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Article

von Willebrand factor is dimerized by protein disulfide isomerase.

Blood - 3 Mar 2016

Lippok Svenja, Kolšek Katra, Löf Achim, Eggert Dennis, Vanderlinden Willem, Müller Jochen P, König Gesa, Obser Tobias, Röhrs Karoline, Schneppenheim Sonja, Budde Ulrich, Baldauf Carsten, Aponte-Santamaría Camilo, Gräter Frauke, Schneppenheim Reinhard, Rädler Joachim O, Brehm Maria A

Abstract excerpt

Multimeric von Willebrand factor (VWF) is essential for primary hemostasis. The biosynthesis of VWF high-molecular-weight multimers requires spatial separation of each step because of varying pH value requirements. VWF is dimerized in the endoplasmic reticulum by formation of disulfide bonds between the C-terminal cysteine knot (CK) domains of 2 monomers. Here, we investigated the basic question of which protein...

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Identifiers

PMID: 26670633
DOI: 10.1182/blood-2015-04-641902

Genes

VWF

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