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Industrial insulin production uses genetically engineered E. coli expressing a proinsulin gene controlled by a tryptophan promoter and containing a methionine linker for later cleavage. The cells also carry ampicillin resistance for selective growth. Seed cultures are stored at −80 °C and production begins by thawing a small amount to inoculate starter cultures, which are progressively scaled to a 50,000-L bioreactor. In the bioreactor, E. coli grow in nutrient-rich media under...
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Insulin secretory vesicles release insulin to stimulate blood glucose uptake and regulate carbohydrate metabolism. When the blood glucose levels increase, glucose enters the pancreatic β-islet cells through glucose transporters. Once inside, glucose is metabolized through glycolysis, the citric acid cycle, and the electron transport chain, producing ATP. This increase in ATP concentration closes ATP-sensitive potassium channels, leading to depolarization of the membrane and the opening of...
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The endoplasmic reticulum (ER) of pancreatic β-cells synthesizes preproinsulin, which consists of a signal peptide, A and B chains, and a C-peptide. Preproinsulin is then cleaved and folded into proinsulin, which translocates to the Golgi apparatus for sorting and packaging into secretory granules. In these granules, enzymatic clipping generates insulin and C-peptide.
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Cell factories for insulin production.

Nabih A Baeshen1, Mohammed N Baeshen2, Abdullah Sheikh3

  • 1Department of Biological Sciences, Faculty of Science, King Abdulaziz University, P.O. Box 80203, Jeddah, 21589, Saudi Arabia. Nabih_baeshen@hotmail.com.

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Summary

The growing demand for recombinant insulin necessitates improved production methods. This review explores enhancing insulin production in E. coli, yeast, and transgenic plants for cost-effective, large-scale manufacturing.

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Area of Science:

  • Biotechnology and Pharmaceutical Manufacturing
  • Metabolic Disorders and Endocrinology

Background:

  • Global diabetes prevalence is rising, increasing demand for recombinant insulin.
  • Current insulin production faces limitations in capacity and cost, hindering accessibility.
  • Alternative delivery methods like inhalation and oral routes require higher insulin doses.

Purpose of the Study:

  • To review strategies for increasing biologically active insulin and analogue production.
  • To evaluate E. coli, yeast, and transgenic plants as expression systems for insulin.
  • To highlight the potential of plant-based systems for cost-effective, large-scale insulin manufacturing.

Main Methods:

  • Review of existing literature on recombinant protein production in microbial hosts (E. coli, yeast).
  • Analysis of research on transgenic plant expression systems for therapeutic proteins.
  • Focus on methods to enhance post-translational modifications and protein refolding.

Main Results:

  • E. coli and Saccharomyces cerevisiae are established hosts for recombinant human insulin production.
  • Transgenic plants show significant potential for high-capacity, cost-effective insulin production.
  • High expression of stable, biologically active proinsulin in plant seeds/leaves demonstrated.

Conclusions:

  • Optimizing production in E. coli and yeast can help meet rising insulin demand.
  • Transgenic plants offer a promising, low-cost platform for large-scale insulin manufacturing.
  • Plant-derived proinsulin supports development of both injectable and oral insulin therapies.