How to incorporate an insulin gene into a plant to produce human insulin Humulin?
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Open access•Journal Article 11 Citations | Our results indicate that the direct intramuscular injection of naked plasmids encoding human preproinsulin gene achieves the effective expression of insulin. |
165 Citations | Plant-derived insulin accumulates to significant levels in transgenic seed (0.13% total seed protein) and can be enzymatically treated in vitro to generate a product with a mass identical to that of the predicted product, DesB(30)-insulin. |
18 Citations | Since the single chain insulin precursor can be produced by gene technology (yeast), use of immobilized trypsin or Ach and the two‐step reaction using the single chain insulin precursor as the starting material ensures the continuous production of human insulin making it a feasible method for industrial manufacture. |
| This work demonstrated that plant-based systems expressing pro-insulin may provide an effective, low-cost approach to produce insulin for the treatment of Types I and II diabetes. | |
Open access•Journal Article 35 Citations | HuMSCs are able to differentiate into insulin-producing cells in vitro. |
20 Citations | The human insulin gene mRNA and human insulin were only detected in the lavage and the coloclysis groups. The human insulin gene can be transfected and expressed successfully by chitosan–pCMV. Ins in NIH3T3 cells and diabetes rats, which indicates that chitosan is a promising, non-viral vector for gene expression. |
114 Citations | We conclude that the transcriptional regulation of insulin production using these glucose- and insulin-sensitive constructs meets the requirements for application in a rodent model of insulin gene therapy. |
| The ability to transfect DNA into adipose cells which remain insulin responsive after one day in primary culture may be helpful for understanding adipose cell-specific gene regulation and elucidating the molecular mechanisms of insulin action. | |
| Bg‐like proteins may be involved in an insulin‐like regulatory mechanism in many plant species. | |
74 Citations | Although there is no sequence similarity between the leginsulin and insulin or insulin-like growth factors, the leginsulin is a possible candidate for plant peptide hormones. |
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Why CHO than yeast For production of insulin?5 answersCHO cells are preferred over yeast for the production of insulin because CHO cells have the ability to perform post-translational modifications, such as glycosylation, which is important for the proper folding and function of insulin. In contrast, yeast cells do not have the machinery to perform these modifications, leading to the production of insulin aggregates and reduced biological activity. Additionally, CHO cells have a higher protein expression capacity compared to yeast, allowing for higher yields of insulin production. Furthermore, CHO cells have been genetically modified to have reduced activity of YAP3 protease, which improves the production of insulin precursors. Overall, the use of CHO cells for insulin production offers advantages in terms of proper folding, higher expression capacity, and improved precursor production compared to yeast.
How can bacteria be engineered to produce insulin?3 answersBacteria can be engineered to produce insulin through a process called recombinant DNA technology. This involves extracting the target insulin genes and recombining them with the genes of engineering bacteria. The engineering bacteria are then cultured and prepared to import a carrier for the insulin genes. The genes are expressed in the bacteria, resulting in the production of insulin. This method allows for the production of large quantities of insulin in a short amount of time, with high purity and stability. Another approach involves engineering commensal bacteria to secrete GLP-1(1-37), which can reprogram intestinal cells into insulin-secreting cells. This method has shown promising results in ameliorating hyperglycemia in a rat model of diabetes. Overall, these methods provide potential avenues for the production of insulin using engineered bacteria.
What downstream processes are involved in the formation of insulin from E. coli?4 answersThe downstream processes involved in the formation of insulin from E. coli include proinsulin recovery from inclusion bodies, inclusion body washing, inclusion body solubilization and oxidative sulfitolysis, cyanogen bromide cleavage, buffer exchange, purification by chromatography, pH precipitation and zinc crystallization methods, proinsulin refolding, enzymatic cleavage, and formulation. In the case of glargine insulin, citraconylation and trypsin cleavage are performed to convert the prepeptide into glargine insulin, followed by purification through ion-exchange chromatography and reverse-phase chromatography. Another method involves the cloning and verification of human insulin, overexpression in E. coli, and optimisation of expression. Additionally, the formation of insulin-related compounds (IRCs) during expression and purification is investigated, and methods for inhibiting IRC formation are presented. The separate isolation of the insulin A- and B-chains from inclusion bodies and their subsequent assembly into native human insulin is also described.
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