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Atick salivary protein targets cathepsin G and chymase and inhibits host inflammation and platelet aggregation

SYSNO ASEP	0358349
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	Atick salivary protein targets cathepsin G and chymase and inhibits host inflammation and platelet aggregation
Author(s)	Chmelař, Jindřich (BC-A) Oliveira, C. J. (BR) Řezáčová, Pavlína (UOCHB-X)_{RID, ORCID} Francischetti, I.M.B. (US) Kovářová, Zuzana (UOCHB-X)_{RID, ORCID} Pejler, G. (SE) Kopáček, Petr (BC-A)_{RID, ORCID} Ribeiro, J.M.C. (US) Mareš, Michael (UOCHB-X)_{RID, ORCID} Kopecký, Jan (BC-A)_RID Kotsyfakis, Michalis (BC-A)_{RID, ORCID}
Source Title	Blood. - : American Society of Hematology - ISSN 0006-4971 Roč. 117, č. 2 (2011), s. 736-744
Number of pages	10 s.
Language	eng - English
Country	US - United States
Keywords	parasite serpin ; IRS-2 ; tick ; Ixodes ricinus ; platelet aggregation ; inflammation ; cathepsin G ; chymase
Subject RIV	EC - Immunology
R&D Projects	IAA600960811 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR)
	LC06009 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
	GAP207/10/2183 GA ČR - Czech Science Foundation (CSF)
CEZ	AV0Z60220518 - PAU-O, BC-A (2005-2011)
	AV0Z40550506 - UOCHB-X (2005-2011)
UT WOS	000286178700045
DOI	10.1182/blood-2010-06-293241
Annotation	A protein with antiinflammatory and anti-platelet effect was identified. It was named IRS-2 (Ixodes ricinus serpin – 2). It belongs into the group of serpins – inhibitors of serine proteases and the mode of action of IRS-2 derives from its inhibitory activity against cathepsin G and mast cell chymase. Antiinflammatory activity was shown using paw edema experiment with mice. IRS-2 inhibited specifically only cathepsin G and thrombin induced platelet aggregation.
Workplace	Biology Centre (since 2006)
Contact	Dana Hypšová, eje@eje.cz, Tel.: 387 775 214
Year of Publishing	2012

Number of the records: 1