Navegando por Palavras-chave "Kunitz"

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    Bauhinia Kunitz-type proteinase inhibitors: structural characteristics and biological properties
    (Walter de Gruyter & Co, 2008-08-01) Oliva, Maria Luiza Vilela [UNIFESP]; Sampaio, Misako Uemura [UNIFESP]; Universidade Federal de São Paulo (UNIFESP)
    Plant proteinase inhibitors are involved in the regulation of the activity of many proteinases and, in consequence, in biological processes driven by proteolysis. in this review, we summarize recent results on the activity of native Bauhinia inhibitors and synthetic derivatives. Structural and functional characteristics and the potential therapeutic use of these inhibitors are also discussed.
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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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    rBmTI-6, a Kunitz-BPTI domain protease inhibitor from the tick Boophilus microplus, its cloning, expression and biochemical characterization
    (Elsevier B.V., 2008-08-01) Sasaki, Sergio D.; Tanaka, Aparecida S. [UNIFESP]; Universidade Federal de São Paulo (UNIFESP); Universidade Federal do ABC (UFABC)
    Boophilus microplus is a rich source of trypsin inhibitors, numerous Kunitz-BPTI (bovine pancreatic trypsin inhibitor) inhibitors have been described from larvae and eggs, named BmTIs. Among them, were characterized inhibitors for trypsin, human neutrophil elastase, human plasma kallikrein and plasmin. BmTIs elicited a protective immunological response against B. microplus infestation in cattle. However, only a small amount of purified natural BmTIs can be obtained from larvae and eggs by chromatographic methods, thus if BmTIs are to be used as vaccine antigens (immunogens) the production of recombinant BmTIs (rBmTIs) is essential. in this work we describe the cloning, expression, purification and characterization of rBmTI-6. rBmTI-6 is a three-headed Kunitz-BPTI inhibitor, expressed in the Pichia pastoris system. Although rBmTI-6 was processed by proteases and glycosylated during the expression process, these post-translational modifications did not alter the ability of rBmTI-6 to inhibit protease activity. Purified rBmTI-6 inhibited trypsin and plasmin. (C) 2008 Elsevier B.V. All rights reserved.