Functional Roles of the von Willebrand Factor Propeptide
| Autor: | Orla Rawley, David Lillicrap |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Endothelium Angiogenesis 030204 cardiovascular system & hematology 03 medical and health sciences symbols.namesake 0302 clinical medicine Von Willebrand factor hemic and lymphatic diseases von Willebrand Factor Von Willebrand disease medicine Humans Amino Acid Sequence Protein precursor Peptide sequence Furin biology Chemistry Hematology Golgi apparatus medicine.disease Cell biology 030104 developmental biology medicine.anatomical_structure cardiovascular system symbols biology.protein |
| Zdroj: | Hamostaseologie. 41(1) |
| ISSN: | 2567-5761 |
| Popis: | The primary polypeptide sequence of von Willebrand factor (VWF) includes an N-terminal 741-amino acid VWF propeptide (VWFpp). In cells expressing VWF, the VWFpp performs two critical functions. In the Golgi, VWFpp mediates the intermolecular disulfide linkages that generate high-molecular-weight VWF multimers. Subsequently, the VWFpp, which is proteolytically cleaved from mature VWF by furin, functions to generate the endothelial storage organelles (Weibel-Palade bodies) in which VWF and a distinct collection of proteins are stored, and from where they undergo regulated secretion from the endothelium. The VWFpp is secreted from endothelial cells as dimers and circulates in plasma with at least some of the dimers associating with a noncovalent manner with the D′D3 domain of mature VWF. The VWFpp has a half-life of 2 to 3 hours in plasma, but to date no extracellular function has been determined for the molecule. Nevertheless, its large size and several biologically interesting structural features (two sets of vicinal cysteines and an RGD sequence) suggest that there may be roles that the VWFpp plays in hemostasis or associated physiological processes such as angiogenesis or wound repair. |
| Databáze: | OpenAIRE |
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