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Science, Technology, Engineering, Management and Medicine
Study on the Discovery and Properties of Anticancer Fibrinolytic Active Protein from Sympiezomias velatus Chevrolat
DOI: https://doi.org/10.62517/jlsa.202407208
Author(s)
Shuaiying Zhang1,2, Yerui Ouyang1,2, Lei Zhu1,2, Yizi Zhang1,2, Jiantao Liu1,2,*
Affiliation(s)
1Key Laboratory of Bioprocess Engineering of Jiangxi Province, College of Life Sciences, Jiangxi Science and Technology Normal University, Nanchang, Jiangxi, China 2Key Laboratory of Microbial Resources and Metabolism of Nanchang, College of Life Sciences, Jiangxi Science and Technology Normal University, Nanchang, Jiangxi, China *Corresponding Author.
Abstract
Sympiezomias velatus Chevrolat, commonly known as the cereal leaf beetle, is an insect pest that mainly affects tobacco crops. Feeding on tobacco leaves, it causes significant economic losses and impacts tobacco production. Due to its wide distribution and high adaptability, S. velatus has become an important model organism for studying croppest control and ecological adaptability. In this experiment, S. velatus was used as the research subject. The crude protein of S. velatus was isolated and extracted using the ammonium sulfate partial salting-out method. The protein activity was assessed using the fiber active plate method. The results demonstrated that three different concentration gradients of crude protein exhibited strong fibrinolytic activity. The optimum temperature for protein activity was found to be 35℃, while the optimal pH was approximately 7.0. Fe3+ significantly inhibited the activity of the fibrinolytic active protein in S. velatus, whereas Ba2+ showed a slight inhibitory effect on βME. Na+ and EDTA did not exhibit any impact. MTT experiments revealed that the fibrinolytic active protein displayed a certain inhibitory effect on cancer cell growth. This study provides valuable references for other research on S. velatus.
Keywords
Sympiezomias velatus Chevrolat; Fibrinolytic Activity; Purification; Anticancer
References
[1] Feller, T., J. Hársfalvi, C. Csányi, B. Kiss, and M. Kellermayer, Plasmin-driven fibrinolysis in a quasi-two-dimensional nanoscale fibrin matrix. J Struct Biol, 2018. 203 (3): p. 273-280. [2] Fan, P., Y. Gao, M. Zheng, T. Xu, P. Schoenhagen, and Z. Jin, Recent progress and market analysis of anticoagulant drugs. J Thorac Dis, 2018. 10 (3): p. 2011-2025. [3] Stephani, L., R.R. Tjandrawinata, D.N. Afifah, Y. Lim, W.T. Ismaya, and M.T.J.H.J.o.B. Suhartono, Food origin fibrinolytic enzyme with multiple actions. 2017. 24 (3): p. 124-130. [4] Li, X., J.W. Li, W.X. Sun, W. Li, H.Y. Gao, T.X. Liu, and M.J. Qu, Candidate Chemosensory Genes Identified in the Adult Antennae of Sympiezomias velatus and Binding Property of Odorant-Binding Protein 15. Front Physiol, 2022. 13: p. 907667. [5] Li-Ping, W.J.S., T.o.Q. Agriculture, and Forestry, Biological Characteristics of Sympiezomias velatus and Screening of Control Agents in Xining. 2018. [6] Hahn, B.S., S.Y. Cho, S.J. Wu, I.M. Chang, K. Baek, Y.C. Kim, and Y.S. Kim, Purification and characterization of a serine protease with fibrinolytic activity from Tenodera sinensis (praying mantis). Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1999. 1430(2): p. 376-386. [7] Papahadjopoulos, D. and D.J. Hanahan, Observations on the interaction of phospholipids and certain clotting factors in prothrombin activator formation. Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1964. 90: p. 436-439. [8] Noble, J., A. Knight, A. Reason, A. Di Matola, and M.J.M.b. Bailey, A comparison of protein quantitation assays for biopharmaceutical applications. 2007. 37: p. 99-111. [9] Sultan, S.A., M.H. Khawaji, J. Alsughayyir, M.A. Alfhili, H.S. Alamri, and B.M. Alrfaei, Antileukemic activity of sulfoxide nutraceutical allicin against THP-1 cells is associated with premature phosphatidylserine exposure in human erythrocytes. Saudi J Biol Sci, 2020. 27 (12): p. 3376-3384. [10] Ulukaya, E., M. Colakogullari, and E.J. Wood, Interference by anti-cancer chemotherapeutic agents in the MTT-tumor chemosensitivity assay. Chemotherapy, 2004. 50 (1): p. 43-50. [11] Nga, N.T.H., T.T.B. Ngoc, N.T.M. Trinh, T.L. Thuoc, and D.T.P. Thao, Optimization and application of MTT assay in determining density of suspension cells. Analytical Biochemistry, 2020. 610: p. 113937.
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