids (namely, Val115, ASP116, Val117, and Lys122) in TfVWD mediate its binding to tetrodotoxin, which was supported by in vitro surface plasmon resonance analysis. Moreover, incubating recombinant rTfVWD together with tetrodotoxin attenuated its toxicity in vivo, further supporting protein–toxin binding and indicating associated toxicity-neutralizing effects. Finally, the expression profiling of TfVWD across different tissues and developmental stages indicated that its distribution patterns mirrored those of tetrodotoxin, suggesting that TfVWD may be involved in tetrodotoxin transport in pufferfish. For the first time, this study reveals the amino acids that mediate the binding of TfVWD to tetrodotoxin and provides a basis for further exploration of the molecular mechanisms underlying the enrichment and transfer of tetrodotoxin in pufferfish.

von Willebrand factor type D domain mutant of SVS-1/SUSD2, vWDm, induces apoptosis in HeLa cells

2007 ◽  
Vol 98 (6) ◽  
pp. 909-915 ◽  
Author(s):  
Tetsuo Sugahara ◽  
Yzumi Yamashita ◽  
Masahito Shinomi ◽  
Yumiko Isobe ◽  
Banri Yamanoha ◽  
...  
Keyword(s):  
Von Willebrand Factor ◽  
Hela Cells ◽  
Type D ◽  
Factor Type ◽  
Von Willebrand ◽  
Willebrand Factor

Multi-metal tolerance of von Willebrand factor type D domain isolated from metal contaminated site by metatranscriptomics approach

2019 ◽  
Vol 661 ◽  
pp. 432-440 ◽  
Author(s):  
Bharti Thakur ◽  
Rajiv Yadav ◽  
Laurent Vallon ◽  
Roland Marmeisse ◽  
Laurence Fraissinet-Tachet ◽  
...  
Keyword(s):  
Von Willebrand Factor ◽  
Metal Tolerance ◽  
Contaminated Site ◽  
Type D ◽  
Factor Type ◽  
Von Willebrand ◽  
Willebrand Factor

scholarly journals Shear stress-independent binding of von Willebrand factor-type 2B mutants p.R1306Q & p.V1316M to LRP1 explains their increased clearance

2015 ◽  
Vol 13 (5) ◽  
pp. 815-820 ◽  
Author(s):  
N. Wohner ◽  
P. Legendre ◽  
C. Casari ◽  
O. D. Christophe ◽  
P. J. Lenting ◽  
...  
Keyword(s):  
Shear Stress ◽  
Von Willebrand Factor ◽  
Factor Type ◽  
Von Willebrand ◽  
Willebrand Factor
Sign in / Sign up

Export Citation Format

Share Document