Code | CSB-EP007587HU |
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In expressing the recombinant human neutrophil elastase (ELANE), E.coli cells are transfected with a DNA expression vector that harbors the gene for the ELANE protein (30-267aa) along with the N-terminal GST-tag gene. The cultured cells then express the intended protein. The recombinant human ELANE protein is collected and purified from the cell lysate through affinity purification, achieving a purity surpassing 90%, as confirmed by SDS-PAGE.
ELANE is a serine protease predominantly found in mammalian granulocytes, particularly concentrated in granules that fuse with phagosomes [1]. ELANE plays a crucial role in various physiological and pathological processes. ELANE is secreted during airway inflammation, contributing to airway hyperreactivity [2]. ELANE regulates inflammation and is implicated in the pathogenesis of chronic obstructive pulmonary disease (COPD) [3][4][8]. ELANE can exert proinflammatory effects by degrading connective tissue components, attacking serum proteins, and altering cellular functions [5].
Studies suggest that ELANE is a potential therapeutic target for various diseases due to its role in promoting neointimal hyperplasia and tumorigenesis [6][7]. Elevated levels of ELANE have been associated with prehypertension, airflow limitation in obese women, and various other diseases [9]. ELANE is a major contributor to tissue destruction in chronic and inflammatory diseases [10]. ELANE is a key player in acute alveolar injury and interstitial edema, with studies highlighting its involvement in increasing vascular permeability in acute respiratory distress syndrome (ARDS) [11].
References:
[1] A. Cole, J. Shi, A. Ceccarelli, Y. Kim, A. Park, & T. Ganz, Inhibition of neutrophil elastase prevents cathelicidin activation and impairs clearance of bacteria from wounds, Blood, vol. 97, no. 1, p. 297-304, 2001. https://doi.org/10.1182/blood.v97.1.297
[2] A. Lockett, Y. Wu, & S. Gunst, Elastase alters contractility and promotes an inflammatory synthetic phenotype in airway smooth muscle tissues, Ajp Lung Cellular and Molecular Physiology, vol. 314, no. 4, p. L626-L634, 2018. https://doi.org/10.1152/ajplung.00334.2017
[3] M. Pawar and S. Abhang, Evaluation of neutrophil elastase/ alpha-1-antitrypsin ratio in different stages of chronic obstructive pulmonary disease (copd) patients, International Journal of Medical Research and Review, vol. 5, no. 7, p. 664-674, 2017. https://doi.org/10.17511/ijmrr.2017.i07.04
[4] R. Brown, R. Lever, N. Jones, & C. Page, Effects of heparin and related molecules upon neutrophil aggregation and elastase release in vitro, British Journal of Pharmacology, vol. 139, no. 4, p. 845-853, 2003. https://doi.org/10.1038/sj.bjp.0705291
[5] P. Ossanna, S. Test, N. Matheson, S. Regiani, & S. Weiss, Oxidative regulation of neutrophil elastase-alpha-1-proteinase inhibitor interactions., Journal of Clinical Investigation, vol. 77, no. 6, p. 1939-1951, 1986. https://doi.org/10.1172/jci112523
[6] M. Yang, Q. Chen, L. Mei, G. Wen, W. An, X. Zhouet al., Neutrophil elastase promotes neointimal hyperplasia by targeting toll‐like receptor 4 (tlr4)–nf‐κb signalling, British Journal of Pharmacology, vol. 178, no. 20, p. 4048-4068, 2021. https://doi.org/10.1111/bph.15583
[7] I. Lerman and S. Hammes, Neutrophil elastase in the tumor microenvironment, Steroids, vol. 133, p. 96-101, 2018. https://doi.org/10.1016/j.steroids.2017.11.006
[8] G. Hansen, H. Gielen‐Haertwig, P. Reinemer, D. Schomburg, A. Harrenga, & K. Niefind, Unexpected active-site flexibility in the structure of human neutrophil elastase in complex with a new dihydropyrimidone inhibitor, Journal of Molecular Biology, vol. 409, no. 5, p. 681-691, 2011. https://doi.org/10.1016/j.jmb.2011.04.047
[9] M. El-Eshmawy, E. El-Adawy, A. Mousa, A. Zeidan, A. El-Baiomy, E. Abdel-Samieet al., Elevated serum neutrophil elastase is related to prehypertension and airflow limitation in obese women, BMC Women S Health, vol. 11, no. 1, 2011. https://doi.org/10.1186/1472-6874-11-1
[10] S. Ahmad, M. Saleem, N. Riaz, Y. Lee, R. Diri, A. Nooret al., The natural polypeptides as significant elastase inhibitors, Frontiers in Pharmacology, vol. 11, 2020. https://doi.org/10.3389/fphar.2020.00688
[11] Y. Guevara, M. Díaz-Reyes, A. Cabrera-Muñoz, A. Monteagudo, M. Rivero, & O. Blanco-Hidalgo, Effect of cuban porcine pulmonary surfactant (surfacen) and rcmpi-ii protease inhibitor on neutrophil elastase activity, Medicc Review, vol. 24, no. 3–4, p. 46, 2022. https://doi.org/10.37757/mr2022.v24.n3-4.7
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