Advanced search
Start date
Betweenand
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

A novel trypsin Kazal-type inhibitor from Aedes aegypti with thrombin coagulant inhibitory activity

Full text
Author(s):
Watanabe, Renata M. O. [1] ; Soares, Tatiane S. [1] ; Morais-Zani, Karen [2] ; Tanaka-Azevedo, Anita M. [2] ; Maciel, Ceres [3] ; Capurro, Margareth L. [3] ; Torquato, Ricardo J. S. [1] ; Tanaka, Aparecida S. [1]
Total Authors: 8
Affiliation:
[1] UNIFESP EPM, Dept Bioquim, BR-04044020 Sao Paulo - Brazil
[2] Inst Butantan, Lab Fisiopatol, BR-05503900 Sao Paulo - Brazil
[3] Univ Sao Paulo, Dept Parasitol, Inst Ciencias Biomed, BR-05508900 Sao Paulo - Brazil
Total Affiliations: 3
Document type: Journal article
Source: Biochimie; v. 92, n. 8, p. 933-939, AUG 2010.
Web of Science Citations: 20
Abstract

Kazal-type inhibitors play several important roles in invertebrates, such as anticoagulant, vasodilator and antimicrobial activities. Putative Kazal-type inhibitors were described in several insect transcriptomes. In this paper we characterized for the first time a Kazal unique domain trypsin inhibitor from the Aedes aegypti mosquito. Previously, analyses of sialotranscriptome of A. aegypti showed the potential presence of a Kazal-type serine protease inhibitor, in female salivary glands, carcass and also in whole male, which we named AaTI (A. aegypti trypsin inhibitor). AaTI sequence showed amino acid sequence similarity with insect thrombin inhibitors, serine protease inhibitor from Litopenaeus vannamei hemocytes and tryptase inhibitor from leech Hirudo medicinalis (LDTI). In this work we expressed, purified and characterized the recombinant AaTI (rAaTI). Molecular weight of purified rAaTI was 7 kDa rAaTI presented dissociation constant (K(i)) of 0.15 and 3.8 nM toward trypsin and plasmin, respectively, and it weakly inhibited thrombin amidolytic activity. The rAaTI was also able to prolong prothrombin time, activated partial thromboplastin time and thrombin time. AaTI transcription was confirmed in A. aegypti female salivary gland and gut 3 h and 24 h after blood feeding, suggesting that this molecule can act as anticoagulant during the feeding and digestive processes. Its transcription in larvae and pupae suggested that AaTI may also play other functions during the mosquito's development. (C) 2010 Elsevier Masson SAS. All rights reserved. (AU)

FAPESP's process: 05/03514-9 - Studies of the physiological function and biotechnological potential of protease inhibitors and anti-hemostatics in hematophagous arthropods
Grantee:Aparecida Sadae Tanaka
Support Opportunities: Research Projects - Thematic Grants