Related Experiment Video

Updated: Sep 21, 2026

Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes
12:24

Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes

Published on: June 3, 2014

Triplet structure of von Willebrand factor reflects proteolytic degradation of high molecular weight multimers

M Furlan1, R Robles, D Affolter

  • 1Central Hematology Laboratory, Inselspital, University of Bern, Switzerland.

Proceedings of the National Academy of Sciences of the United States of America
|August 15, 1993
PubMed

Insights

Low molecular weight (LMW) von Willebrand factor (vWF) forms exhibit complex structures, suggesting they originate from high molecular weight (HMW) vWF through blood proteolysis.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Hematology

Background:

  • Von Willebrand factor (vWF) exists in various molecular weight forms, including high molecular weight (HMW) and low molecular weight (LMW) populations.
  • The structural organization and formation pathways of LMW vWF multimers are not fully elucidated.

Purpose of the Study:

  • To investigate the subunit composition and structural characteristics of LMW vWF multimers.
  • To propose a model for the formation of LMW vWF from HMW vWF.

Main Methods:

  • Isolation of HMW and LMW vWF from normal human plasma.
  • Mild reduction of interdimeric disulfide bridges in vWF preparations.
  • Sodium dodecyl sulfate-agarose gel electrophoresis.
  • Immunoblotting using anti-vWF antiserum and specific monoclonal antibodies (MAbs) against NH2-terminal (MAb 418) and COOH-terminal (MAb 9) epitopes.

Main Results:

  • LMW vWF multimers were resolved into triplet sets.
  • The slowest migrating band in the triplet represents an asymmetric structure with intact and fragmented vWF subunits linked by disulfide bridges.
  • Intermediate and fastest migrating bands correspond to dimers of COOH-terminal and NH2-terminal fragments, respectively.
  • Higher triplet families contain additional asymmetric dimeric fragments.

Conclusions:

  • LMW vWF structures are complex, involving disulfide-linked fragments of the vWF subunit.
  • The findings support a model where LMW vWF forms are generated by proteolytic cleavage of HMW vWF in circulation.

More Related Videos

Investigating von Willebrand Factor Pathophysiology Using a Flow Chamber Model of von Willebrand Factor-platelet String Formation08:30

Investigating von Willebrand Factor Pathophysiology Using a Flow Chamber Model of von Willebrand Factor-platelet String Formation

Published on: August 14, 2017

The Development and Application of Biophysical Assays for Evaluating Ternary Complex Formation Induced by Proteolysis Targeting Chimeras (PROTACS)07:22

The Development and Application of Biophysical Assays for Evaluating Ternary Complex Formation Induced by Proteolysis Targeting Chimeras (PROTACS)

Published on: January 12, 2024

Related Concept Videos

Protein Folding01:49

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation which is critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.Protein Structure Is Critical to Its Biological FunctionProteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein and Protein Structure02:39

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.A protein's shape is critical to its function. For example, an enzyme can...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...