Post by account_disabled on Oct 26, 2023 12:27:34 GMT 1
The dysregulated activity of proteases in humans is related to a series of diseases. Neutrophil elastase is a protease controlled by the α1-antitrypsin inhibitor (AAT) that is naturally produced by the liver. Mutations in the SERPINA 1 gene cause deficiency of this inhibitor and the consequence of this is the appearance of various pathologies in humans. Given that plant species are promising sources for the discovery of new drugs, the present study aimed to evaluate the inhibitory effect of extracts on elastase, where IC 50 values of 8.1 ± 1.4 µg/ml ( aqueous extract) and 3.3 ± 0.6 µg/ml (ethanolic extract).
These results suggest that Sedum dendroideum extracts may be a potential source of bioactive compounds for the discovery of new elastase inhibitors. Keywords: Balm, IC 50, inhibitors. INTRODUCTION Proteases are fundamental enzymes for a large number of physiological processes such as protein digestion, reproduction, blood coagulation, the Kallikrein-Kinin system and europe mobile number list fibrinolysis (Otín & Bonde, 2008). In humans, the unregulated activity of proteases is related to several pathological conditions such as cancer, inflammatory processes, thrombosis, arthritis, skin diseases and pulmonary emphysema. For this reason, the activity of proteases needs to be controlled and regulated (Rawlings et al. , 2004). Recent research has revealed that proteases have become important targets for drug development.
Elastase is a protease produced mainly by the pancreas and neutrophils, and has the property of hydrolyzing components of the extracellular matrix, such as collagen, elastin, laminin and proteoglycans (Thomson & Kapadia, 1979). The proteolytic activity of neutrophil elastase is strictly regulated by the endogenous protein inhibitor called α-1-antitrypsin (AAT). Mutations in the SERPINA 1 gene, Pi locus, located on chromosome 14 (14q31-32) cause AAT deficiency (Siedle, et al ., 2003). Without the presence of its natural inhibitor, abundant elastase generates tissue damage, as this enzyme is the main protease released by neutrophils in inflammatory processes.
These results suggest that Sedum dendroideum extracts may be a potential source of bioactive compounds for the discovery of new elastase inhibitors. Keywords: Balm, IC 50, inhibitors. INTRODUCTION Proteases are fundamental enzymes for a large number of physiological processes such as protein digestion, reproduction, blood coagulation, the Kallikrein-Kinin system and europe mobile number list fibrinolysis (Otín & Bonde, 2008). In humans, the unregulated activity of proteases is related to several pathological conditions such as cancer, inflammatory processes, thrombosis, arthritis, skin diseases and pulmonary emphysema. For this reason, the activity of proteases needs to be controlled and regulated (Rawlings et al. , 2004). Recent research has revealed that proteases have become important targets for drug development.
Elastase is a protease produced mainly by the pancreas and neutrophils, and has the property of hydrolyzing components of the extracellular matrix, such as collagen, elastin, laminin and proteoglycans (Thomson & Kapadia, 1979). The proteolytic activity of neutrophil elastase is strictly regulated by the endogenous protein inhibitor called α-1-antitrypsin (AAT). Mutations in the SERPINA 1 gene, Pi locus, located on chromosome 14 (14q31-32) cause AAT deficiency (Siedle, et al ., 2003). Without the presence of its natural inhibitor, abundant elastase generates tissue damage, as this enzyme is the main protease released by neutrophils in inflammatory processes.