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• W4362510152 abstract "Imbalances between proteases and protease inhibitors have been associated with several pathological conditions including emphysema as seen in α1-antitrypsin deficiency. For this pathological condition, unimpeded neutrophil elastase activity has been ascribed a pivotal role in the destruction of lung tissue and thus in disease progression. Therefore, low, or non-quantifiable neutrophil elastase (NE) activity levels determined in bronchoalveolar lavage solutions indicate the success of α1-antitrypsin (AAT) augmentation therapy as NE activity will be erased. To overcome the known limitations of available elastase activity assays regarding sensitivity and selectivity, we developed a new elastase activity assay, which fundamentally relies on the highly specific complex formation between AAT and active elastase. Plate-bound AAT captured active elastase from the sample undergoing complex formation, followed by the immunological detection of human NE. This assay principle facilitated the measurement of low pM amounts of active human NE. The data of the assay performance check demonstrated adequate accuracy and precision profiles meeting currently accepted best practices for this activity assay, which can be classified as a ligand-binding assay. Furthermore, spike-recovery studies at low human NE levels, carried out for three human bronchoalveolar samples, resulted in recoveries within the 100 ± 20% range, while good linearity and parallelism of the samples’ dilution-response curves was observed. Altogether, complemented by the data of selectivity and robustness studies and the accuracy and precision profile obtained in buffer, this newly developed human NE activity assay was demonstrated to perform accurately and precisely in clinically relevant samples." @default.
• W4362510152 created "2023-04-06" @default.
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• W4362510152 date "2023-05-01" @default.
• W4362510152 modified "2023-10-14" @default.
• W4362510152 title "Selective and sensitive measurement of human neutrophil elastase in clinical samples based on a novel assay principle for protease activity measurement" @default.
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• W4362510152 doi "https://doi.org/10.1016/j.jpba.2023.115376" @default.
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