N-linked glycan stabilisation of the VWF A2 domain.
London, United Kingdom. In Blood, Feb 2016
UNASSIGNED: Shear forces in the blood trigger a conformational transition in the VWF A2 domain, from its native folded to an unfolded state, in which the cryptic scissile bond (Y1505-M1606) is exposed and can then be proteolysed by ADAMTS13.
Role of fluid shear stress in regulating VWF structure, function and related blood disorders.
Buffalo, United States. In Biorheology, Dec 2015
Once in blood, the protein multimer distribution is dynamically regulated by fluid shear stress which has two opposing effects: it promotes the aggregation or self-association of multiple VWF units, and it simultaneously reduces multimer size by facilitating the force-dependent cleavage of the protein by various proteases, most notably ADAMTS13 (a disintegrin and metalloprotease with thrombospondin type repeats, motif 1 type 13).
Pathogenesis of thrombotic microangiopathies.
Philadelphia, United States. In Annu Rev Pathol, 2007
The congenital and idiopathic TTP syndromes are caused primarily by deficiency of ADAMTS13, owing to mutations in the ADAMTS13 gene or autoantibodies that inhibit ADAMTS13 activity.