Lufaxin, a novel factor Xa inhibitor from the salivary gland of the sand fly lutzomyia longipalpis, blocks protease-activated receptor 2 activation and inhibits inflammation and thrombosis in vivo

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F12%3A00380194" target="_blank" >RIV/60077344:_____/12:00380194 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1161/ATVBAHA.112.253906" target="_blank" >http://dx.doi.org/10.1161/ATVBAHA.112.253906</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1161/ATVBAHA.112.253906" target="_blank" >10.1161/ATVBAHA.112.253906</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Lufaxin, a novel factor Xa inhibitor from the salivary gland of the sand fly lutzomyia longipalpis, blocks protease-activated receptor 2 activation and inhibits inflammation and thrombosis in vivo

Popis výsledku v původním jazyce

OBJECTIVE: Blood-sucking arthropods' salivary glands contain a remarkable diversity of antihemostatics. The aim of the present study was to identify the unique salivary anticoagulant of the sand fly Lutzomyia longipalpis, which remained elusive for decades. METHODS AND RESULTS: Several L. longipalpis salivary proteins were expressed in human embryonic kidney 293 cells and screened for inhibition of blood coagulation. A novel 32.4-kDa molecule, named Lufaxin, was identified as a slow, tight, noncompetitive, and reversible inhibitor of factor Xa (FXa). Notably, Lufaxin's primary sequence does not share similarity to any physiological or salivary inhibitors of coagulation reported to date. Lufaxin is specific for FXa and does not interact with FX, Dansyl-Glu-Gly-Arg-FXa, or 15 other enzymes. In addition, Lufaxin blocks prothrombinase and increases both prothrombin time and activated partial thromboplastin time. Surface plasmon resonance experiments revealed that FXa binds Lufaxin with an

Název v anglickém jazyce

Lufaxin, a novel factor Xa inhibitor from the salivary gland of the sand fly lutzomyia longipalpis, blocks protease-activated receptor 2 activation and inhibits inflammation and thrombosis in vivo

Popis výsledku anglicky

OBJECTIVE: Blood-sucking arthropods' salivary glands contain a remarkable diversity of antihemostatics. The aim of the present study was to identify the unique salivary anticoagulant of the sand fly Lutzomyia longipalpis, which remained elusive for decades. METHODS AND RESULTS: Several L. longipalpis salivary proteins were expressed in human embryonic kidney 293 cells and screened for inhibition of blood coagulation. A novel 32.4-kDa molecule, named Lufaxin, was identified as a slow, tight, noncompetitive, and reversible inhibitor of factor Xa (FXa). Notably, Lufaxin's primary sequence does not share similarity to any physiological or salivary inhibitors of coagulation reported to date. Lufaxin is specific for FXa and does not interact with FX, Dansyl-Glu-Gly-Arg-FXa, or 15 other enzymes. In addition, Lufaxin blocks prothrombinase and increases both prothrombin time and activated partial thromboplastin time. Surface plasmon resonance experiments revealed that FXa binds Lufaxin with an

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

—

Projekt

<a href="/cs/project/GAP502%2F12%2F2409" target="_blank" >GAP502/12/2409: Úloha inhibitorů proteáz z klíštěcích slin v interakcích mezi klíšťaty, patogeny a hostitelem</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2012

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Arteriosclerosis Thrombosis and Vascular Biology

ISSN

1079-5642

e-ISSN

—

Svazek periodika

32

Číslo periodika v rámci svazku

9

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

12

Strana od-do

2185-2198

Kód UT WoS článku

000307773100021

EID výsledku v databázi Scopus

—