HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Veterinary Medicine / Faculty of Veterinary Medicine >
Peer-reviewed Journal Articles, etc >

Ayadualin, a novel RGD peptide with dual antihemostatic activities from the sand fly Lutzomyia ayacuchensis, a vector of Andean-type cutaneous leishmaniasis

This item is licensed under: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International

Files in This Item:
Biochimie_112p.49-56.pdf905.79 kBPDFView/Open
Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/60725

Title: Ayadualin, a novel RGD peptide with dual antihemostatic activities from the sand fly Lutzomyia ayacuchensis, a vector of Andean-type cutaneous leishmaniasis
Authors: Kato, Hirotomo Browse this author →KAKEN DB
Gomez, Eduardo A. Browse this author
Fujita, Megumi Browse this author
Ishimaru, Yuka Browse this author
Uezato, Hiroshi Browse this author →KAKEN DB
Mimori, Tatsuyuki Browse this author →KAKEN DB
Iwata, Hiroyuki Browse this author →KAKEN DB
Hashiguchi, Yoshihisa Browse this author →KAKEN DB
Keywords: RDG peptide
Sand fly
Saliva
Anticoagulant
Antiplatelet
Issue Date: May-2015
Publisher: Elsevier
Journal Title: Biochimie
Volume: 112
Start Page: 49
End Page: 56
Publisher DOI: 10.1016/j.biochi.2015.02.011
PMID: 25724270
Abstract: Sequence analysis of the Lutzomyia (Lu.) ayacuchensis salivary gland cDNA library identified a short peptide containing an RGD (Arg-Gly-Asp) sequence flanked by two cysteine residues in the C-terminal end as the most abundant transcript. In the present study, a recombinant protein of the RGD-containing peptide, designated ayadualin, was expressed in Escherichia colt and its activity was characterized. Ayadualin inhibited both collagen and ADP-induced platelet aggregations by interfering with the binding of integrin alpha(IIb)beta(3) to fibrinogen. The RGD sequence and cysteine residues located on both sides of the RGD sequence were essential for the inhibitory action. Moreover, ayadualin efficiently inhibited the intrinsic blood coagulation pathway irrespective of the RGD sequence. Measuring the enzymatic activity of coagulation factors using chromogenic substrates revealed that ayadualin efficiently inhibited factor XIIa (FXIIa) activity in a dose-dependent manner. In addition, pre-incubation of ayadualin with FXII inhibited FXIIa activity, while activated FXIIa was not affected by ayadualin, indicating that ayadualin inhibits the activation of FXII, but not enzymatic activity of FXIIa. These results indicated that ayadualin plays an important role in the blood feeding of Lu. ayacuchensis by inhibiting host hemostasis via dual mechanisms. (C) 2015 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved.
Rights: http://creativecommons.org/licenses/by-nc-nd/4.0/
Type: article (author version)
URI: http://hdl.handle.net/2115/60725
Appears in Collections:獣医学院・獣医学研究院 (Graduate School of Veterinary Medicine / Faculty of Veterinary Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 加藤 大智

Export metadata:

OAI-PMH ( junii2 , jpcoar )

MathJax is now OFF:


 

 - Hokkaido University