R. Ghasemi , H. Hashemzadeh , H. Razavi , B. Yakhchali ,
Volume 9, Issue 1 (1-2018)
Abstract
Introduction: Growth hormone is a non-glycosylated polypeptide strand of the pituitary glands of all vertebrates that has a wide range of biological activities and considering the importance of this hormone and its importance and diverse therapeutic applications in medicine, its recombinant production can be of great importance. In recent decades, protein engineering and genetic engineering have resulted in a high level of expression and production of this protein in a variety of hosts, including Escherichia coli bacteria using new techniques and methodes, hormone purification and assay are carried out easily. Therefore, the aim of this review was to investigate the production of recombinant human growth hormone (rhGH) and future challenges.
Conclusion: One of the problems of the expression and purification of the human growth hormone may involve that maybe noted the production of inclusion bodies in the expression of recombinant proteins in the cell cytoplasm, the contamination caused by host proteins, low protein recovery from these inclusion bodies, low protein secretion into the Periplasmic space, high cost of production, especially in Purification stage and so on. Due to the lack of need for glycosylated hormone and high efficiency and simplicity of work, bacterial systems, especially Escherichia coli, are the most economical and effective systems for the expression of heterologous proteins. The hormone purification stage is usually the most costly process. Therefore, an optimal design for achieving the highest target protein recovery with the elimination of all contamination from the final product and reducing the purification step is required.
Volume 23, Issue 3 (7-2020)
Abstract
Aims: Living cells have an electrical charge created by the presence of ions and free radicals. Magnetic fields interact with ions, especially ferromagnetic materials such as iron that affect living cells. A common feature of about 20 different diseases is the aggregation of proteins in the form amyloid structure. In the current study, the effect of static magnetic field (SMF) on the formation and the toxicity of amyloid structures was investigated.
Materials & Methods: CHO cells were exposed to 6mT SMF in three consecutive days, and the effect of SMF on the formation of amyloid structures in the intrinsic proteins of these cells related to the control was investigated using thioflavin T (ThT) binding assay. The formation of amyloid structures in CHO cells expressing human ProIAPP cells was analyzed by observation of proIAPP protein aggregates linked to GFP protein. The effect of SMF on the toxicity of lysozyme oligomers on CHO and Hela cells was also compared with the controls.
Findings: Exposure of CHO cells to magnetic fields does not have a significant effect on the formation of amyloid structures in the intrinsic proteins of CHO cells and the amount of these structures in CHO cells expressing proIAPP protein but can increase the toxicity of lysozyme oligomers on CHO and Hela cells.
Conclusion: The magnetic field does not have a significant effect on the formation of amyloid structures in the 6mT SMF strength, but it adds to the toxicity of these structures.
