What Is Insulin?
Insulin is a hormone made by the pancreas that allows your body to use sugar (glucose) from carbohydrates in the food that you eat for energy or to store glucose for future use. Insulin helps keeps your blood sugar level from getting too high (hyperglycemia) or too low (hypoglycemia). The cells in your body need sugar for energy. However, sugar cannot go into most of your cells directly. After you eat food and your blood sugar level rises, cells in your pancreas (known as beta cells) are signaled to release insulin into your bloodstream. Insulin then attaches to and signals cells to absorb sugar from the bloodstream. Insulin is often described as a “key,” which unlocks the cell to allow sugar to enter the cell and be used for energy. If you have more sugar in your body than it needs, insulin helps store the sugar in your liver and releases it when your blood sugar level is low or if you need more sugar, such as in between meals or during physical activity. Therefore, insulin helps balance out blood sugar levels and keeps them in a normal range. As blood sugar levels rise, the pancreas secretes more insulin. If your body does not produce enough insulin or your cells are resistant to the effects of insulin, you may develop hyperglycemia (high blood sugar), which can cause long-term complications if the blood sugar levels stay elevated for long periods of time. Insulin Treatment for Diabetes People with type 1 diabetes cannot make insulin because the beta cells in their pancreas are damaged or destroyed. Therefore, these people will need insulin injections to allow their body to process glucose and avoid complications from hyperglycemia. People with type 2 diabetes do not respond well or are resistant to insulin. They may need insulin shots to help them better process Continue reading >>
Ask The Diabetes Team
Question: From the United Kingdom: How is artificial insulin made? Answer: What a great question! I'm not sure how much detail you're interested in, but here is the short answer. Insulin is created in a special non-disease-producing laboratory strain of E. coli bacteria (not the same type that causes diarrhea and kidney problems that you may be familiar with) that has been genetically altered by the addition of the gene for human insulin production. The bacteria produces the insulin which is then chemically harvested from the medium in which the bacteria is grown, purified and prepared for human use. Here is the long answer if you are interested: [Note: the following is adapted from Overview of Biotechnology at the End of the 20th Century. Please see that reference for even more details.] Modern biotechnology began when recombinant human insulin was first marketed in the United States in 1982. The effort leading up to this landmark event began in the early 1970's when research scientists developed protocols to construct vectors, by cutting out and pasting pieces of DNA together to create a new piece of DNA (recombinant DNA), that could be inserted into the bacterium, Escherichia coli (transformation). If one of the pieces of the new DNA included a gene which produced a protein enzyme that broke down a particular antibiotic, the bacterium would be resistant to that antibiotic and could grow in a medium containing it. To the piece of DNA that conferred resistance of Escherichia coli to a particular antibiotic was added the human gene for the making of insulin. If this recombinant DNA containing the human insulin gene was used to transform Escherichia coli,and the bacteria were plated on an agar plate containing the antibiotic, the bacteria that grew contained not only the Continue reading >>
Synthetic human insulin is identical to your own. However, relative to the rapid-acting insulin analogs, regular human insulin has several undesirable features. Synthetic human insulin is identical in structure to your own natural insulin. But when it is injected under the skin it doesn’t work as well as natural insulin. This is because injected human insulin clumps together and takes a long time to get absorbed. The activity of this synthetic human insulin is not well synchronized with your body’s needs. In this section, you will find information about: Fast-acting injected insulin Relative to the rapid-acting insulin analogs, Regular human insulin has undesirable features, such as a delayed onset of action, and variable peak and duration of action when it is injected under the skin. Because of this, fewer and fewer medical providers are prescribing Regular insulin. The delayed onset of action is the reason you have to inject the insulin and wait before eating. And the variable duration of action predisposes to low blood sugars long after the meal is over. REGULAR INSULIN IS LESS PREDICTABLE THAN RAPID-ACTING ANALOG VERSIONS when injected under the skin. Long-acting injected insulin NPH (Neutral Protamine Hagedorn) is a longer-acting human insulin that is used to cover blood sugar between meals, and to satisfy your overnight insulin requirement. A fish protein, protamine, has been added to the Regular human insulin to delay its absorption. This long acting insulin is a cloudy suspension that needs to be remixed thoroughly before each injection. Because NPH is a suspension of different sized crystals, it has a very unpredictable absorption rate and action. This results in more frequent low and high blood sugars. The use of NPH has declined with the availability of o Continue reading >>
Pork insulin differs from human by only one amino acid residue, a difference largely invisible to the human immune system, which means that pork insulin is only weakly antigenic and causes few allergic reactions. Porcine insulin was traditionally favoured by the Danish insulin manufacturers, since their farming industry was orientated towards pork rather than beef. Highly purified pork insulin is virtually indistinguishable from biosynthetic human insulin in its clinical effects, although the latter is slightly more soluble and thus absorbed more rapidly. Some patients have reported loss of hypoglycaemic warning symptoms on switching from pork to human insulin and should therefore be treated with their preferred insulin, although objective evidence for this phenomenon is lacking. History The Danish insulin manufacturers Nordisk and Novo began manufacturing pork insulin in the 1920s and produced this almost exclusively thereafter. The decision was based simply upon availability, and it was not appreciated that pork insulin was closer than beef to human insulin until some 50 years later. Danish insulin was always noted for its purity, and was marketed in the 1930s without the addition of disinfectants, considered essential by manufacturers elsewhere. When glucagon was finally eliminated from other insulins in the 1950s, it was already shown to be absent from Novo insulin. See History of glucagon. The introduction of monocomponent (highly purified, single peak) pork insulin in the 1970s stimulated considerable interest in the role of insulin antibodies in modifying the pharmacokinetics of injected insulin and, coincidentally, represented the first involvement of immunologists in the study of diabetes. See the Discovery of type 1 diabetes. Highly purified insulin represente 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 >>
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 History Of Insulin
Since insulin was discovered in 1921, it has become one of the most thoroughly studied molecules in scientific history. Diabetes has been recognized as a distinct medical condition for at least 3,500 years, but its cause was a mystery until early this century. In the early 1920s, researchers strongly suspected that diabetes was caused by a malfunction in the digestive system related to the pancreas gland, a small organ that sits on top of the liver. At that time, the only way to "control" diabetes was through a diet low in carbohydrate and sugar, and high in fat and protein. Instead of dying shortly after diagnosis, this diet allowed diabetics to live - but only for about a year. Exactly what was wrong, or missing, in the sugar metabolism pathway of people with diabetes was unknown until a group of Canadian researchers purified insulin in 1921 and proved that diabetes is a disease of insulin deficiency. As with most major scientific discoveries, the groundwork for the discovery of insulin, had been laid by several others before the Canadian researchers isolated it. In 1889, two European researchers, Minkowski and von Mering, found that when the pancreas gland was removed from dogs, they developed all the symptoms of diabetes and died soon afterwards. Minkowski and von Mering proposed that the pancreas was crucial for sugar metabolism. Later experimenters narrowed the search to the Islets of Langerhans-clusters of specialized cells within the pancreas. In 1910, Sharpey-Shafer of Edinburgh suggested a single chemical was missing from the pancreas in diabetic people. He proposed calling this chemical "insulin," and later the successful Canadian researchers took him up on the suggestion. Meanwhile, an American scientist E. L. Scott was partially successful in extracting ins 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 cell’s 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 bacteri Continue reading >>
What Is Insulin?
The insulin your body makes naturally is a hormone. Insulin helps move sugar from the blood into the body’s cells, where it can be used for energy. The pancreas releases insulin all the time. The pancreas is an organ that sits near the stomach. Special cells in the pancreas, called beta cells, make insulin. In between meals, the pancreas releases a low level of insulin to help the body produce energy. When you eat, your blood sugar (also known as blood glucose) rises. The pancreas releases more insulin to take sugar from the food you eat and bring it to the cells to be changed into energy. This brings the blood sugar level in the blood back down. Insulin works like a key, unlocking cells to help deliver sugar from the blood. Every cell in the body has a lock on its cell wall, called a receptor. Insulin fits into that lock like a key, allowing sugar to enter the cells. When the body is not able to make enough insulin, blood sugar is locked out of the cells, causing it to stay in the bloodstream. This leads to blood sugar building until the levels are too high, which is also called hyperglycemia. This extra sugar is what makes people feel the symptoms of diabetes, such as often feeling tired or thirsty. In the case of diabetes, when the body is either not making enough insulin, or cannot use it properly, insulin therapy is often used to replace what the body no longer produces. History of Insulin Therapy From the 1920s to the 1980s, insulin from animals is used for treatment In the 1980s, the first generation of man-made insulin, called "human insulin," is created. This man-made insulin was genetically identical to the body’s naturally produced insulin By the late 1990s, man-made insulin analogs were being developed. Insulin analogs are similar to regular human insuli Continue reading >>
Ocr Gateway Triple Science Topics
Genetic engineering can be used to create organisms that produce large amounts of useful substances - for example, bacteria can be engineered to produce human insulin to treat diabetics. Genetic engineering can also be used to create and store DNA fingerprints, which can be used for identification purposes. Genetic engineering Genetic engineering involves altering the genetic code of an organism by inserting a gene or genes from another organism. Bacteria can be genetically engineered (genetically modified) to produce useful human proteins including human growth hormone and human insulin. One advantage of using bacteria is that they can be grown in large fermenters, producing large amounts of these useful proteins. You should be able to describe the main stages in genetic engineering, and in particular how this works for engineering bacteria to produce human insulin. Main stage Insulin example Desired gene is identified Human insulin gene is identified The gene is removed from the organism’s DNA The gene for making human insulin is cut out of some human DNA The DNA in other organism is cut open A loop of bacterial DNA is cut open The gene is inserted into the cut DNA The human insulin gene is inserted into the cut loop, and this loop is inserted into a bacterial cell The inserted gene works in the transgenic (genetically engineered) organism The bacterial cell produces human insulin The transgenic organism is cloned to produce lots of identical copies The transgenic bacterium is cloned to make lots of copies Large amounts of human insulin is collected The animation shows how this works. You have an old or no version of Flash - you need to upgrade to view this content! Go to the WebWise Flash install guide DNA fingerprinting A person’s DNA is unique to them. Their DN Continue reading >>
Why Is Insulin So Expensive In The U.s.?
Dr. Jeremy Greene sees a lot of patients with diabetes that's out of control. In fact, he says, sometimes their blood sugar is "so high that you can't even record the number on their glucometer." Greene, a professor of medicine and history of medicine at Johns Hopkins University, started asking patients at his clinic in Baltimore why they had so much trouble keeping their blood sugar stable. He was shocked by their answer: the high cost of insulin. Greene decided to call some local pharmacies, to ask about low-cost options. He was told no such options existed. "Only then did I realize there is no such thing as generic insulin in the United States in the year 2015," he says. Greene wondered why that was the case. Why was a medicine more than 90 years old so expensive? He started looking into the history of insulin, and has published a paper about his findings in this week's issue of the New England Journal of Medicine. The story of insulin, it turns out, starts back in the late 1800s. That's when scientists discovered a link between diabetes and damaged cells in the pancreas — cells that produce insulin. In the early 1920s, researchers in Toronto extracted insulin from cattle pancreases and gave it to people who had diabetes, as part of a clinical trial. The first patient was a 14-year-old boy, who made a dramatic recovery. Most others recovered as well. Soon, insulin from pigs and cattle was being produced and sold on a massive scale around the world. But for some, the early forms of the medicine weren't ideal. Many people required multiple injections every day, and some developed minor allergic reactions. Over the next few decades, scientists figured out how to produce higher-quality insulin, Greene says. They made the drug purer, so recipients had fewer bad reaction Continue reading >>
"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 >>
You And Your Hormones
What is insulin? Insulin is a hormone made by an organ located behind the stomach called the pancreas. Here, insulin is released into the bloodstream by specialised cells called beta cells found in areas of the pancreas called islets of langerhans (the term insulin comes from the Latin insula meaning island). Insulin can also be given as a medicine for patients with diabetes because they do not make enough of their own. It is usually given in the form of an injection. Insulin is released from the pancreas into the bloodstream. It is a hormone essential for us to live and has many effects on the whole body, mainly in controlling how the body uses carbohydrate and fat found in food. Insulin allows cells in the muscles, liver and fat (adipose tissue) to take up sugar (glucose) that has been absorbed into the bloodstream from food. This provides energy to the cells. This glucose can also be converted into fat to provide energy when glucose levels are too low. In addition, insulin has several other metabolic effects (such as stopping the breakdown of protein and fat). How is insulin controlled? When we eat food, glucose is absorbed from our gut into the bloodstream. This rise in blood glucose causes insulin to be released from the pancreas. Proteins in food and other hormones produced by the gut in response to food also stimulate insulin release. However, once the blood glucose levels return to normal, insulin release slows down. In addition, hormones released in times of acute stress, such as adrenaline, stop the release of insulin, leading to higher blood glucose levels. The release of insulin is tightly regulated in healthy people in order to balance food intake and the metabolic needs of the body. Insulin works in tandem with glucagon, another hormone produced by the pan 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 >>
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 >>