Native multimer analysis of plasma and platelet von Willebrand factor compared to denaturing separation: Implication for the interpretation of satellite bands

@article{Hohenstein2011NativeMA,
  title={Native multimer analysis of plasma and platelet von Willebrand factor compared to denaturing separation: Implication for the interpretation of satellite bands},
  author={Kurt Hohenstein and Andrea Griesmacher and G{\"u}nter Weigel and Georg Golderer and Helmut Werner Ott},
  journal={ELECTROPHORESIS},
  year={2011},
  volume={32}
}
Blue native electrophoresis (BNE) was applied to analyze the von Willebrand factor (vWF) multimers in their native state and to present a methodology to perform blue native electrophoresis on human plasma proteins, which has not been done before. The major difference between this method and the commonly used SDS‐agarose gel electrophoresis is the lack of satellite bands in the high‐resolution native gel. To further analyze this phenomenon, a second dimension was performed under denaturing… 
View on Wiley
ediss.uni-goettingen.de
3 Citations

3 Citations

Citation Type

Citation Type

von Willebrand Factor multimers profiling with a semi‐automated system
TLDR
A rapid and sensitive semi‐automated method to visualize the multimeric structure of vWF and reduces the time required from 72 to 8 h and is proposed for the first level screening ofvWF multimer deficiency.
Native analysis of plasma‐derived clotting factor VIII concentrates: “Sponge effect” and contaminants
TLDR
Analysis of two commercially available plasma‐derived FVIII preparations, Beriate and Emoclot, through native gel‐based approaches (CN‐PAGE) found the presence of complexes, which resisted the cryoprecipitation, chromatographic and heat treatment processing steps.
von Willebrand factor, clotting factors, and clotting inhibitors in apheresis platelet concentrates
Apheresis platelet concentrates (APCs) are usually stored in citrated plasma at 22°C. The stability of coagulation proteins—von Willebrand factor (vWF), clotting factors (CFs), and their…

References

SHOWING 1-10 OF 36 REFERENCES
The complex multimeric composition of factor VIII/von Willebrand factor
TLDR
The studies suggest that factor VII/vonWillebrand factor in IIA von Willebrand's disease is structurally different from that in other forms of the disorder and indicate that the multimeric composition of factor VIII/von Wille Brand factor is more complex than can be explained by simple linear polymerization of a single protomer.
Analysis of von Willebrand factor multimers by simultaneous high- and low-resolution vertical SDS-agarose gel electrophoresis and Cy5-labeled antibody high-sensitivity fluorescence detection.
TLDR
HSFD shows that this method has high discriminatory power for visualization and densitometric analysis of platelets and plasma vWF multimers in various types of v WD and allows rapid classification of vWD types, to separate types 2A and 2B.
Heterogeneity of plasma von Willebrand factor multimers resulting from proteolysis of the constituent subunit.
TLDR
It is demonstrated that proteolytic cleavage of the constituent subunit is one of the causes determining the heterogeneous size distribution of plasma von Willebrand factor (vWf) multimers, and that platelet vWf stored in alpha-granules is protected from proteolysis.
Visualization of von Willebrand factor multimers by immunoenzymatic stain using avidin-biotin peroxidase complex.
TLDR
A technique for the detection of von Willebrand factor multimers separated by discontinuous SDS agarose electrophoresis has been developed using non-radioactive compounds and is useful for screening or classifying cases with vWD in general laboratories.
Triplet structure of von Willebrand factor reflects proteolytic degradation of high molecular weight multimers.
TLDR
The results suggest that the slowest migrating band of the dimeric triplet set of LMW vWF represents an asymmetric structure composed of an intact subunit to which one NH2- terminal and one COOH-terminal fragment are linked by disulfide bridges.
A new variant of type II von Willebrand disease with aberrant multimeric structure of plasma but not platelet von Willebrand factor (type IIF).
TLDR
This new variant of vonWillebrand disease is characterized by the presence of a dysfunctional von Willebrand factor molecule that exhibits unique structural abnormalities in plasma but appears to be normal in platelets.
A variant of type II von willebrand disease with an abnormal triplet structure and discordant effects of protease inhibitors on plasma and platelet von willebrand factor structure
TLDR
It is characterized as having a long bleeding time, no aggregation of her platelet‐rich plasma (PRP) to ristocetin, and very low plasma and platelet von Willebrand antigen (vWf Ag) and vWf activity.
Multimeric structure of platelet factor VIII/von Willebrand factor: the presence of larger multimers and their reassociation with thrombin-stimulated platelets.
TLDR
A structural difference between platelet and plasma FVIII/vWF that suggests a specific role for platelet FV III/ vWF in hemostasis is shown.
Biochemistry and genetics of von Willebrand factor.
  • J. Sadler
  • Biology, Medicine
    Annual review of biochemistry
  • 1998
TLDR
Growing body of information about VWF synthesis, structure, and function has allowed the reclassification of VWD based upon distinct pathophysiologic mechanisms that appear to correlate with clinical symptoms and the response to therapy.
A new variant of dominant type II von Willebrand's disease with aberrant multimeric pattern of factor VIII-related antigen (type IID).
TLDR
A new type II variant form of von Willebrand's disease has been recognized in a mother and daughter who have bleeding manifestations typical of von Wilkinson's disease, and it is suggested that this new variant be labeled type IID, until a more appropriate nomenclature is developed.
...
1
2
3
4
...