Immunologic differentiation of classic hemophilia (factor VIII deficiency) and von Willebrand's disease

Zimmerman, Theodore S.; Ratnoff, Oscar D.; Powell, Arnold E.

doi:10.1172/jci106480

Cited by 645 publications

(151 citation statements)

References 22 publications

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“…Patients with von Willebrand's disease have long bleeding times and decreased platelet retention in glass bead columns (6). This disease is associated with reduced Factor VIII procoagulant activity and a decrease in the amount of circulating Factor VIII protein, determined immunologically (7).…”

Section: Introductionmentioning

confidence: 99%

The interaction of bovine factor VIII with human platelets.

Kirby¹,

Mills²

1975

J. Clin. Invest.

104

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A B S T R A C T Treatment of human platelets with purified bovine Factor VIII caused three types of aggregation: (a) primary agglutination; (b) secondary aggregation involving the platelet release reaction; and (c) super-aggregation, in which the platelets were gathered into only a few large clumps. Removal of calcium ions or treatment with p-hydroxymercuriphenyl sulfonate blocked the release reaction, but not primary agglutination or super-aggregation. Platelets treated with formalin were not aggregated by ADP, thrombin, or collagen, but were agglutinated by bovine Factor VIII, although they did not show super-aggregation. Formalin-treated platelets were agglutinated by phytohemagglutinin P less extensively and less rapidly than by bovine Factor VIII. Treatment of platelets and Factor VIII with neuraminidase released 60 and 53%, respectively, of the sialic acid residues without affecting the agglutination reaction or the procoagulant activity of the Factor VIII. Agglutination was inhibited by high salt concentrations, dextran sulfate, and heparin. During agglutination, both the procoagulant and platelet-agglutinating activities of Factor VIII became bound to the platelet surface.

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Section: Introductionmentioning

confidence: 99%

The interaction of bovine factor VIII with human platelets.

Kirby¹,

Mills²

1975

J. Clin. Invest.

104

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“…The present investigation relates to an earlier collaborative study in which the levels of FVIII-RA in normal, VWD, and hemophilic dogs were determined independently in our two laboratories (Z-3,6), using the Laurel1 electroimmunoassay (1). Initial results in our laboratory indicated that the plasma from 14 German shepherds with moderate VWD had an average of 48.1 f 6.5% FVIII-RA and 41.5 * 22.4% factor VIII activity, whereas plasma from seven different canine strains of severe hemophilia A had 127 f 45% FVIII-RA and cl% factor VIII activity (2,3).…”

Section: Introductionmentioning

confidence: 99%

Factor VIII-related antigen in canine hemophilia and von Willebrand's disease: Variation when measured with different agaroses

Benson

Bouma²,

Dodds

1975

Thrombosis Research

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“…Assays for activated factors were performed in 10 X 75 mm polystyrene tubes without the addition of kaolin. One unit of activity was arbitrarily defined as that amount present in 1 ml of a standard pooled plasma (18).…”

Section: Methodsmentioning

confidence: 99%

Inhibitory spectrum of alpha 2-plasmin inhibitor.

Saito¹,

Goldsmith²,

Moroi³

et al. 1979

Proc. Natl. Acad. Sci. U.S.A.

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ABSTRACTarPlasmin inhibitor (a2PI) has been recently characterized as a fast-reacting inhibitor of plasmin in human plasma and appears to play an important role in the regulation of fibrinolysis in vivo. We have studied the effect of purified a2PI upon various proteases participating in human blood coagulation and kinin generation. At physiological concentration (50 ;sg/ml), a2PI inhibited the clot-promoting and prekallikrein-activating activity of Hageman factor fragments, the amidolytic, kininogenase, and clot-promoting activities of plasma kallikrein, and the clot-promoting properties of activated plasma thromboplastin antecedent (PTA, Factor XIa) and thrombin. a2PI had minimal inhibitory effect on surface-bound activated PTA and activated Stuart factor (Factor Xa). a2PI did not inhibit the activity of activated Christmas factor (Factor IXa) or urinary kallikrein. Heparin (1.5-2.0 units/ml) did not enhance the inhibitory function of a2PI. These results suggest that, like other plasma protease inhibitors, a2PI possesses a broad in vitro spectrum of inhibitory properties.a2-Plasmin inhibitor (a2PI) has been recently identified as a fast-reacting inhibitor of plasmin in human plasma (1-3). a2PI has strong inhibitory activity against plasmin and is the first inhibitor that reacts with plasmin, whether plasminogen activation occurs in vitro or in vivo (4-6).Although the action of a2PI on plasmin is well characterized, relatively little information is available about the effect of this newly isolated inhibitor upon other plasma proteases (7,8). This paper reports the effect of physiologic concentrations of a2PI upon various proteases participating in blood coagulation and kinin generation and defines the in vitro spectrum of this inhibitor. We also compare the action of a2PI with that of some other plasma protease inhibitors in these systems. MATERIALS AND METHODSInhibitors. Human a2PI was prepared as described (1) and was judged greater than 95% homogeneous on disc gel electrophoresis, sodium dodecyl sulfate gel electrophoresis, and immunoelectrophoresis. The concentration of purified a2PI was determined by using 7.03 as extinction coefficient El% at 280 um. a2-Macroglobulin (a2M), isolated from human plasma (9), gave a single band by sodium dodecyl sulfate gel electrophoresis after reduction with 2-mercaptoethanol (Mr, approximately 180,000). The concentration of a2M was determined by single radial immunodiffusion on Immuno-plates (Hyland, Costa Mesa, CA). Normal serum contains approximately 2 mg of a2M per ml. a2M at 2 mg/ml was essentially free of a2PI (<0.2 ,g/ml) when tested by a sensitive radioitnmunoassay for a2PI (unpublished data). a2M (8 mg/ml) contained no detectable C1 esterase inhibitor (Clinh), a1-antitrypsin, or antithrombin III as assayed by immunodiffusion using monospecific antiserum. Purified Clinh and monospecific antiserum against Clinh were generous gifts of J. Pensky

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Immunologic differentiation of classic hemophilia (factor VIII deficiency) and von Willebrand's disease

Cited by 645 publications

References 22 publications

The interaction of bovine factor VIII with human platelets.

The interaction of bovine factor VIII with human platelets.

Factor VIII-related antigen in canine hemophilia and von Willebrand's disease: Variation when measured with different agaroses

Inhibitory spectrum of alpha 2-plasmin inhibitor.

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