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Expression of variant von willebrand factor vwf complementary dna in heterologous cells requirement of the pro polypeptide in vwf multimer formation


, : Expression of variant von willebrand factor vwf complementary dna in heterologous cells requirement of the pro polypeptide in vwf multimer formation. EMBO (European Molecular Biology Organization) Journal 6(10): 2885-2890

Von Willebrand factor (vWF) is a multimeric plasma glycoprotein synthesized by vascular endothelial cells as a pre-pro-polypeptide with a highly repetitive domain structure, symbolized by the formula: (H)-D1-D2-D'-D3-A1-A2-A3-D4-B1-B2-B3-C1-C2-(OH) a heterologous expression system for the synthesis of recombinant vWF protein was developed, consisting of a monkey kidney cell line (COS-1), transfected with full-length vWF cDNA. This system was shown to mimic the constitutive secretory pathway of vWF in endothelial cells, since dimerization and multimerization occur similarly. To determine whether the pro-polypeptide, composed of the domains D1 and D2, is involved in vWF multimerization, a vWF cDNA was constructed that lacked the coding sequence for the pro-polypeptide. The mutant vWF protein, expressed by COS-1 cells transfected with this cDNA, did not assemble beyond the dimer stage. From this observation, we conclude that (i) dimerization does not involve the pro-polypeptide of pro-vWF and (ii) the presence of the pro-polypeptide, as part of pro-vWF, is obligatory for multimerization. It is argued that the interactions, required for interchain binding, are mediated by the D domains.


Accession: 005432398

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Related references

Verweij, C.L.; Hart, M.; Pannekoek, H., 1987: Expression of variant von Willebrand factor (vWF) cDNA in heterologous cells: requirement of the pro-polypeptide in vWF multimer formation. Von Willebrand factor (vWF) is a multimeric plasma glycoprotein synthesized by vascular endothelial cells as a pre-pro-polypeptide with a highly repetitive domain structure, symbolized by the formula: (H)-D1-D2-D'-D3-A1-A2-A3-D4-B1-B2-B3-C1-C...

Verweij C.L.; Hart M.; Pannekoek H., 1987: Von willebrand factor vwf pro polypeptide is required for vwf multimer formation. Thrombosis & Haemostasis 58(1): 8

Leyte, A.; Voorberg, J.; Van Schijndel, H.B.; Duim, B.; Pannekoek, H.; Van Mourik, J.A., 1991: The pro-polypeptide of von Willebrand factor is required for the formation of a functional factor VIII-binding site on mature von Willebrand factor. We have established that a recombinant von Willebrand Factor (vWF) mutant (vWFdelpro) that lacks the propolypeptide, in contrast with mature wild-type vWF, with which it is identical in terms of primary amino acid sequence, is not able to form a c...

Verweij, C.L.; Hart, M.; Pannekoek, H., 1988: Proteolytic cleavage of the precursor of von Willebrand factor is not essential for multimer formation. Monkey kidney cells (COS-1), transfected with full-length human von Willebrand factor (vWF) cDNA encoding the precursor of vWF (pro-vWF), mimic the characteristics of the biosynthesis and of the constitutive secretory pathway, displayed by culture...

Mannucci, P.M.; Abildgaard, C.F.; Gralnick, H.R.; Hill, F.G.; Hoyer, L.W.; Lombardi, R.; Nilsson, I.M.; Tuddenham, E.; Meyer, D., 1985: Multicenter comparison of von Willebrand factor multimer sizing techniques. Report of the Factor VIII and von Willebrand Factor Subcommittee. A multicenter study of various types of von Willebrand's disease (vWD) was conducted in order to compare the different electrophoretic techniques used to evaluate von Willebrand factor multimers in plasma. Seven laboratories participated in t...

Bonthron D.T.; Handin R.I.; Kaufman R.J.; Wasley L.C.; Orr E.C.; Mitsock L.M.; Ewenstein B.; Loscalzo J.; Ginsburg D.; Orkin S.H., 1986: Structure of pre pro von willebrand factor and its expression in heterologous cells. Nature (London) 324(6094): 270-273

Metzner, H.J.; Hermentin, P.; Cuesta-Linker, T.; Langner, S.; Müller, H.G.; Friedebold, J., 1999: Characterization of factor VIII/von Willebrand factor concentrates using a modified method of von Willebrand factor multimer analysis. In order to provide patients with von Willebrand disease a factor VIII (FVIII)/von Willebrand factor (vWF) concentrate of reproducible quality, an SDS-agarose gel electrophoresis method has been established to determine the content of the high mol...

Enayat M.S.; Hill F.G.H., 1986: Evaluation of monoclonal antibodies to von willebrand factor antigen for use in autoradiography von willebrand factor multimer analyses. Ricerca in Clinica e in Laboratorio 16(1): 95

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