| Full text | |
| Author(s): |
Melo, Pollyana M. S.
[1]
;
Bagnaresi, Piero
[1]
;
Paschoalin, Thaysa
[2]
;
Hirata, Izaura Y.
[1]
;
Gazarini, Marcos L.
[3]
;
Carmona, Adriana K.
[1]
Total Authors: 6
|
| Affiliation: | [1] Univ Fed Sao Paulo, Dept Biofis, BR-04039032 Sao Paulo - Brazil
[2] Univ Fed Sao Paulo, Dept Microbiol Imunol & Parasitol, BR-04023062 Sao Paulo - Brazil
[3] Univ Fed Sao Paulo, Dept Biociencias, BR-11060001 Santos, SP - Brazil
Total Affiliations: 3
|
| Document type: | Journal article |
| Source: | Molecular and Biochemical Parasitology; v. 193, n. 1, p. 45-54, JAN 2014. |
| Web of Science Citations: | 4 |
| Abstract | |
Malaria is a disease caused by Plasmodium parasites and remains one of the most prevalent and persistent maladies, affecting hundreds of millions of people. In the present work, we evaluated the capability of Plasmodium falciparum proteases to hydrolyze the multifunctional protein plasminogen, which is implicated in angiogenesis and coagulation processes by the generation of angiostatin and plasmin, respectively. Using fluorescence microscopy, we visualized the internalization of FITC-labeled plasminogen in erythrocytes infected by P. falciparum and showed that the parasites are able to hydrolyze the protein. The cleavage of plasminogen by the P. falciparum proteases was also observed by SDS-PAGE, followed by immunoblotting with anti-angiostatin antibody. N-terminal sequencing of the main generated fragments indicated that they are comprised in the five plasminogen kringle domains, suggesting as being angiostatin-like peptides. This assumption was reinforced by the demonstration that the products of plasminogen processing mimic angiostatin functions, including the capability to inhibit angiogenesis and to stimulate calcium response in endothelial cells in vitro. However, no plasmin activity was detected after plasminogen hydrolysis by P. falciparum. Nonetheless, exogenous tissue plasminogen activator (tPA) activated plasmin in infected erythrocytes, suggesting that the uptake of plasminogen by P. falciparum may be modulated by the vertebrate host. Taken together, the data presented here provide evidence for the processing of host plasminogen by malaria parasites to generate active fragments that may modulate host physiology events during malaria infection. (C) 2014 Elsevier B.V. All rights reserved. (AU) | |
| FAPESP's process: | 10/51423-0 - Bioactive peptides and peptidases: biological and immunobiological activities in infectious diseases and cancer |
| Grantee: | Luiz Rodolpho Raja Gabaglia Travassos |
| Support Opportunities: | Research Projects - Thematic Grants |
| FAPESP's process: | 09/11261-4 - Study of action of proteases of Plasmodium falciparum in the parasite-host relationship |
| Grantee: | Piero Bagnaresi |
| Support Opportunities: | Scholarships in Brazil - Post-Doctoral |
| FAPESP's process: | 09/53840-0 - Fluorescence system for investigations of physiological and pathophysiological aspects in cellular models |
| Grantee: | Adriana Karaoglanovic Carmona |
| Support Opportunities: | Multi-user Equipment Program |