PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 7942503

Treating hemophilia.

C W Peterson
View original source ↗Export metadata ↓

Abstract

Hemophilias A and B are inherited disorders of clotting-factor production that are characterized by low levels of factor VIII- or IX-coagulant activity. The clinical course of patients with hemophilia is marked by episodes of hemorrhage, some spontaneous and some related to trauma or medical procedures. The physical well-being of patients with hemophilia is maintained by the prevention of bleeding when possible and by prompt, effective treatment of bleeding when it occurs. Factor-replacement therapy continues to be the mainstay of hemophilia treatment, but like pharmacotherapy for other disease states, it is most effective when provided within the framework of a well-designed, individualized therapeutic plan. Currently available factor concentrates have a much greater safety profile than older products, but they are not free of adverse effects. Patients with inhibitors continue to present a challenge in restoring hemostasis. Pharmacists can play an important role in the pharmaceutical care of patients with hemophilia.

Explore related subjects

Antifibrinolytic AgentsDeamino Arginine VasopressinFactor VIIIHemophilia AHemophilia BHumansComparative StudyJournal ArticleReview

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

C W Peterson. 1994. Treating hemophilia.. https://doi.org/10.1016/s0160-3450(15)30341-x

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2007

A variant of recombinant factor VIIa with enhanced procoagulant and antifibrinolytic activities in an in vitro model of hemophilia.

OBJECTIVE: Recombinant factor VIIa (rFVIIa, NovoSeven) has proven efficacy in treating bleeding in hemophilia patients with inhibitors. A rFVIIa analog with mutations V158D/E296V/M298Q (NN1731) exhibits increased procoagulant activity in in vitro and in vivo models. The aim of this work was to define the effects of NN1731 toward factor X activation, platelet activation, thrombin generation, and fibrin clot formation and stability. METHODS AND RESULTS: In a cell-based in vitro model of hemophilia, rFVIIa and NN1731 similarly increased factor X activation on tissue factor-bearing cells; however, NN1731 exhibited 30-fold higher factor Xa generation on platelets than similar rFVIIa concentrations. NN1731-mediated thrombin generation depended on platelet activation, but NN1731 did not directly activate platelets. NN1731 produced 4- to 10-fold higher maximal thrombin generation rates than equal rFVIIa concentrations. Both rFVIIa and NN1731 shortened clotting times in the absence of factors IX and VIII; however, NN1731 did so at 50-fold lower concentrations than were required of rFVIIa. In fibrinolytic conditions, both rFVIIa and NN1731 increased fibrin formation and stability; however, NN1731 was effective at 50-fold lower concentrations than were required of rFVIIa. CONCLUSIONS: By increasing factor Xa generation, NN1731 promotes the formation of thrombin and a stable clot to a greater degree than rFVIIa.

Antifibrinolytic Agents↗
PubMed2006

BcSAK1, a stress-activated mitogen-activated protein kinase, is involved in vegetative differentiation and pathogenicity in Botrytis cinerea.

The gene bcsak1, encoding a mitogen-activated protein kinase (MAPK) of Botrytis cinerea, was cloned and characterized. The protein has high homology to the yeast Hog1 and to corresponding MAPKs from filamentous fungi, but it shows unique functional features. The protein is phosphorylated under osmotic stress, specific fungicides, and oxidative stress mediated by H(2)O(2) and menadione. Northern blot analyses indicate that only a subset of typical oxidative stress response genes is regulated by BcSAK1. In contrast to most other fungal systems, Deltabcsak1 mutants are significantly impaired in vegetative and pathogenic development: they are blocked in conidia formation, show increased sclerotial development, and are unable to penetrate unwounded plant tissue. These data indicate that in B. cinerea the stress-activated MAPK cascade is involved in essential differentiation programs.

Antifibrinolytic Agents↗