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Today, we're discussing insulin, a crucial hormone for blood sugar regulation. Can anyone tell me what happens in the body when insulin is not produced?
Without insulin, blood sugar levels can rise uncontrollably, leading to diabetes.
Exactly! Now, let’s dive into how insulin was traditionally produced. Insulin was extracted from the pancreas of cattle and pigs, which had some drawbacks. What do you think those drawbacks could be?
It could cause allergic reactions because the human body might react to animal proteins.
Correct! These reactions made it important to find an alternative. Let's explore the solution of creating insulin using biotechnology.
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By using recombinant DNA technology, we can now produce human insulin in bacteria. Can someone explain how that works?
Isn't it about inserting the DNA sequences for the insulin chains into bacteria?
Precisely! The two chains of insulin are produced separately in *E. coli*. Once produced, they’re combined to form the functional insulin. How does this process help mitigate the issues faced with animal-derived insulin?
Since it's identical to human insulin, there's much less chance of an allergic reaction.
Exactly! The production of insulin using *E. coli* not only solves the allergic response issue but also allows for mass production on demand.
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Now that we understand how insulin is produced, let's talk about its impact. What changes has this technology brought to diabetes management?
It has made insulin treatment much more reliable and accessible for patients.
Right! Mass production means more consistent insulin availability. How do you think this affects patient health outcomes?
Patients can manage their diabetes better, which reduces complications over time.
Absolutely! By improving diabetes management, we have improved the quality of life for many individuals. Very well said!
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Genetically engineered insulin is produced using recombinant DNA technology, allowing for the mass production of a human-identical hormone that is safe for diabetic patients. The section discusses the historical context of insulin production, the advantages of using recombinant techniques, and the challenges associated with insulin therapy.
Insulin is a vital hormone for blood sugar regulation, particularly important for managing diabetes. Historically, insulin was extracted from the pancreas of animals, but this practice often led to allergic reactions and was not sustainable for large populations.
In 1983, Eli Lilly developed a breakthrough process utilizing recombinant DNA (rDNA) technology. By introducing DNA sequences corresponding to insulin's two chains (A and B) into plasmids within E. coli bacteria, researchers were able to produce these chains separately. The chains are then combined to form functional human insulin through the creation of disulfide bonds.
This revolutionary production method not only addressed the insufficiency of animal-derived insulin but also ensured that the insulin produced is structurally identical to human insulin, significantly reducing the likelihood of immune responses. The ability to produce large quantities of insulin safely had a profound impact on diabetes management, enabling better health outcomes for millions of people worldwide.
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Management of adult-onset diabetes is possible by taking insulin at regular time intervals. What would a diabetic patient do if enough human-insulin was not available? If you discuss this, you would soon realise that one would have to isolate and use insulin from other animals. Would the insulin isolated from other animals be just as effective as that secreted by the human body itself and would it not elicit an immune response in the human body? Now, imagine if bacterium were available that could make human insulin. Suddenly the whole process becomes so simple. You can easily grow a large quantity of the bacteria and make as much insulin as you need.
Diabetes is a condition where the body cannot produce enough insulin, a hormone that helps regulate blood sugar levels. Traditionally, insulin was extracted from animal sources like pigs or cattle, which can cause allergic reactions in some patients because it is not identical to human insulin. The introduction of genetically engineered bacteria that can produce human insulin simplifies diabetes management. By modifying bacteria to produce the exact form of insulin needed, we can create a reliable and consistent supply, ensuring diabetic patients receive effective treatment.
Imagine needing to cook a dish that requires a specific ingredient, but you can only find similar ingredients that don't taste the same. It would be frustrating and may not satisfy everyone's taste. Now, picture a restaurant that can grow that exact ingredient itself, ensuring every dish is made perfectly. This is similar to how genetically engineered bacteria provide the precise insulin needed for treating diabetes.
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Insulin used for diabetes was earlier extracted from pancreas of slaughtered cattle and pigs. Insulin from an animal source, though caused some patients to develop allergy or other types of reactions to the foreign protein. Insulin consists of two short polypeptide chains: chain A and chain B, that are linked together by disulphide bridges. In mammals, including humans, insulin is synthesised as a pro-hormone (like a pro-enzyme, the pro-hormone also needs to be processed before it becomes a fully mature and functional hormone) which contains an extra stretch called the C peptide. This C peptide is not present in the mature insulin and is removed during maturation into insulin.
The usage of insulin from animal sources can lead to allergic reactions because the protein structure in animal insulin differs from human insulin. The insulin molecule itself consists of two chains (A and B) linked by bonds, and when produced in mammals, it initially exists as a larger precursor called pro-insulin, which contains additional segments (C peptide). These segments are removed to create the functional form of insulin. Understanding this process is key in engineering bacteria to produce a structurally identical version that our bodies can use without adverse reactions.
Think of a complex puzzle: the complete picture has extra pieces that aren’t part of the final design. When you complete the puzzle, you must remove those extra pieces for it to look right. Similarly, when insulin is produced in animals, extra segments need to be removed for it to function effectively in humans just like removing unnecessary puzzle pieces for a perfect finish.
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The main challenge for production of insulin using rDNA techniques was getting insulin assembled into a mature form. In 1983, Eli Lilly an American company prepared two DNA sequences corresponding to A and B, chains of human insulin and introduced them in plasmids of E. coli to produce insulin chains. Chains A and B were produced separately, extracted and combined by creating disulfide bonds to form human insulin.
The production of human insulin through recombinant DNA (rDNA) technology involves several steps. First, scientists identify the specific DNA sequences that code for the insulin chains. They then introduce these sequences into plasmids (circular DNA) within the bacterium E. coli. The bacteria are engineered to produce these chains, which are harvested and combined to form insulin. This technology ensures that the insulin produced is identical to what the human body naturally makes, eliminating the risk of allergic reactions and improving the effectiveness of diabetes treatments.
Consider a bakery that specializes in making custom cakes. They need specific ingredients (DNA sequences for the insulin chains) to create the perfect cake (insulin). Once they have the recipes, they can bake multiple cakes at once, combining the elements just right to create something that tastes exactly like the original family recipe without any differences. This is how bacteria can be used to replicate human insulin efficiently.
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Key Concepts
Genetically Engineered Insulin: Insulin created using recombinant DNA technology to match human insulin structure.
Recombinant DNA Technology: A method of combining DNA from different organisms.
E. coli as a Host: A common bacterium used to produce recombinant proteins.
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Insulin produced by E. coli that is identical in structure to human insulin.
Clinical use of genetically engineered insulin for diabetic patients.
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Insulin's role, a sugar control, without it, chaos would take its toll.
Once there was a patient named Sam, who needed insulin, but animal sources made him jam. Then scientists found a way, using bacteria in a brilliant display, now Sam has insulin every day.
R.I.C.E.: Recombinant Insulin Created Efficiently.
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Review the Definitions for terms.
Term: Insulin
Definition:
A hormone produced by the pancreas that regulates blood sugar levels.
Term: Recombinant DNA technology
Definition:
A method used to create DNA molecules by combining genetic material from different sources.
Term: E. coli
Definition:
A type of bacteria often used as a host for gene cloning and protein expression.
Term: Prohormone
Definition:
An inactive precursor form of a hormone that must be converted to its active form.