Regular ArticleBiosynthesis, processing and secretion of von Willebrand factor: biological implications
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2016, Biophysical JournalCitation Excerpt :In the event of vascular injury, the multimeric plasma protein von Willebrand Factor (VWF) mediates platelet adhesion, aggregation, and cross-linking to maintain hemostasis (1,2). VWF is either constitutively secreted into the circulation or is stored in Weibel-Palade bodies and released in the form of ultralarge multimers in response to physiological and pathophysiological stimuli (3). A carefully controlled balance of VWF binding to platelets, and VWF cleavage by ADAMTS13 (a disintegrin and metalloprotease with thrombospondin type 1 motif, member 13) (4–6) is required for hemostasis.
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2013, Biophysical JournalExpression of terminal α2-6-linked sialic acid on von Willebrand factor specifically enhances proteolysis by ADAMTS13
2010, BloodCitation Excerpt :In the endoplasmic reticulum, individual VWF monomers are assembled into dimers through the formation of C-terminal disulphide bonds.7 Subsequently, VWF dimers form high-molecular-weight multimers in the Golgi after another round of N-terminal disulphide bond formation.8 The multimeric composition of plasma VWF is a critical determinant of its functional activity, because larger multimers bind both collagen and platelets with significantly higher affinities and are thus more efficient in inducing platelet aggregation under high-shear conditions.9,10
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