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The preparation of recombinant human PGF protein starts with inserting the PGF gene fragment (19-170aa) into a plasmid, which is then used to transform E.coli cells. Once the transformed cells express the recombinant PGF protein, it is subjected to affinity chromatography purification. Following purification, the protein's purity is analyzed via SDS-PAGE, reaching over 97%. The recombinant PGF protein has also been validated to be biologically active, as it chemoattracts human monocytes using a concentration range of 5.0-50 ng/ml. The endotoxin level of this PGF protein is less than 1.0 EU/μg as measured by the LAL method.
Human PGF is a member of the VEGF family, specifically involved in angiogenesis and vasculogenesis during pregnancy. PGF is primarily secreted by the syncytiotrophoblast layer of the placenta and plays a crucial role in promoting blood vessel formation, which is essential for adequate placental and fetal development [1][2]. The protein exists in multiple isoforms, which arise from alternative splicing of its mRNA, leading to variations in its structure and function [2].
PGF interacts with specific receptors, including the VEGFR-1, which mediates its effects on endothelial cells and contributes to regulating placental blood flow [3][4]. The expression of PGF is influenced by various factors, including hypoxia, which can lead to increased levels of this growth factor in the placenta. This response is critical for adapting to the changing oxygen levels during pregnancy [5]. Moreover, PGF has been implicated in the pathophysiology of several pregnancy-related complications, such as preeclampsia, where an imbalance in the PGF and sFlt-1 (soluble fms-like tyrosine kinase-1) ratio is observed [5][4].
PGF is also involved in immune regulation within the placenta. It can modulate maternal immune responses, which is vital for maintaining a healthy pregnancy and preventing fetal rejection [6]. Furthermore, PGF's involvement in the placental secretome highlights its potential as a biomarker for pregnancy complications, as alterations in its levels can indicate placental dysfunction [7][8].
References:
[1] P. Koh, C. Won, H. Noh, G. Cho, & W. Choi. Expression of pituitary adenylate cyclase activating polypeptide and its type i receptor mrnas in human placenta, Journal of Veterinary Science, vol. 6, no. 1, p. 1, 2005. https://doi.org/10.4142/jvs.2005.6.1.1
[2] P. Lacal, C. Failla, et al. Human melanoma cells secrete and respond to placenta growth factor and vascular endothelial growth factor, Journal of Investigative Dermatology, vol. 115, no. 6, p. 1000-1007, 2000. https://doi.org/10.1046/j.1523-1747.2000.00199.x
[3] Y. Murakami, T. Kobayashi, et al. Exogenous vascular endothelial growth factor can induce preeclampsia-like symptoms in pregnant mice, Seminars in Thrombosis and Hemostasis, vol. 31, no. 03, p. 307-313, 2005. https://doi.org/10.1055/s-2005-872437
[4] B. Grimaldi, H. Kohan-Ghadr, & S. Drewlo. The potential for placental activation of pparγ to improve the angiogenic profile in preeclampsia, Cells, vol. 11, no. 21, p. 3514, 2022. https://doi.org/10.3390/cells11213514
[5] A. Colson, C. Depoix, P. Baldin, C. Hubinont, P. Sonveaux, & F. Debiève. Hypoxia‐inducible factor 2 alpha impairs human cytotrophoblast syncytialization: new insights into placental dysfunction and fetal growth restriction, The Faseb Journal, vol. 34, no. 11, p. 15222-15235, 2020. https://doi.org/10.1096/fj.202001681r
[6] E. Hsiao and P. Patterson. Activation of the maternal immune system induces endocrine changes in the placenta via il-6, Brain Behavior and Immunity, vol. 25, no. 4, p. 604-615, 2011. https://doi.org/10.1016/j.bbi.2010.12.017
[7] T. Napso, X. Zhao, et al. Unbiased placental secretome characterization identifies candidates for pregnancy complications,, 2020. https://doi.org/10.1101/2020.07.12.198366
[8] T. Michelsen, T. Henriksen, D. Reinhold, T. Powell, & T. Jansson. The human placental proteome secreted into the maternal and fetal circulations in normal pregnancy based on 4‐vessel sampling, The Faseb Journal, vol. 33, no. 2, p. 2944-2956, 2018. https://doi.org/10.1096/fj.201801193r
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