1986•Cold Spring Harbor Symposia on Quantitative BiologyRequires access

Isolation and Expression of cDNAs Encoding Human Factor VII

Kathleen L. Berkner, S. Busby, Earl W. Davie, Charles Edward Hart, M Y Insley, Walter Kisiel, A. Kumar, Mark J. Murray, Patrick J. O’Hara, Richard G. Woodbury, Frederick S. Hagen

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Abstract

Two alternative pathways exist for the activation of factor X, a step required to convert prothrombin to thrombin in the later stages of the coagulation cascade. In the intrinsic pathway of blood coagulation, a series of protease-mediated activations ultimately generates factor IXa (see Fig. 1). This protein, coupled with factor VIIIa, produces factor Xa from factor X by cleavage of a glycopeptide from the heavy-chain amino terminus (Davie et al. 1979). An identical proteolysis is effected by factor VIIa and tissue factor in the extrinsic pathway of blood coagulation. Tissue factor, a membrane-bound protein, normally does not circulate in plasma. Upon vessel disruption, however, it can complex with factor VIIa to catalyze the factor X activation in a Ca++- and phospholipid-dependent manner (Østerud and Rapaport 1977).

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Two alternative pathways exist for the activation of factor X, a step required to convert prothrombin to thrombin in the later stages of the coagulation cascade. In the intrinsic pathway of blood coagulation, a series of protease-mediated activations ultimately generates factor IXa (see Fig. 1). This protein, coupled with factor VIIIa, produces factor Xa from factor X by cleavage of a glycopeptide from the heavy-chain amino terminus (Davie et al. 1979). An identical proteolysis is effected by factor VIIa and tissue factor in the extrinsic pathway of blood coagulation. Tissue factor, a membrane-bound protein, normally does not circulate in plasma. Upon vessel disruption, however, it can complex with factor VIIa to catalyze the factor X activation in a Ca++- and phospholipid-dependent manner (Østerud and Rapaport 1977).

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Available abstract

Two alternative pathways exist for the activation of factor X, a step required to convert prothrombin to thrombin in the later stages of the coagulation cascade. In the intrinsic pathway of blood coagulation, a series of protease-mediated activations ultimately generates factor IXa (see Fig. 1). This protein, coupled with factor VIIIa, produces factor Xa from factor X by cleavage of a glycopeptide from the heavy-chain amino terminus (Davie et al. 1979). An identical proteolysis is effected by factor VIIa and tissue factor in the extrinsic pathway of blood coagulation. Tissue factor, a membrane-bound protein, normally does not circulate in plasma. Upon vessel disruption, however, it can complex with factor VIIa to catalyze the factor X activation in a Ca++- and phospholipid-dependent manner (Østerud and Rapaport 1977).

Key concepts: Tissue factor, Factor X, Factor IXa, Proteolysis, Thrombin, Factor V, Chemistry, Prothrombinase

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