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Observational Patient Diary Study of Treatment Doses for Patients With Haemophilia With Inhibitors to Factors VIII and IX

2014-08-27 03:29:15 | BioPortfolio

Summary

This study is conducted in the United States of America (USA). The aim of this study is to investigate the at-home-administration of bypassing agents for treatment of bleeding episodes in patients with congenital haemophilia with inhibitors to factors VIII and IX. We are further investigating how bleeding episodes affect the quality of life of the patient and their family or caregivers

Study Design

Observational Model: Case-Only, Time Perspective: Prospective

Conditions

Haemophilia A

Intervention

activated recombinant human factor VII, Feiba VH

Location

Novo Nordisk Clinical Trial Call Center
Princeton
New Jersey
United States
08540

Status

Completed

Source

Novo Nordisk

Results (where available)

View Results

Links

Published on BioPortfolio: 2014-08-27T03:29:15-0400

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Medical and Biotech [MESH] Definitions

Activated form of factor XI. In the intrinsic pathway, Factor XI is activated to XIa by factor XIIa in the presence of cofactor HMWK; (HIGH MOLECULAR WEIGHT KININOGEN). Factor XIa then activates factor IX to factor IXa in the presence of calcium.

A hemostatic disorder characterized by a poor anticoagulant response to activated protein C (APC). The activated form of Factor V (Factor Va) is more slowly degraded by activated protein C. Factor V Leiden mutation (R506Q) is the most common cause of APC resistance.

Heat- and storage-stable plasma protein that is activated by tissue thromboplastin to form factor VIIa in the extrinsic pathway of blood coagulation. The activated form then catalyzes the activation of factor X to factor Xa.

Storage-stable blood coagulation factor acting in the intrinsic pathway. Its activated form, IXa, forms a complex with factor VIII and calcium on platelet factor 3 to activate factor X to Xa. Deficiency of factor IX results in HEMOPHILIA B (Christmas Disease).

Activated form of factor VIII. The B-domain of factor VIII is proteolytically cleaved by thrombin to form factor VIIIa. Factor VIIIa exists as a non-covalent dimer in a metal-linked (probably calcium) complex and functions as a cofactor in the enzymatic activation of factor X by factor IXa. Factor VIIIa is similar in structure and generation to factor Va.

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