Effect of recombibant Protein FGF-7 (fibroblast growth factor 7) on stimulating fibroblast prolifection
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DOI:
https://doi.org/10.46223/HCMCOUJS.tech.vi.21.1.4429.2026Abstract
Fibroblast growth factor (FGF7/KGF), belonging to the FGF family, has long been known for its role in wound healing, angiogenesis, and especially cell growth stimulation. Therefore, generating a large quantity of highly purified FGF7 for applications in regenerative biomedical research is a significant challenge. The mouse fibroblast cell line (L929) plays a crucial role because fibroblasts are largely involved in the entire wound healing process, particularly at the end of the healing process. In this study, FGF7 was generated using recombinant technology and its stimulation of mouse fibroblasts was evaluated. The results showed that the recombinant FGF-7 protein source achieved a concentration of 75.5 µg/ml with 96.2% purity from the Escherichia coli BL21 (DE3) expression system. The MTT assay results showed that after 24 hours of culture, fibroblast cells achieved the highest proliferation rate at a concentration of 10 µg/ml (1.76 times) compared to the control without FGF-7 supplementation at the same time.Downloads
References
Assenberg, R., Wan, P. T., Geisse, S., & Mayr, L. M. (2013). Advances in recombinant protein expression for use in pharmaceutical research. Current Opinion in Structural Biology, 23(3), 393-402. https://doi.org/10.1016/j.sbi.2013.03.008
Beenken, A., & Mohammadi, M. (2009). The FGF family: Biology, pathophysiology and therapy. Nature Reviews Drug Discovery, 8(3), 235-253. https://doi.org/10.1038/nrd2792
Bell, C. E., & Lewis, M. (2000). A closer view of the conformation of the Lac repressor bound to operator. Nature Structural Biology, 7(3), 209-214. https://doi.org/10.1038/73317
Bucur, M., Constantin, C., Neagu, M., Zurac, S., Dinca, O., Vladan, C., Cioplea, M., Popp, C., Nichita, L., & Ionescu, E. (2018). Alveolar blood clots and platelet-rich fibrin induce in vitro fibroblast proliferation and migration. Experimental and Therapeutic Medicine. https://doi.org/10.3892/etm.2018.7063
Crowe, A. R., & Yue, W. (2023). Semi-quantitative determination of protein expression using immunohistochemistry staining and analysis. Bio-protocol, 9(24), e3465. https://doi.org/10.21769/BioProtoc.3465
Danilenko, D. M., Ring, B. D., Yanagihara, D., Benson, W., Wiemann, B., Starnes, C. O., & Pierce, G. F. (1995). Keratinocyte growth factor is an important endogenous mediator of hair follicle growth, development, and differentiation: Normalization of the nu/nu follicular differentiation defect and amelioration of chemotherapy-induced alopecia. The American Journal of Pathology, 147(1), 145-154.
Guo, X., Degenstein, L., & Fuchs, E. (1996). Keratinocyte growth factor is required for hair development but not for wound healing. Genes & Development, 10(1), 165-175.
Ibrahimi, O. A., Eliseenkova, A. V., Plotnikov, A. N., Yu, K., Ornitz, D. M., & Mohammadi, M. (2001). Structural basis for fibroblast growth factor receptor 2 activation in Apert syndrome. Proceedings of the National Academy of Sciences, 98(13), 7182-7187. https://doi.org/10.1073/pnas.121183798
Itoh, N., & Ornitz, D. M. (2004). Evolution of the FGF and FGFR gene families. Trends in Genetics, 20(11), 563-569. https://doi.org/10.1016/j.tig.2004.08.007
Jafari, B., Hamzeh-Mivehroud, M., Moosavi-Movahedi, A. A., & Dastmalchi, S. (2018). Identification of novel single-domain antibodies against FGF7 using phage display technology. SLAS Discovery, 23(2), 193-201. https://doi.org/10.1177/2472555217728520
Kim, Y. S., Lee, J. S., Jeong, M. Y., Jang, J. W., & Kim, M. S. (2024). Recombinant human fibroblast growth factor 7 obtained from stable Chinese hamster ovary cells enhances wound healing. Biotechnology Journal, 19(5), e2300596. https://doi.org/10.1002/biot.202300596
Le, X. M. H., Dang, T. T. P., & Tran, T. L. (2014). Nghiên cứu tái gấp cuộn protein leptin người tái tổ hợp từ thể vùi của Escherichia coli [Research on the refolding of recombinant human leptin protein from inclusion bodies of Escherichia coli]. Tạp chí Sinh học, 36(1se), 54-61.
Liu, J.-R., Xu, G.-M., Shi, X.-M., & Zhang, G.-J. (2017). Low temperature plasma promoting fibroblast proliferation by activating the NF-ΚB pathway and increasing cyclind1 expression. Scientific Reports, 7(1), Article 11698. https://doi.org/10.1038/s41598-017-12043-w
Memarzadeh, S., Xin, L., Mulholland, D. J., Mansukhani, A., Wu, H., Teitell, M. A., & Witte, O. N. (2007). Enhanced paracrine FGF10 expression promotes formation of multifocal prostate adenocarcinoma and an increase in epithelial androgen receptor. Cancer Cell, 12(6), 572-585. https://doi.org/10.1016/j.ccr.2007.11.002
Mirhosseini, S. A., Latifi, A. M., Hosseini, H. M., Seidmoradi, R., Aghamollaei, H., & Farnoosh, G. (2019). The efficient solubilization and refolding of recombinant organophosphorus hydrolyses inclusion bodies produced in Escherichia coli. Journal of Applied Biotechnology Reports, 6(1), 20-25. http://doi:10.29252/JABR.06.01.04
Nguyen, B. T., Nguyen, Q. D., Ngo, T. V., Truong, N. H. N., & Duong, X. H. (2019). Expression, purification, and characterization of His-TAT-HA2 fused apoptin from Chicken Anemia Virus, targeting cancer therapy. In Proceedings of the 1st scientific conference on the application of biotechnology and biomedical technology in clinical medicine in 2019 (pp. 153-165).
Ornitz, D. M., & Itoh, N. (2015). The fibroblast growth factor signaling pathway. WIREs Developmental Biology, 4(3), 215-266. https://doi.org/10.1002/wdev.176
Pierce, G. F., Mustoe, T. A., Altrock, B. W., Deuel, T. F., & Thomason, A. (1991). Role of platelet‐derived growth factor in wound healing. Journal of Cellular Biochemistry, 45(4), 319-326. https://doi.org/10.1002/jcb.240450403
Rosano, G. L., & Ceccarelli, E. A. (2014). Recombinant protein expression in Escherichia coli: Advances and challenges. Frontiers in Microbiology, 5, Article 172. https://doi.org/10.3389/fmicb.2014.00172
Rubin, J. S., Osada, H., Finch, P. W., Taylor, W. G., Rudikoff, S., & Aaronson, S. A. (1989). Purification and characterization of a newly identified growth factor specific for epithelial cells. Proceedings of the National Academy of Sciences, 86(3), 802-806. https://doi.org/10.1073/pnas.86.3.802
Shaoul, R., Eliahu, L., Sher, I., Hamlet, Y., Miselevich, I., Goldshmidt, O., & Ron, D. (2006). Elevated expression of FGF7 protein is common in human gastric diseases. Biochemical and Biophysical Research Communications, 350(4), 825-833. https://doi.org/10.1016/j.bbrc.2006.08.198
Spielberger, R., Stiff, P., Bensinger, W., Gentile, T., Weisdorf, D., Kewalramani, T., Shea, T., Yanovich, S., Hansen, K., Noga, S., McCarty, J., LeMaistre, C. F., Sung, E. C., Blazar, B. R., Elhardt, D., Chen, M.-G., & Emmanouilides, C. (2004). Palifermin for oral mucositis after intensive therapy for hematologic cancers. New England Journal of Medicine, 351(25), 2590-2598. https://doi.org/10.1056/nejmoa040125
Tekin, M., Akay, H. O., Fitoz, S., Birnbaum, S., Cengiz, F., Sennaroğlu, L., İncesulu, A., Konuk, E. Y., Bayrak, A. H., Şentürk, S., Cebeci, I., Ütine, G., Tunçbilek, E., Nance, W., & Duman, D. (2008). Homozygous FGF3 mutations result in congenital deafness with inner ear agenesis, Microtia, and Microdontia. Clinical Genetics, 73(6), 554-565. https://doi.org/10.1111/j.1399-0004.2008.01004.x
Tekin, M., Hişmi, B. Ö., Fitoz, S., Özdağ, H., Cengiz, F. B., Sırmacı, A., Aslan, İ., İnceoğlu, B., Yüksel-Konuk, E. B., Yılmaz, S. T., Yasun, Ö., & Akar, N. (2007). Homozygous mutations in fibroblast growth factor 3 are associated with a new form of syndromic deafness characterized by inner ear agenesis, Microtia, and Microdontia. The American Journal of Human Genetics, 80(2), 338-344. https://doi.org/10.1086/510920
Tran, H. T. K., Hoang, D. T., & Nguyen, A. T. K. (2018). Nuôi cấy tế bào sợi từ mô chuột [Cuture fibroblasts isolated from mouse tissues]. Tạp chí Sinh học, 40(1), 69-75. https://doi.org/10.15625/0866-7160/v40n1.8789
Truzzi, F., Valerii, M. C., Tibaldi, C., Zhang, Y., Abduazizova, V., Spisni, E., & Dinelli, G. (2020). Are supplements safe? Effects of gallic and ferulic acids on in vitro cell models. Nutrients, 12(6), Article 1591. https://doi.org/10.3390/nu12061591
Venkatesan, M., Semper, C., Skrivergaard, S., Di Leo, R., Mesa, N., Rasmussen, M. K., Young, J. F., Therkildsen, M., Stogios, P. J., & Savchenko, A. (2022). Recombinant production of growth factors for application in cell culture. iScience, 25(10), Article 105054. https://doi.org/10.1016/j.isci.2022.105054
Wilkie, A. O. M., Slaney, S. F., Oldridge, M., Poole, M. D., Ashworth, G. J., Hockley, A. D., Hayward, R. D., David, D. J., Pulleyn, L. J., Rutland, P., Malcolm, S., Winter, R. M., & Reardon, W. (1995). Apert syndrome results from localized mutations of FGFR2 and is allelic with Crouzon syndrome. Nature Genetics, 9(2), 165-172. https://doi.org/10.1038/ng0295-165
Zhang, Y., Olsen, D. R., Nguyen, K. B., Olson, P. S., Rhodes, E. T., & Mascarenhas, D. (1998). Expression of eukaryotic proteins in soluble form in Escherichia coli. Protein Expression and Purification, 12(2), 159-165. https://doi.org/10.1006/prep.1997.0834
