Effect of invertebrate serine proteinase inhibitors on carrageenan-induced pleural exudation and bradykinin release

Malavazi-Piza, Kelly C; Araújo, Magali; Godinho, Rosely Oliveira; Tanaka, Aparecida S.

doi:10.1016/j.intimp.2004.06.004

Cited by 4 publications

(1 citation statement)

References 43 publications

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“…The kinin extraction from BALF, plasma, or lung was performed according to the method described by Shimamoto et al, 1988 [28], with some modifications [29]. A cocktail of protease inhibitors (24 µ M SBTI, 10 μ M lisinopril, 10 mM EDTA, 100 μ M TPCK, 10 μ M E-64, 5.0 mM o-phenanthroline, 1.0 mM AEBSF, and 9.0 μ M aprotinin) was added to BALF, plasma, or lungs, and samples were centrifuged at 950 ×g for 15 min at 4°C.…”

Section: Methodsmentioning

confidence: 99%

Protease Inhibitors Extracted fromCaesalpinia echinataLam. Affect Kinin Release during Lung Inflammation

et al. 2016

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Inflammation is an essential process in many pulmonary diseases in which kinins are generated by protease action on kininogen, a phenomenon that is blocked by protease inhibitors. We evaluated kinin release in an in vivo lung inflammation model in rats, in the presence or absence of CeKI (C. echinata kallikrein inhibitor), a plasma kallikrein, cathepsin G, and proteinase-3 inhibitor, and rCeEI (recombinant C. echinata elastase inhibitor), which inhibits these proteases and also neutrophil elastase. Wistar rats were intravenously treated with buffer (negative control) or inhibitors and, subsequently, lipopolysaccharide was injected into their lungs. Blood, bronchoalveolar lavage fluid (BALF), and lung tissue were collected. In plasma, kinin release was higher in the LPS-treated animals in comparison to CeKI or rCeEI groups. rCeEI-treated animals presented less kinin than CeKI-treated group. Our data suggest that kinins play a pivotal role in lung inflammation and may be generated by different enzymes; however, neutrophil elastase seems to be the most important in the lung tissue context. These results open perspectives for a better understanding of biological process where neutrophil enzymes participate and indicate these plant inhibitors and their recombinant correlates for therapeutic trials involving pulmonary diseases.

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Section: Methodsmentioning

confidence: 99%

Protease Inhibitors Extracted fromCaesalpinia echinataLam. Affect Kinin Release during Lung Inflammation

et al. 2016

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Invertebrate trypsins: a review

Sánchez‐Paz²,

2008

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Food protein hydrolysis, a crucial step in digestion, is catalyzed by trypsin enzymes from the digestive apparatus of invertebrates. Trypsin appeared early in evolution and occurs in all phyla and, in the digestive systems of invertebrates, it became the most abundant proteinase. As in vertebrates, invertebrate trypsin is also present in several forms (isoenzymes). Its physiological importance in food protein digestion in several invertebrate species has emerged with compelling evidence; and several other physiological functions, such as regulation of digestive functions, are now settled. Recent advances in the knowledge of invertebrate trypsin synthesis, regulation, genetics, catalytic characteristics; structure, evolution, as well as inhibition, especially in non-Drosophilidae insects and in some crustaceans are reviewed. Most of the existing information is largely based on the use of several tools, including molecular techniques, to answer many still open questions and solve medical, agricultural, and food quality problems.

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Bradykinin release and inactivation in brain of rats submitted to an experimental model of Alzheimer's disease

et al. 2006

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Effect of invertebrate serine proteinase inhibitors on carrageenan-induced pleural exudation and bradykinin release

Cited by 4 publications

References 43 publications

Protease Inhibitors Extracted fromCaesalpinia echinataLam. Affect Kinin Release during Lung Inflammation

Protease Inhibitors Extracted fromCaesalpinia echinataLam. Affect Kinin Release during Lung Inflammation

Invertebrate trypsins: a review

Bradykinin release and inactivation in brain of rats submitted to an experimental model of Alzheimer's disease

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