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In addition to these antigenic variations, there are four size variants of GPIbα: A, B, C and D (from largest to smallest). Three antigens (HPA-2a, -2b and -12bw) on GPIb have been described ( Table 37.2), but none on GPIX or GPV. Absence of the complex results in the inherited bleeding disorder Bernard–Soulier syndrome. There are approximately 25 000 GPb/IX molecules and 12 000 GPV molecules per platelet. GPIb is non-covalently associated with GPIX (CD42a) and GPV (CD42d). 128 GPIb comprises two disulfide-bonded subunits, GPIbα (CD42b) and GPIbβ (CD42c). The GPIb-VWF interaction can also activate platelets through intracellular signals. GPIb/IX/V binds VWF and mediates the adhesion of platelets to exposed vascular subendothelium surfaces under conditions of high shear stress, and interaction essential for slowing circulating platelets, allowing formation of arterial thrombi.
G Daniels, in Blood and Bone Marrow Pathology (Second Edition), 2011 Antigens on the GPIb/IX/V (CD42) complex This chapter concludes with suggestions for potential areas of future investigation. In addition, there is no specific therapy for patients with thrombotic disorders associated with supernormal levels of either FVIII or VWF. Currently, deficiencies of the proteins are managed with plasma-derived or recombinant concentrates, but they are so expensive as to be unaffordable for as many as 70% of people with bleeding disorders. Mutations that decrease the activity of VWF or FVIII result in VWD or hemophilia A, respectively, and those associated with higher than normal levels of the proteins promote thrombosis. FVIIIa in the tenase complex juxtaposes FIXa with FX, enabling the formation of FXa and the generation of sufficient thrombin for hemostasis. FVIII binds to the membranes of activated platelets and is converted to FVIIIa by trace amounts of thrombin generated through the tissue factor-FVIIa pathway.
Shear stress uncoils VWF, exposing sites that bind platelets and induce platelet aggregation. VWF is the principal modulator of circulating FVIII. After circulating for several hours (FVIII T/2 is 12 h and VWF T/2 is 15 h), the complex binds to receptors on macrophages and endothelial cells, and is degraded. They become associated in the Weibel-Palade bodies of endothelial cells and are released together when these cells are stimulated. The binding sites for the two proteins are located within the C1 domain of FVIII and the D’D3 domain of VWF. The FVIII/VWF complex links the initiation and amplification phases of blood coagulation. Recombinant VWF peptide (VWF71) has similar characteristics to FRETS-VWF73, which is highly sensitive rapid assay without interference with plasma proteins such as bilirubin or hemoglobin.ĭavid Green, in Hemophilia and Von Willebrand Disease, 2018 Summary The coefficient of variation was reported as 5.8%. The amount of ADAMTS13 activity is determined by measuring the unabsorbed HRP activity remaining in solution. Uncleaved substrate is removed by adsorption with streptavidin agarose. ADAMTS13 in the test plasma cleaves the peptide substrate. Alternatively, VWF73 has been conjugated to horseradish peroxidase (HRP) at the N-terminus and labeled with biotin at the C-terminus. The reported coefficient of variation for this test is <20%. The amount of lysine tag that is released after cleavage by ADAMTS13 corresponds to the amount of ADAMTS13 activity. After release, the lysine tag is captured by CM10 cationic protein chip and measured by surface-enhanced laser desorption/ionization time-of-flight mass spectrometer. The lysine tag is released after cleavage of VWF by ADAMTS13. Recombinant VWF peptide (vWF73) can be fused with a lysine tag. Antun MD, MSc, in Transfusion Medicine and Hemostasis (Third Edition), 2019 Other Peptide Methods
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