Erratum to "Action of plant proteinase inhibitors on enzymes of physiopathological importance" [An Acad Bras Cienc 81(2009): 615-621]

Oliva, Maria Luiza Vilela; Sampaio, Misako U.

doi:10.1590/s0001-37652010000200016

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“…Other natural serine protease inhibitors have already also been studied in disease models. Plant inhibitors like Enterolobium contortisiliquum trypsin inhibitor (EcTI) that is a polyspecific inhibitor of the Kunitz family, extracted from Enterolobium contortisiliquum seeds [94] and it has inhibitory activity on trypsin, chymotrypsin, plasma kallikrein, plasmin, and HNE with Ki in nM range [95]. EcTI were used in an experimental inflammatory model in C57/Bl6 mice induced by HNE, the results showed a decrease in pulmonary inflammation, oxidative stress and mechanical alterations, consolidating the therapeutic potential of the inhibitor [96].…”

Section: Resultsmentioning

confidence: 99%

Neutrophil elastase inhibitor purification strategy from cowpea seeds

et al. 2019

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Serine proteases and its inhibitors are involved in physiological process and its deregulation lead to various diseases like Chronic Obstructive Pulmonary Disease (COPD), pulmonary emphysema, skin diseases, atherosclerosis, coagulation diseases, cancer, inflammatory diseases, neuronal disorders and other diseases. Serine protease inhibitors have been described in many species, as well as in plants, including cowpea beans (Vigna unguiculata (L.) Walp). Here, we purified and characterized a protease inhibitor, named VuEI (Vigna unguiculata elastase inhibitor), from Vigna unguiculata, with inhibitory activity against HNE (human neutrophil elastase) and chymotrypsin but has no inhibitory activity against trypsin and thrombin. VuEI was obtained by alkaline protein extraction followed by three different chromatographic steps in sequence. First, an ion exchange chromatography using Hitrap Q column was employed, followed by two reversed-phase chromatography using Source15RPC and ACE18 columns. The molecular mass of VuEI was estimated in 10.99 kDa by MALDI-TOF mass spectrometry. The dissociation constant (Ki) to HNE was 9 pM. These data indicate that VuEI is a potent inhibitor of human neutrophil elastase, besides to inhibit chymotrypsin.

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Section: Resultsmentioning

confidence: 99%