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• W2000394518 abstract "We have previously identified a mutation (R273W) in the von Willebrand factor (VWF) propeptide that results in quantitative deficiency of plasma VWF and a loss of high molecular weight VWF multimers. Recombinant VWF having the R273W mutation (rVWFR273W) expressed in COS-7 cells demonstrated severely impaired secretion and degradation in an intracellular location [Allen, S., et al. (2000) Blood 96, 560-568]. In this report we used pulse-chase analysis and endoglycosidase H digestion of wild-type rVWF and rVWFR273W immunoprecipitated from COS-7 cells to show that rVWFR273W was retained in the endoplasmic reticulum (ER). We demonstrate for the first time that wild-type rVWF and rVWFR273W interacted with the thiol-dependent oxidoreductase ERp57 during biosynthesis in the ER. Pulse chase analysis demonstrated that the interactions of rVWFR273W with ERp57 and calnexin were prolonged compared to wild-type rVWF. In contrast there was no apparent difference between rVWFR273W and wild-type rVWF in their time-courses of interaction with calreticulin." @default.
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• W2000394518 date "2001-01-01" @default.
• W2000394518 modified "2023-09-25" @default.
• W2000394518 title "Endoplasmic Reticulum Retention and Prolonged Association of a von Willebrand's Disease-Causing von Willebrand Factor Variant with ERp57 and Calnexin" @default.
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• W2000394518 doi "https://doi.org/10.1006/bbrc.2000.4139" @default.
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