Characterization of a single-domain von Willebrand factor type C protein (HaSVC) from the salivary gland of the tick Hyalomma asiaticum

2021 ◽  
pp. 108190
Author(s):  
Haiyan Gong ◽  
Jialin Yao ◽  
Bingbing Zhang ◽  
Yongzhi Zhou ◽  
Houshuang Zhang ◽  
...  
Keyword(s):  
Salivary Gland ◽  
Von Willebrand Factor ◽  
Single Domain ◽  
C Protein ◽  
Type C ◽  
Factor Type ◽  
Von Willebrand ◽  
Willebrand Factor

scholarly journals Solution Structure and Dynamics of a Prototypical Chordin-like Cysteine-rich Repeat (von Willebrand Factor Type C Module) from Collagen IIA

2004 ◽  
Vol 279 (51) ◽  
pp. 53857-53866 ◽  
Author(s):  
Joanne M. O'Leary ◽  
John M. Hamilton ◽  
Charlotte M. Deane ◽  
Najl V. Valeyev ◽  
Linda J. Sandell ◽  
...  
Keyword(s):  
Von Willebrand Factor ◽  
Solution Structure ◽  
Structure And Dynamics ◽  
Type C ◽  
Factor Type ◽  
Von Willebrand ◽  
Willebrand Factor

scholarly journals Binding between Crossveinless-2 and Chordin Von Willebrand Factor Type C Domains Promotes BMP Signaling by Blocking Chordin Activity

PLoS ONE ◽  
2010 ◽  
Vol 5 (9) ◽  
pp. e12846 ◽  
Author(s):  
Jin-Li Zhang ◽  
Lucy J. Patterson ◽  
Li-Yan Qiu ◽  
Daria Graziussi ◽  
Walter Sebald ◽  
...  
Keyword(s):  
Von Willebrand Factor ◽  
Bmp Signaling ◽  
Type C ◽  
Factor Type ◽  
Von Willebrand ◽  
Willebrand Factor

Characterization of Partial Gene Deletions in Type III von Willebrand Disease with Alloantibody Inhibitors

1994 ◽  
Vol 72 (02) ◽  
pp. 180-185 ◽  
Author(s):  
David J Mancuso ◽  
Elodee A Tuley ◽  
Ricardo Castillo ◽  
Norma de Bosch ◽  
Pler M Mannucci ◽  
...  
Keyword(s):  
Von Willebrand Factor ◽  
Von Willebrand Disease ◽  
Pcr Analysis ◽  
Gene Deletions ◽  
Factor Gene ◽  
Type Iii ◽  
Large Deletions ◽  
Von Willebrand ◽  
Willebrand Factor

Summaryvon Willebrand factor gene deletions were characterized in four patients with severe type III von Willebrand disease and alloantibodies to von Willebrand factor. A PCR-based strategy was used to characterize the boundaries of the deletions. Identical 30 kb von Willebrand factor gene deletions which include exons 33 through 38 were identified in two siblings of one family by this method. A small 5 base pair insertion (CCTGG) was sequenced at the deletion breakpoint. PCR analysis was used to detect the deletion in three generations of the family, including two family members who are heterozygous for the deletion. In a second family, two type III vWD patients, who are distant cousins, share an -56 kb deletion of exons 22 through 43. The identification and characterization of large vWF gene deletions in these type III vWD patients provides further support for the association between large deletions in both von Willebrand factor alleles and the development of inhibitory alloantibodies.

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.

scholarly journals Substructure of human von Willebrand factor. Proteolysis by V8 and characterization of two functional domains.

1986 ◽  
Vol 261 (33) ◽  
pp. 15679-15689 ◽  
Author(s):  
L J Fretto ◽  
W E Fowler ◽  
D R McCaslin ◽  
H P Erickson ◽  
P A McKee
Keyword(s):  
Von Willebrand Factor ◽  
Functional Domains ◽  
Von Willebrand ◽  
Willebrand Factor

Further specificity characterization of von Willebrand factor inhibitors developed in two patients with severe von Willebrand disease

Blood ◽  
1988 ◽  
Vol 72 (1) ◽  
pp. 116-120 ◽  
Author(s):  
MF Lopez-Fernandez ◽  
R Martin ◽  
C Lopez-Berges ◽  
F Ramos ◽  
N Bosch ◽  
...  
Keyword(s):  
Von Willebrand Factor ◽  
Complex Structure ◽  
Relative Proportion ◽  
Von Willebrand Disease ◽  
Rabbit Antibody ◽  
Human Factor Viii ◽  
Rabbit Polyclonal Antibody ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract Circulating inhibitors against von Willebrand factor (vWF) that show the properties of heterologous IgG antibodies have been described in a few patients with severe von Willebrand disease (vWD). The present study provides further characterization of inhibitors from two patients with severe vWD. Inhibitors in both, like polyclonal rabbit antibody, detected all sizes of multimers and the complex structure of each multimer from platelets and plasma of normal individuals as well as from plasma of patients with IIA, IIB, and IIC vWD. Both inhibitors and the rabbit antibody reacted mainly with the intact 225-Kd vWF subunit and the 189-H and 140-Kd fragments in contrast to monoclonal antibodies specific for vWF fragments that detected a higher relative proportion of 176-Kd fragment. Furthermore, all these antibodies recognized fragment III, although one inhibitor and rabbit polyclonal antibody reacted poorly and the other inhibitor did not react at all with reduced fragment II of vWF digested with Staphylococcus aureus V-8 protease. These data suggest that although human inhibitors from severe vWD patients may behave, to some extent, as polyclonal heterologous antibodies against native vWF, the former show striking differences in their target specificity as well as a much broader specificity than that described for human factor VIII inhibitors.

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