Effect of fibronectin and von willebrand factor on the adhesion of human fixed washed platelets to collagen immobilized beads

Aihara, Morio; Takami, Hideki; Sawada, Yukimasa; Morimoto, Shigeo; Kariya, Katsutoshi; Kudo, Ikuo; Ueno, Kayo; Kimura, Asano; Yoshida, Yutaka

doi:10.1016/0049-3848(86)90167-2

Cited by 9 publications

(7 citation statements)

References 17 publications

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“…FWP adhered to collagen in the absence of any agonist and the binding capacity of FWP was stable for more than a year when FWP were stored at 4° C. The adhesion was increased by NHP or purified vWF as previously described (10,11). The degree of adhesion, expressed as the total increase in light transmission, was reduced by increasing ionic strength and abolished at a final ionic strength of 0.3 (data nof shown).…”

Section: Fwp Adhesionsupporting

confidence: 53%

“…Correspondence to: Morio Aihara, M.D., The First Department of Internal Medicine, Hirosaki University School of Medicine, S Zaifu-cho, Hirosaki 036, Japan presence or absence of von Willebrand factor (vWF). However, the rate of FWP adhesion to collagen is increased dose-dependently by the addition of vWF as normal plasma or in a purified system (9)(10)(11). Perret et al (12) reported that agglutination of human FWP by fibrillar collagen is dependent on vWF (collagen cofactor; CCo).…”

Section: Introductionmentioning

confidence: 99%

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Glycoprotein Ib Has a Partial Role in Platelet-von Willebrand Factor Collagen Interaction

et al. 1988

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SummaryThe adhesion of human fixed washed platelets (FWP) to collagen was decreased after treatment with Serratia marcescens protease (SP), which removed 95% of the glycocalicin from platelet membrane glycoprotein (GP) lb. However, the diminished adhesion of SP treated FWP to collagen could still be increased in the presence of purified von Willebrand factor (vWF). This ability of vWF to increase FWP adhesion to collagen is defined as collagen cofactor (CCo). The adhesion of FWP to collagen was not affected by a monoclonal antibody (MAb) to GP Ilb/IIIa (10E5), that inhibits ADP and collagen induced platelet aggregation. On the other hand, it was decreased by 50% by a MAb to GP lb (6D1), that inhibits ristocetin induced platelet aggregation. Adhesion of FWP in buffer to collagen was completely inhibited by Ricinus communis agglutinin I or concanavalin A, while Lens culinalis agglutinin and wheat germ agglutinin showed 50% inhibition. The FWP adhesion to collagen in the presence of vWF (normal plasma) was unaffected by MAbs to GP Ilb/IIIa (10E5, P2, HPL1) but was decreased to 32-38% by MAbs to GP lb (6D1, AN51, HPL11). A MAb to vWF (CLB-RAg 35), that inhibits ristocetin induced binding of vWF to platelets, decreased the CCo of normal plasma by 70%. The MAb, CLB-RAg 201, that inhibits the binding of vWF to collagen, completely inhibited the CCo of normal plasma. In conclusion, our data suggest that (1) GP lb has a partial role in FWP adhesion to collagen; (2) the binding of vWF to collagen is required for the expression of CCo; (3) CCo is partly mediated through GP lb; but (4) other platelet membrane protein(s) besides GP lb or GP Ilb/IIIa must also be involved in FWP-vWF-collagen interactions.

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Section: Fwp Adhesionsupporting

confidence: 53%

Section: Introductionmentioning

confidence: 99%

Glycoprotein Ib Has a Partial Role in Platelet-von Willebrand Factor Collagen Interaction

et al. 1988

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“…To prepare collagen coated glass beads, 5 ml of the collagen in distilled water (250-2,OOO,ug/ml) was added by 1.0 ml of 0.1 M ammonium bicarbonate in a plastic box. Fifteen grams of glass beads (0.3-0.4 mm in diameter, Eiken, Tokyo) were then added to the collagen solution and the mixture was vacuum dried overnight at room temperature (Aihara et al 1986). …”

Section: Methodsmentioning

confidence: 99%

“…Saito et al (1986) have reported that bovine factor XIII (FXIII) may be a platelet receptor for collagen. We have previously described that the adhesion of human fixed washed platelets (FWP) to the fibrillar collagen is affected by plasma adhesive proteins such as von Willebrand factor or fibronectin (Aihara et al 1986) and platelet membrane glycoprotein Ib has a partial role in this interaction (Aihara et al 1988).…”

mentioning

confidence: 99%

Factor XIII is not involved in human platelet-collagen interaction.

Aihara

Sawada

Takami

et al. 1989

Tohoku J. Exp. Med.

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A. and YOSHIDA, Y. Factor XIII is Not Involved in Human Platelet-Collagen Interaction. Tohoku J. Exp. Med., 1989, 159 (1), [37][38][39][40][41][42][43][44] A role of factor XIII (FXIII) on the interaction of human platelets with collagen was investigated using either formaldehyde fixed-washed platelets (FWP) or nonfixed platelets. The adhesion of FWP to bovine type I collagen was measured by using either an aggregometer or a collagen immobilized glass beads column. The interaction of non-fixed human platelets with collagen was measured with in vitro bleeding time (Thrombostat-4,000), which was performed by passing citrated whole blood through the filter covered with rat type I collagen under the constant shear stress. FWP adhesion to the collagen immobilized column (1,300 p g collagen) was not changed by the addition of commercial FXIII preparation (Fibrogammin) ; the adhesion was 42.7% in the presence of 1% human serum albumin, 42-43% in the presence of 1-2 U/ml of FXIII. The addition of rabbit antibody to FXIII to normal FWP did not change the degree of a dhesion ; 42.3% (1:100 anti-FXIII) and 46.1% (normal rabbit serum). Furthermore, platelets from the patient with congenital FXIII deficiency normally aggregated by bovine collagen and the adhesion of the patient FWP to the collagen was similar to that of normal FWP. Prolongation of partial thromboplastin time and the changes of thromboelastograph of normal plasma were observed after mixing with the collagen, and factor VIII, FXIII and von Willebrand factor were adsorbed by the collagen. The amount of FXIII in normal human plasma bound to collagen was 17, 23 and 54% at the concentration of the collagen 250, 500 and 1,000 p g/ml, respectively. The binding of plasma ristocetin cofactor was not different between normal control and the patient with FXIII deficiency. These data suggest that FXIII is not involved in human platelet interaction with the type I collagen, while FXIII in normal human plasma binds to the collagen. platelet ; collagen ; factor XIII and factor XIII deficiency

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“…vWF interacts with several components such as platelet glycoprotein (GP) Ib, GP IIb/IIIa, collagen or extracellular matrices and heparin (Ruggeri et al 1982; Santoro and Cowan 1982;Coller et al 1983;Wagner et al 1984 ;Fujimura et al 1987). Previous experiments have shown that large multimers of vWF antigen (vWF : Ag) preferentially bind to fibrillar collagen in suspension (Santoro 1983; Aihara et al 1984), and increase the adhesion of human fixed washed platelets (FWP) to fibrillar collagen (Aihara et al 1986). Recently, the agglutination of FWP by collagen is dependent on vWF and the biological activity of vWF is terminated as collagen cofactor (CCo) (Perret et al 1985).…”

mentioning

confidence: 99%

Two affinity immunoelectrophoretic methods for studying collagen interaction with von Willebrand factor antigen.

Aihara

Kudo

Ishigaki

et al. 1987

Tohoku J. Exp. Med.

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Effect of fibronectin and von willebrand factor on the adhesion of human fixed washed platelets to collagen immobilized beads

Cited by 9 publications

References 17 publications

Glycoprotein Ib Has a Partial Role in Platelet-von Willebrand Factor Collagen Interaction

Glycoprotein Ib Has a Partial Role in Platelet-von Willebrand Factor Collagen Interaction

Factor XIII is not involved in human platelet-collagen interaction.

Two affinity immunoelectrophoretic methods for studying collagen interaction with von Willebrand factor antigen.

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