<i>Bauhinia</i> Kunitz-type proteinase inhibitors: structural characteristics and biological properties

Oliva, Maria Luiza Vilela; Sampaio, Misako U.

doi:10.1515/bc.2008.119

Cited by 32 publications

(5 citation statements)

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“…Arabidopsis Kunitz-PI;1, as we dubbed the protein here, has a molecular mass of ≈21 kDa which is similar to that of other Kunitz-PIs (Oliva and Sampaio, 2008, 2009). However, despite the presence of the family-defining Kunitz motif, Arabidopsis Kunitz-PI;1 was unable to inhibit trypsin and chymotrypsin ( Figure 1 ).…”

Section: Discussionmentioning

confidence: 87%

An Ethylene-Protected Achilles’ Heel of Etiolated Seedlings for Arthropod Deterrence

et al. 2016

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A small family of Kunitz protease inhibitors exists in Arabidopsis thaliana, a member of which (encoded by At1g72290) accomplishes highly specific roles during plant development. Arabidopsis Kunitz-protease inhibitor 1 (Kunitz-PI;1), as we dubbed this protein here, is operative as cysteine PI. Activity measurements revealed that despite the presence of the conserved Kunitz-motif the bacterially expressed Kunitz-PI;1 was unable to inhibit serine proteases such as trypsin and chymotrypsin, but very efficiently inhibited the cysteine protease RESPONSIVE TO DESICCATION 21. Western blotting and cytolocalization studies using mono-specific antibodies recalled Kunitz-PI;1 protein expression in flowers, young siliques and etiolated seedlings. In dark-grown seedlings, maximum Kunitz-PI;1 promoter activity was detected in the apical hook region and apical parts of the hypocotyls. Immunolocalization confirmed Kunitz-PI;1 expression in these organs and tissues. No transmitting tract (NTT) and HECATE 1 (HEC1), two transcription factors previously implicated in the formation of the female reproductive tract in flowers of Arabidopsis, were identified to regulate Kunitz-PI;1 expression in the dark and during greening, with NTT acting negatively and HEC1 acting positively. Laboratory feeding experiments with isopod crustaceans such as Porcellio scaber (woodlouse) and Armadillidium vulgare (pillbug) pinpointed the apical hook as ethylene-protected Achilles’ heel of etiolated seedlings. Because exogenous application of the ethylene precursor 1-aminocyclopropane-1-carboxylic acid (ACC) and mechanical stress (wounding) strongly up-regulated HEC1-dependent Kunitz-PI;1 gene expression, our results identify a new circuit controlling herbivore deterrence of etiolated plants in which Kunitz-PI;1 is involved.

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Section: Discussionmentioning

confidence: 87%

An Ethylene-Protected Achilles’ Heel of Etiolated Seedlings for Arthropod Deterrence

et al. 2016

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“…Bauhinia seeds are rich in serine and cysteine proteases inhibitors (Oliva and Sampaio, 2008; Oliva et al, 2010, 2011). Oliva et al (1999) isolated the Bauhinia bauhinioides kallikrein inhibitor (BbKI) from seeds of B. bauhinioides , which is a 18-kDa protein with a similar primary structure to that of other plant Kunitz-type inhibitors but is devoid of disulphide bridges.…”

Section: Roles Of Plant Protease Inhibitors In Health and Disease Conmentioning

confidence: 99%

Plant Protease Inhibitors in Therapeutics-Focus on Cancer Therapy

2016

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Plants are known to have many secondary metabolites and phytochemical compounds which are highly explored at biochemical and molecular genetics level and exploited enormously in the human health care sector. However, there are other less explored small molecular weight proteins, which inhibit proteases/proteinases. Plants are good sources of protease inhibitors (PIs) which protect them against diseases, insects, pests, and herbivores. In the past, proteinaceous PIs were considered primarily as protein-degrading enzymes. Nevertheless, this view has significantly changed and PIs are now treated as very important signaling molecules in many biological activities such as inflammation, apoptosis, blood clotting and hormone processing. In recent years, PIs have been examined extensively as therapeutic agents, primarily to deal with various human cancers. Interestingly, many plant-based PIs are also found to be effective against cardiovascular diseases, osteoporosis, inflammatory diseases and neurological disorders. Several plant PIs are under further evaluation in in vitro clinical trials. Among all types of PIs, Bowman-Birk inhibitors (BBI) have been studied extensively in the treatment of many diseases, especially in the field of cancer prevention. So far, crops such as beans, potatoes, barley, squash, millet, wheat, buckwheat, groundnut, chickpea, pigeonpea, corn, and pineapple have been identified as good sources of PIs. The PI content of such foods has a significant influence on human health disorders, particularly in the regions where people mostly depend on these kind of foods. These natural PIs vary in concentration, protease specificity, heat stability, and sometimes several PIs may be present in the same species or tissue. However, it is important to carry out individual studies to identify the potential effects of each PI on human health. PIs in plants make them incredible sources to determine novel PIs with specific pharmacological and therapeutic effects due to their peculiarity and superabundance.

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“…Bauhinia bauhinioides cruzipain inhibitor (BbCI) is an 18 kDa Kunitz-type proteinase inhibitor isolated from Bauhinia bauhinioides seeds [9]. BbCI inhibits the activity of different serine proteinases, such as human neutrophil elastase, porcine pancreatic elastase, and cathepsin G. BbCI also inhibits the activity of cysteine proteinases, such as cathepsin L, cruzipain, and cruzain [10]. The goal of this study was to test the hypothesis that Bauhinia bauhinioides cruzipain inhibitor (BbCI) limits elastase-induced alterations in pulmonary mechanics, emphysema development, lung inflammation, extracellular matrix remodeling, and oxidative stress.…”

Section: Introductionmentioning

confidence: 99%

Plant Proteinase Inhibitor BbCI Modulates Lung Inflammatory Responses and Mechanic and Remodeling Alterations Induced by Elastase in Mice

Almeida-Reis

Theodoro-Junior

Oliveira

et al. 2017

BioMed Research International

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Background. Proteinases play a key role in emphysema. Bauhinia bauhinioides cruzipain inhibitor (BbCI) is a serine-cysteine proteinase inhibitor. We evaluated BbCI treatment in elastase-induced pulmonary alterations. Methods. C57BL/6 mice received intratracheal elastase (ELA group) or saline (SAL group). One group of mice was treated with BbCI (days 1, 15, and 21 after elastase instillation, ELABC group). Controls received saline and BbCI (SALBC group). After 28 days, we evaluated respiratory mechanics, exhaled nitric oxide, and bronchoalveolar lavage fluid. In lung tissue we measured airspace enlargement, quantified neutrophils, TNFα-, MMP-9-, MMP-12-, TIMP-1-, iNOS-, and eNOS-positive cells, 8-iso-PGF2α, collagen, and elastic fibers in alveolar septa and airways. MUC-5-positive cells were quantified only in airways. Results. BbCI reduced elastase-induced changes in pulmonary mechanics, airspace enlargement and elastase-induced increases in total cells, and neutrophils in BALF. BbCI reduced macrophages and neutrophils positive cells in alveolar septa and neutrophils and TNFα-positive cells in airways. BbCI attenuated elastic and collagen fibers, MMP-9- and MMP-12-positive cells, and isoprostane and iNOS-positive cells in alveolar septa and airways. BbCI reduced MUC5ac-positive cells in airways. Conclusions. BbCI improved lung mechanics and reduced lung inflammation and airspace enlargement and increased oxidative stress levels induced by elastase. BbCI may have therapeutic potential in chronic obstructive pulmonary disease.

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Bauhinia Kunitz-type proteinase inhibitors: structural characteristics and biological properties

Cited by 32 publications

References 50 publications

An Ethylene-Protected Achilles’ Heel of Etiolated Seedlings for Arthropod Deterrence

An Ethylene-Protected Achilles’ Heel of Etiolated Seedlings for Arthropod Deterrence

Plant Protease Inhibitors in Therapeutics-Focus on Cancer Therapy

Plant Proteinase Inhibitor BbCI Modulates Lung Inflammatory Responses and Mechanic and Remodeling Alterations Induced by Elastase in Mice

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