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Multimeric composition of endothelial cell-derived von Willebrand factor
H M Tsai1, R L Nagel, V B Hatcher
1Division of Hematology, Montefiore Medical Center, Bronx, NY 10467.
Blood
|June 1, 1989
Summary
Human endothelial cells release large von Willebrand factor (vWF) multimers, suggesting they are precursors to plasma vWF. Smaller vWF multimers appear to be intermediate forms in multimerization.
Area of Science:
- Biochemistry
- Cell Biology
- Hematology
Background:
- Von Willebrand factor (vWF) is a multimeric glycoprotein crucial for hemostasis.
- The multimeric structure of vWF influences its function and is essential for platelet adhesion.
- Endothelial cells (ECs) are the primary source of vWF in circulation.
Purpose of the Study:
- To investigate the multimeric composition of von Willebrand factor (vWF) derived from human endothelial cells (ECs).
- To determine the relationship between EC-derived vWF and plasma vWF multimers.
- To elucidate the process of vWF multimerization and release from ECs.
Main Methods:
- SDS-agarose gel electrophoresis and autoradiography were employed to analyze vWF multimers.
- Human umbilical vein endothelial cells (HUVECs) were cultured to study EC-derived vWF.
- Analysis of vWF in cell lysates and conditioned culture media was performed.
Main Results:
- Two distinct vWF multimers were identified in EC lysates: a smaller one (~950 Kd) and a larger one exceeding plasma vWF size.
- A large EC-vWF multimer was detected in culture media within 10 minutes and persisted for days.
- The smaller EC-vWF multimer was not found in conditioned media, suggesting it's an intermediate form.
Conclusions:
- Endothelial cells release a large, fully polymerized vWF multimer, which is likely the precursor to plasma vWF.
- The smaller vWF multimer identified in EC lysates represents a major intermediate in the vWF multimerization process.
- Plasma vWF multimers are likely formed from the large endothelial vWF after its release into circulation.