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Titolo:
Factor VII and single-chain plasminogen activator-activating protease - Activation and autoactivation of the proenzyme
Autore:
Kannemeier, C; Feussner, A; Stohr, HA; Weisse, J; Preissner, KT; Romisch, J;
Indirizzi:
Univ Giessen, Fac Med, Inst Biochem, D-35392 Giessen, Germany Univ Giessen Giessen Germany D-35392 t Biochem, D-35392 Giessen, Germany Aventis Behring GmbH, Res, Marburg, Germany Aventis Behring GmbH MarburgGermany ehring GmbH, Res, Marburg, Germany
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 13, volume: 268, anno: 2001,
pagine: 3789 - 3796
SICI:
0014-2956(200107)268:13<3789:FVASPA>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
SERINE-PROTEASE; HUMAN PLASMA; FLUORESCENCE; PURIFICATION; THROMBIN; PHBP;
Keywords:
autocatalytic activation; factor VII-activating protease; plasma hyaluronan-binding protein; pro-urokinase; serine protease;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
19
Recensione:
Indirizzi per estratti:
Indirizzo: Preissner, KT Univ Giessen, Fac Med, Inst Biochem, Friedrichstr 24, D-35392 Giessen, Germany Univ Giessen Friedrichstr 24 Giessen Germany D-35392 ermany
Citazione:
C. Kannemeier et al., "Factor VII and single-chain plasminogen activator-activating protease - Activation and autoactivation of the proenzyme", EUR J BIOCH, 268(13), 2001, pp. 3789-3796

Abstract

Structural and biological characteristics of a recently described plasma serine protease, which displayed factor VII as well as pro-urokinase-activating properties in vitro, indicated a dual role for this factor VII-activating protease (FSAP) in hemostasis. Only the active protease (two-chain FSAP)has been isolated from plasma and from a prothrombin complex concentrate, whereas activators of the proenzyme have not been identified so far. After purification of the FSAP proenzyme from cryo-poor plasma by adsorption to an immobilized mAb and subsequent ion-exchange chromatography, activation togenerate two-chain FSAP was followed by a direct chromogenic assay as wellas by the ability of two-chain FSAP to activate prourokinase. purified single-chain FSAP underwent autoactivation leading to the typical protease two-chain pattern and subsequent degradation products, as demonstrated by Western-blotting analysis using a site-specific mAb. This autoactivation was significantly enhanced in the presence of heparin, whereas Ca2+ ions stabilized single-chain FSAP (the proenzyme) resulting in slower autoactivation kinetics. Correspondingly, the heparin-augmented reaction, which was associated with autodegradation particularly of the protease domain, was slowed downby co-incubation with Ca2+. Of the other proteases and cofactors tested, only urokinase (uPA) was able to generate the typical two-chain FSAP pattern. Studies with different forms of uPA suggest that the catalytic activity of pro-urokinase/uPA is needed to activate single-chain FSAP, indicating that it is the only hemostatic protease that can act as a physiological activator of FSAP.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 12:23:42