Role of factor VIII-von Willebrand factor and fibronectin in the interaction of platelets in flowing blood with monomeric and fibrillar human collagen types I and III.

Abstract

Platelet adhesion to monomeric collagen types I and III, which were purified from human umbilical arteries, was studied in a perfusion chamber under well defined flow conditions. For this purpose, glass coverslips were coated with 20-30 'sg/cm2 of collagen types I and III by spraying a solution of these collagens with a retouching air brush. Platelet deposition increased with the time of perfusion. Adhesion to both collagen types was similar in the first 3 min, but increased platelet deposition occurred on collagen type III after 3 min due to thrombus formation. Adhesion at a shear rate of 800 s-' was strongly impaired with plasma of a patient with von Willebrand's disease or with fibronectin-free plasma. Addition of purified fibronectin to fibronectin-free plasma restored adhesion to the level obtained with normal plasma. Platelet deposition in normal plasma increased with increasing shear rates. Platelet deposition in VWD-plasma was normal at 490 s-', but there was no increase at higher shear rates. Platelet deposition in fibronectin-free plasma was diminished at all shear rates studied from 490 to 1,300 sO.Perfusion with a human albumin solution (HAS) to which purified Factor VIII-von Willebrand factor complex (FVIII-VWF) and fibronectin had been added gave similar platelet deposition as with normal plasma. Preincubation of collagen with FVIII-VWF and perfusion with HAS containing fibronectin, or, conversely, preincubation with fibronectin and perfusion with HAS containing FVIII-VWF, also resulted in adhesion similar to that observed in normal plasma. Similar adhesion was also observed after preincubation with both FVIII-VWF and fibronectin and subsequent perfusion with HAS alone. Sequential preincubations with first FVIII-VWF and then fibronectin, or with first fibronectin and then FVIII-VWF followed by perfusion with HAS, also gave a similar adhesion as observed with normal plasma.These data indicate that platelet adhesion to monomeric collagen types I and III is dependent on both FVIII-VWF and fibronectin. FVIII-VWF is only required at relatively high shear rates; fibronectin also at relatively low shear rates. Their Part of this work was presented at the IXth International Congress on Thrombosis and Haemostasis, Stockholm, Sweden, 1983, and has been published in abstract form in Thromb. Haemostasis, 50:1276.Address correspondence to Dr. Houdijk.Receivedfor publication 14 November 1983 and in revisedform 14 September 1984.complementary role in platelet adhesion suggests separate binding sites for FVIII-VWF and fibronectin on collagen.Platelet deposition on preformed fibrils of collagen types I and III was also studied. Initial adhesion expressed as percentage surface coverage was similar to that found with monomeric collagen, but thrombus formation was much enhanced.Adhesion on fibrillar collagen at 800 s-5 was impaired in VWD-plasma and fibronectin-free plasma, and was restored by addition of purified fibronectin to fibronectin-free plasma.When perfusions were performed with HAS, only addition of ...

Fibronectin in platelet adhesion to human collagen types I and III. Use of nonfibrillar and fibrillar collagen in flowing blood studies.

“…272829 We previously reported that nonfibrillar collagen is less reactive in promoting platelet adhesion under flow conditions than the fibrillar form and that type I is less reactive than type III. 7 The requirement of platelet deposition for fibronectin is most pronounced in the less reactive collagen types.…”

Propolypeptide and mature portions of von Willebrand factor of bovine origin recognize different sites on type‐I collagen obtained from bovine tendon

“…Collagen is particularly important for initiation of platelet activation leading to successful formation of a hemostatic plug [3]. Mature von Willebrand factor (m-vWF) of human origin is one of the adhesive glycoproteins believed to participate in collagen-induced platelet aggregation [4,51. It binds to both monomeric and fibrillar forms of type-I and type-I11 collagens in vitro, and its binding domain for collagen has been fairly well investigated [6 -91.…”

Axial dependence of platelet-collagen interactions in flowing blood. Upstream thrombus growth impairs downstream platelet adhesion.

“…12 Platelets adhere rapidly to the subendothelium and subsequently produce mural thrombi. The growth of these thrombi is reversible, and most of the aggregated platelets have disappeared within 20 minutes, apparently without affecting platelets adherent to the deendothelialized area.…”