Navegando por Palavras-chave "Plasmin"

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    BmTI-A, a Kunitz type inhibitor from Rhipicephalus microplus able to interfere in vessel formation
    (Elsevier Science Bv, 2016) Soares, Tatiane S. [UNIFESP]; Oliveira, Felipe [UNIFESP]; Torquato, Ricardo J. S. [UNIFESP]; Sasaki, Sergio D.; Araujo, Mariana S. [UNIFESP]; Paschoalin, Thaysa [UNIFESP]; Tanaka, Aparecida S. [UNIFESP]
    Rhipicephalus microplus is an ectoparasite responsible for transmissions of babesiosis and anaplasmosis causing large losses to livestock production. To survive R. microplus tick produces several active molecules, such as protease inhibitors. This ectoparasite has been described as a rich source of serine protease inhibitors most of them are Kunitz-BPTI members named BmTIs which have no clear function yet. In the present work, we described the expression and functional characterization of rBmTI-A which showed to be similar to the native BmTI-A, a double-headed Kunitz-BPTI inhibitor, capable to inhibit trypsin, human neutrophil elastase (HNE), human plasma kalikrein (HuPK) and human plasmin. rBmTI-A was able to cause a decrease of HUVEC cell viability. Besides, the rBmTI-A showed to be a potent inhibitor of "in vitro" vessel formation. Our results suggested that BmTI-A may participate in the blood acquisition process interfering in the vessel formation during the tick parasite life stage, around 20 days. In conclusion, BmTI-A is a promising molecule to be used in the drug design and development of new method of R. microplus control. (C) 2016 Elsevier B.V. All rights reserved.
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    Human tissue kallikreins 3 and 5 can act as plasminogen activator releasing active plasmin
    (Elsevier B.V., 2013-04-12) Souza, Lucas R. de; Melo, Pollyana Maria Saud [UNIFESP]; Paschoalin, Thaysa [UNIFESP]; Carmona, Adriana Karaoglanovic [UNIFESP]; Kondo, Marcia Yuri [UNIFESP]; Hirata, Izaura Yoshico [UNIFESP]; Blaber, Michael; Tersariol, Ivarne Luis dos Santos [UNIFESP]; Takatsuka, Joyce; Juliano, Maria Aparecida [UNIFESP]; Juliano, Luiz [UNIFESP]; Gomes, Roseli A.; Puzer, Luciano; Universidade Federal do ABC (UFABC); Universidade Federal de São Paulo (UNIFESP); Florida State Univ; Univ Mogi das Cruzes; Univ Fed Triangulo Mineiro
    Human tissue kallikreins (KLKs) are a group of serine proteases found in many tissues and biological fluids and are differentially expressed in several specific pathologies. Here, we present evidences of the ability of these enzymes to activate plasminogen. Kallikreins 3 and 5 were able to induce plasmin activity after hydrolyzing plasminogen, and we also verified that plasminogen activation was potentiated in the presence of glycosaminoglycans compared with plasminogen activation by tPA. This finding can shed new light on the plasminogen/plasmin system and its involvement in tumor metastasis, in which kallikreins appear to be upregulated. (C) 2013 Elsevier Inc. All rights reserved.
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    Plasmodium falciparum proteases hydrolyze plasminogen, generating angiostatin-like fragments
    (Elsevier B.V., 2014-01-01) Melo, Pollyana Maria Saud [UNIFESP]; Bagnaresi, Piero [UNIFESP]; Paschoalin, Thaysa [UNIFESP]; Hirata, Izaura Yoshico [UNIFESP]; Gazarini, Marcos Leoni [UNIFESP]; Carmona, Adriana Karaoglanovic [UNIFESP]; Universidade Federal de São Paulo (UNIFESP)
    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.