How Insulin Is Made - Material, Manufacture, History, Used, Parts, Components, Structure, Steps, Product
Background Insulin is a hormone that regulates the amount of glucose (sugar) in the blood and is required for the body to function normally. Insulin is produced by cells in the pancreas, called the islets of Langerhans. These cells continuously release a small amount of insulin into the body, but they release surges of the hormone in response to a rise in the blood glucose level. Certain cells in the body change the food ingested into energy, or blood glucose, that cells can use. Every time a person eats, the blood glucose rises. Raised blood glucose triggers the cells in the islets of Langerhans to release the necessary amount of insulin. Insulin allows the blood glucose to be transported from the blood into the cells. Cells have an outer wall, called a membrane, that controls what enters and exits the cell. Researchers do not yet know exactly how insulin works, but they do know insulin binds to receptors on the cell's membrane. This activates a set of transport molecules so that glucose and proteins can enter the cell. The cells can then use the glucose as energy to carry out its functions. Once transported into the cell, the blood glucose level is returned to normal within hours. Without insulin, the blood glucose builds up in the blood and the cells are starved of their energy source. Some of the symptoms that may occur include fatigue, constant infections, blurred eye sight, numbness, tingling in the hands or legs, increased thirst, and slowed healing of bruises or cuts. The cells will begin to use fat, the energy source stored for emergencies. When this happens for too long a time the body produces ketones, chemicals produced by the liver. Ketones can poison and kill cells if they build up in the body over an extended period of time. This can lead to serious illne Continue reading >>
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"Insulin therapy" redirects here. For the psychiatric treatment, see Insulin shock therapy. Insulin is used as a medication to treat high blood sugar. This includes in diabetes mellitus type 1, diabetes mellitus type 2, gestational diabetes, and complications of diabetes such as diabetic ketoacidosis and hyperosmolar hyperglycemic states. It is also used along with glucose to treat high blood potassium levels. Typically it is given by injection under the skin, but some forms may also be used by injection into a vein or muscle. The common side effect is low blood sugar. Other side effects may include pain or skin changes at the sites of injection, low blood potassium, and allergic reactions. Use during pregnancy is relatively safe for the baby. Insulin can be made from the pancreas of pigs or cows. Human versions can be made either by modifying pig versions or recombinant technology. It comes in three main types short–acting (such as regular insulin), intermediate–acting (such as NPH insulin), and longer-acting (such as insulin glargine). Insulin was first used as a medication in Canada by Charles Best and Frederick Banting in 1922. It is on the World Health Organization's List of Essential Medicines, the most effective and safe medicines needed in a health system. The wholesale cost in the developing world is about US$2.39 to $10.61 per 1,000 iu of regular insulin and $2.23 to $10.35 per 1,000 iu of NPH insulin. In the United Kingdom 1,000 iu of regular or NPH insulin costs the NHS 7.48 pounds, while this amount of insulin glargine costs 30.68 pounds. Medical uses Giving insulin with an insulin pen. Insulin is used to treat a number of diseases including diabetes and its acute complications such as diabetic ketoacid Continue reading >>
How Insulin Is Made Using Bacteria
Website Search Description: Synthetic human insulin was the first golden molecule of the biotech industry and the direct result of recombinant DNA technology. Currently, millions of diabetics worldwide use synthetic insulin to regulate their blood sugar levels. Synthetic insulin is made in both bacteria and yeast. Keywords: recombinant dna technology,blood sugar levels,human insulin,biotech industry,diabetics,molecule,bacteria,yeast Synthetic human insulin was the first golden molecule of the biotech industry and the direct result of recombinant DNA technology. Currently, millions of diabetics worldwide use synthetic insulin to regulate their blood sugar levels. Synthetic insulin i Continue reading >>
How Is Synthetic Insulin Made?
Synthetic insulin was first made in 1978 by scientists at Genetech, Inc. and City of Hope National Medical Center. This achievement was a giant step forward in insulin production for people with diabetes. Previously, pig and cattle pancreas glands were the only viable method of production. While sufficient for most diabetics, the use of animals to produce insulin did cause some allergic reactions, as it was not a true human match to insulin. Scientists use recombinant DNA gene technology to synthesize insulin. Insulin is composed of two amino acid chains that are joined together. The A chain has 21 amino acids, while the B chain has 30. These amino acid chains have a specific order. The process is somewhat complicated so the following is an excerpt from the Genetech press release explaining the actual scientific process: Insulin is a protein hormone composed of two chains of amino acids: an A chain and a B chain linked together by two disulfide bonds. The A chain is composed of 21 amino acids and the B chain of 30 amino acids, each arranged in a uniquely ordered sequence. Proteins are made by translating the genetic information which is carried in a cells genes. Scientists synthesized in the laboratory genes for the two insulin A and B chains. This was accomplished by chemically linking together small pieces of DNA sequence and then joining them in a specific manner to form complete genes. Once the genes were synthesized, they were stitched into circular DNA strands called plasmids using special enzymes to perform the molecular surgery. Plasmids are rings of DNA which are found within the cell. The newly constructed plasmids containing the transplanted genetic material were introduced into a benign E. coli bacterial strain. Once inside the bacteria, the genes were swit Continue reading >>
Diabetics Not Told Of Insulin Risk
Evidence that thousands of diabetics in Britain may have suffered a deterioration in their health from synthetic insulin has been withheld by the British Diabetics Association, whose role is to advise patients and to protect their interests. The evidence was contained in a report, commissioned by the association and completed six years ago, which highlighted dangers faced by about 10 per cent of the 150,000 diabetics who had been switched from the traditional animal-derived insulin to synthetic human insulin. Some of those adversely affected began, without warning, to go into comas, known as hypoglycaemic episodes or 'hypos'. Some suffered severe injuries, a few crashed their cars, and others believed they would have died had they not been rescued as they lay unconscious. An estimated 15,000 people may still suffer because they are injecting themselves twice a day with insulin that may not suit them. Many doctors are unaware of the problem, or have failed to put their patients back on animal insulin because they do not know it is still available. The association says it did not publish the report because it was 'too alarmist'. Simon O'Neill, head of diabetes care services, said the association agreed that up to 20 per cent of insulin injectors preferred animal insulin and had experienced difficulties with synthetic insulin. He added that the association had published a report, The Insulin Debate, which dealt with the issues, continued to keep members informed of developments, and campaigned to keep animal insulin available to sufferers. Synthetic insulin is manufactured by two major drug companies, the Danish Novo Nordisk and US giant Elli Lilly. Neither company accepts that the synthetic version has negative effects. The report was compiled following 3,000 letters of c Continue reading >>
This article is about the insulin protein. For uses of insulin in treating diabetes, see insulin (medication). Not to be confused with Inulin. Insulin (from Latin insula, island) is a peptide hormone produced by beta cells of the pancreatic islets, and it is considered to be the main anabolic hormone of the body. It regulates the metabolism of carbohydrates, fats and protein by promoting the absorption of, especially, glucose from the blood into fat, liver and skeletal muscle cells. In these tissues the absorbed glucose is converted into either glycogen via glycogenesis or fats (triglycerides) via lipogenesis, or, in the case of the liver, into both. Glucose production and secretion by the liver is strongly inhibited by high concentrations of insulin in the blood. Circulating insulin also affects the synthesis of proteins in a wide variety of tissues. It is therefore an anabolic hormone, promoting the conversion of small molecules in the blood into large molecules inside the cells. Low insulin levels in the blood have the opposite effect by promoting widespread catabolism, especially of reserve body fat. Beta cells are sensitive to glucose concentrations, also known as blood sugar levels. When the glucose level is high, the beta cells secrete insulin into the blood; when glucose levels are low, secretion of insulin is inhibited. Their neighboring alpha cells, by taking their cues from the beta cells, secrete glucagon into the blood in the opposite manner: increased secretion when blood glucose is low, and decreased secretion when glucose concentrations are high. Glucagon, through stimulating the liver to release glucose by glycogenolysis and gluconeogenesis, has the opposite effect of insulin. The secretion of insulin and glucagon into the Continue reading >>
With a speed no longer seen in drug discovery and development, insulin was isolated for the first time in 1921 from animal sources and commercialized within 12 months. Decades later, it took just four years for developers to move from expressing recombinant insulin in bacteria to launching the world's first biotechnology drug product. Scientists Frederick G. Banting and Charles H. Best, working in a lab provided by John J. R. MacLeod at the University of Toronto, isolated the polypeptide hormone and began testing it in dogs. By 1922, with the help of James B. Collip and pharmaceutical company partners, the researchers could purify and produce animal-based insulin in larger quantities. Insulin is produced by beta cells in the pancreas and is the most important hormone in the body to regulate blood glucose levels. A partial or complete lack of insulin causes diabetes, which, untreated, is often fatal by the teenage years. The World Health Organization reports that an estimated 177 million people worldwide have diabetes. Although not a cure, insulin injections have been the standard treatment since 1924. Before insulin was discovered, diabetes was managed through diet, which allowed patients to survive, but generally for just a few years after diagnosis. Remarkable medical results were achieved with the first insulin injections. Doctors finally had a means to offer patients a nearly normal quality of life, and it quickly became necessary to increase insulin production. The Toronto scientists had trouble, however, with consistently isolating and purifying the drug. Connaught Laboratories in Canada, now part of Sanofi-Aventis, assisted, and Eli Lilly & Co. proposed developing large-scale production methods. The university initially rebuffed offers from Lilly, but an agreemen Continue reading >>
Synthetic Insulin :: Dna Learning Center
Genentech, the first biotechnology company, established in 1976. The insulin receptor substrate 1 (IRS1, also known as A0484) is a docking and adaptor protein that is multiply phosphorylated by a variety of protein kinases and is the major substrate of the insulin and insulin-like growth factor receptors (IGFRs). The A and B chains of insulin. Insulin can be isolated from the pancreas of pigs and cows for human use. Charles Best (L) and Frederick Banting (R) discovered insulin, 1928. Walter Gilbert talks about the reasons for making insulin with recombinant DNA. Professor Bruce McEwen describes the blood-brain barrier, which prevents most proteins from accessing the brain. Selective proteins can cross the barrier, instigating processes such as neurogenesis. The 3-phosphoinositide-dependent protein kinase 1 (PDK1 or A0260) is a serine/threonine protein kinase of the AGC group, PKB family. Walter Gilbert's group tried to isolate the human insulin DNA sequence using the rat insulin DNA sequence. Walter Gilbert talks about his group's early success with isolating the rat insulin gene and making recombinant rat insulin. Continue reading >>
How Did They Make Insulin From Recombinant Dna?
Recombinant DNA is a technology scientists developed that made it possible to insert a human gene into the genetic material of a common bacterium. This “recombinant” micro-organism could now produce the protein encoded by the human gene. Continue reading >>
First Successful Laboratory Production Of Human Insulin Announced
South San Francisco, Calif. -- September 6, 1978 -- Genentech, Inc. and City of Hope National Medical Center, a private research institution and hospital in Duarte, California today announced the successful laboratory production of human insulin using recombinant DNA technology. Insulin is a protein hormone produced in the pancreas and used in the metabolism of sugar and other carbohydrates. The synthesis of human insulin was done using a process similar to the fermentation process used to make antibiotics. The achievement may be the most significant advance in the treatment of diabetes since the development of animal insulin for human use in the 1920's. The insulin synthesis is the first laboratory production DNA technology. Recombinant DNA is the technique of combining the genes of different organisms to form a hybrid molecule. DNA (deoxyribonucleic acid), the substances genes are composed of, contains the chemical record in which genetic information is encoded. Scientists at Genentech and City of Hope inserted synthetic genes carrying the genetic code for human insulin, along with the necessary control mechanism, into an E. coli bacterial strain which is a laboratory derivative of a common bacteria found in the human intestine. Once inside the bacteria, the genes were "switched-on" by the bacteria to translate the code into either "A" or "B" protein chains found in insulin. The separate chains were then joined to construct complete insulin molecules. The development of genetically engineered human insulin was funded by Genentech. However, the work was a cooperative effort between Genentech and City of Hope. The synthesis of human insulin gene was accomplished by four scientists at City of Hope Medical Center led by Roberto Crea, Ph.D., and Keichi Itakura, Ph.D. Scien Continue reading >>
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History Of Insulin
Dr Frederick Banting and medical student Charles Best perform experiments on the pancreases of dogs in Toronto, Canada. Professor John Macleod provides Banting and Best with a laboratory to carry out the experiments. When the pancreases are removed the dogs showed symptoms of diabetes. The pancreas was then sliced and ground up into an injectable extract. This is injected a few times a day which helped the dogs to regain health. Given the early success, Macleod wants to see more evidence that the procedure worked and provides pancreases from cows to make the extract which is named ‘insulin’. Bertram Collip, a biochemist, joins the research team to provide help with purifying the insulin to be used for testing on humans. Banting and Best clearly had confidence in the insulin as they were the first humans to test the insulin by injecting themselves with it which caused them to experience weakness and dizziness, signs of hypoglycemia. After the group had experimented enough to gain an understanding of the required doses and how best to treat hypoglycemia, their insulin is deemed ready to be tried on patients. Tweet Type 2 diabetes mellitus is a metabolic disorder that results in hyperglycemia (high blood glucose levels) due to the body: Being ineffective at using the insulin it has produced; also known as insulin resistance and/or Being unable to produce enough insulin Type 2 diabetes is characterised by the body being unable to metabolise glucose (a simple sugar). This leads to high levels of blood glucose which over time may damage the organs of the body. From this, it can be understood that for someone with diabetes something that is food for ordinary people can become a sort of metabolic poison. This is why people with diabetes are advised to avoid sources of dieta Continue reading >>
Tweet Human insulin is the name which describes synthetic insulin which is laboratory grown to mimic the insulin in humans. Human insulin was developed through the 1960s and 1970s and approved for pharmaceutical use in 1982. Before human insulin was developed animal insulin, usually a purified form of porcine (pork) insulin, was used. How is human insulin produced? Human insulin is laboratory created by growing insulin proteins within E-coli bacteria (Escherichia coli). What types of human insulin are available? Human insulin is available in two forms, a short acting (regular) form and an intermediate acting (NPH) form. NPH (Neutral Protamine Hagedorn) insulin, also known as isophane insulin, is a suspension meaning that the insulin vial should be rolled or repeatedly turned upside down to ensure the solution is uniformly cloudy. Some examples of human insulin: Regular (short acting): Humulin S, Actrapid, Insuman Rapid NPH (intermediate acting): Humulin I, Insuman basal, Insulatard Premixed human insulins: Humulin M2, M3 and M5, Insuman Comb 15, 25 and 50 What are premixed human insulins? Premixed insulins consist of a mix of regular and NPH insulin. The premixed insulins are available in a number of different ratios of mixing. For example Humulin M3 is a mix of 30% short acting to 70% intermediate whereas Humulin M5 is made up of 50% of both short and intermediate acting. In recent years there has been a trend to replace human insulins with newer premixed analogue insulins. How quickly do human insulins act? Short acting (regular) insulin starts to act from about 30 minutes after injecting, with their peak action occurring between 2 and 3 hours after injecting. The duration is up to 10 hours. Intermediate acting (NPH) insulin takes about 2 to 4 hours to start acting, h Continue reading >>
The Great Debate: Natural Animal Or Artificial ‘human’ Insulin?
Home » Diabetic Commonsense » The Great Debate: Natural Animal or Artificial ‘Human’ Insulin? Diabetes commonsense The Great Debate: Natural Animal or Artificial ‘Human’ Insulin? Progress towards becoming a well-balanced diabetic is not helped by the wide range and increasing choice of insulins being put on the market. Is this complication really necessary? Over forty varieties of insulin (3) are advertised and none of them would be on the shelves unless manufacturers could make a profit by selling them. Commonsense tells me to complain loudly about having to find my way and make the right choices through the insulin maze. It does not matter if we select the wrong toothpaste or cat food, but insulin is different. The diabetic community cannot survive without this life-saving drug. We therefore form a captive market and, as any economist will tell you, this creates a perfect opportunity for experts to manipulate and exploit us. Have our gurus the time or inclination to guide us through this jungle of short, medium, long-term and mixed insulins? Do they explain the scientific jargon and help us make a free and informed choice? In this search for the right insulin, newly-diagnosed diabetics, handcuffed by ignorance and fear, are particularly vulnerable. No way can they decide for themselves which insulin to use. They have to be guided by the care team who, in these circumstances, have no option but to take control. Let us hope that sooner rather than later, these fledgling diabetics will be able to fly from the nest and act on their own initiative to make an informed choice of which insulin suits them best. Three clues will help us make up our mind. The first is not to abdicate in favour of the care team or encourage them to steal our melody. The second clue is n Continue reading >>
In 1978, Genentech scientist Dennis Kleid toured a factory in Indiana where insulin was being made from pigs and cattle. “There was a line of train cars filled with frozen pancreases,” he says. At the time, it took 8,000 pounds of pancreas glands from 23,500 animals to make one pound of insulin. Diabetics lack this hormone, which regulates the amount of glucose in the blood. The manufacturer, Eli Lilly, needed 56 million animals per year to meet the increasing U.S. demand for the drug. They had to find a new insulin alternative, fast. Genentech had the expertise to make synthetic human insulin—in laboratories, from bacteria, using their recently-proven recombinant DNA technology. But could they make enough of the miniscule insulin molecules to replace these trainloads of pancreases and provide an alternative option for people living with diabetes? The scientists would have to coax the bacteria to produce insulin from the synthetic DNA at high enough concentrations to make an economically viable product. This meant that each bacteria needed to churn out so much of the protein per cell that if they could do it, they’d look like stuffed olives under a microscope. If not, Genentech’s work would have ended as a scientific curiosity, with no new option for diabetics. I don’t want to hear that word, impossible...tell me what you need to get it done. Kleid didn’t think they could get that kind of yield. He told Genentech founder, Bob Swanson, flat-out that it couldn’t be done. But Swanson refused to accept it. “I don’t want to hear that word, impossible,” he told Kleid. “Tell me what you need to get it done.” The high-stakes, high-pressure race to create synthetic insulin had started over a year earlier. Eli Lilly, the main U.S. producer of insulin, ha Continue reading >>
Heres Why Insulin Is So Expensive And What You Can Do About It
The numbers are in: U.S. spending on diabetes drugs increased from $10 billion to $22 billion per year between 2002 and 2012, according to a recent study . And most of that cost was due to skyrocketing prices for one diabetes medication: insulin. Take, for example, Lantus , one of the most popular insulins on the market. The price of a 10-milliliter vial has shot up from under $40 in 2001 to around $275 today. And these costs are hitting more people every year. About 30 million people in the U.S. have diabetes up from 10 million 20 years ago with another 89 million experiencing prediabetes. One study estimates that up to one-third of Americans could have diabetes by 2050. With so many people affected by rising insulin costs, it makes sense to wonder why prices are so high. Today there are two major categories of insulin. Synthetic human insulin was introduced in the early 1980s and appears under brand names like Humulin R and Novolin 70/30 . Genetically modified analog insulin was developed in the 1990s to provide several benefits over human insulin. Analog insulins take effect more quickly, their effects are more consistent and predictable, and they reduce the frequency of low and high blood sugar. Popular analog insulins are Lantus , Humalog , and Novolog . The prices for both types of insulin have risen over the years, but analog insulin is often much more expensive (compare $25 for Novolin 70/30 versus $323 for Humalog 50/50 ). Due to the added convenience and benefits of analog insulin, 96% of insulin prescriptions in the U.S. are now for analogs. However, a growing body of research suggests that synthetic human insulin is just as effective for managing diabetes. Get the best ways to save on your prescriptions delivered to your inbox. Producing insulin is more exp Continue reading >>