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What Are The Major Drawbacks Of Using Insulin Purified From Animals

What Is Genetic Engineering? - Definition And Examples

What Is Genetic Engineering? - Definition And Examples

How do we make the insulin used by diabetic patients? In this lesson, you'll learn the basics of how genetic engineering can be used to transform a bacterial host cell into a genetically-modified organism that produces human insulin. Diabetes is a disease in which the patient has trouble regulating his or her blood glucose level. Until the early 1900s, this was a deadly disease. Imbalanced glucose levels would induce coma and eventually death. Arguably, one of the greatest medical discoveries of the twentieth century was the development of genetic engineering technology. Let's imagine ourselves in the shoes of scientists struggling to develop a cure for diabetic-induced death. For some diabetic patients, uncontrolled glucose levels is simply the result of a lack of a hormone called insulin. Insulin facilitates glucose transport into cells, thus lowering blood glucose levels. If that's true, we should be able to treat this form of diabetes by providing the diabetic patient with insulin. Okay. Easier said than done. Where are we going to get all this insulin? Scientists eventually determined that insulin purified from animals like cattle or pigs was sufficient to treat the insulin deficiency in these diabetic patients. While this was a major medical breakthrough, the animal substitute wasn't without its side effects. Some patients suffered an allergic reaction. As we will see, genetic engineering would eventually solve this problem and pave the way for an entire new field of scientific and medical possibilities. Genetic Engineering Genetic engineering is the process by which scientists modify the genome of an organism. Creation of genetically modified organisms requires recombinant DNA. Recombinant DNA is a combination of DNA from different organisms or different location Continue reading >>

Downstream Processing

Downstream Processing

Downstream processing refers to the recovery and purification of biosynthetic products, particularly pharmaceuticals, from natural sources such as animal or plant tissue or fermentation broth, including the recycling of salvageable components and the proper treatment and disposal of waste. It is an essential step in the manufacture of pharmaceuticals such as antibiotics, hormones (e.g. insulin and humans growth hormone), antibodies (e.g. infliximab and abciximab) and vaccines; antibodies and enzymes used in diagnostics; industrial enzymes; and natural fragrance and flavor compounds. Downstream processing is usually considered a specialized field in biochemical engineering, itself a specialization within chemical engineering, though many of the key technologies were developed by chemists and biologists for laboratory-scale separation of biological products. Downstream processing and analytical bioseparation both refer to the separation or purification of biological products, but at different scales of operation and for different purposes. Downstream processing implies manufacture of a purified product fit for a specific use, generally in marketable quantities, while analytical bioseparation refers to purification for the sole purpose of measuring a component or components of a mixture, and may deal with sample sizes as small as a single cell. Stages[edit] A widely recognized heuristic for categorizing downstream processing operations divides them into four groups which are applied in order to bring a product from its natural state as a component of a tissue, cell or fermentation broth through progressive improvements in purity and concentration. Removal of insolubles is the first step and involves the capture of the product as a solute in a particulate-free liquid, for e Continue reading >>

Humulin : Synthetic Insulin

Humulin : Synthetic Insulin

Humulin is synthetic human insulin prepared by using genetic engineering. Humulin is manufactured from DNA sources in laboratory, using recombinant DNA technology. Synthetic insulin is also called genetically engineered insulin. The synthetic insulin (humulin) is as effective as hormone insulin secreted by human pancreas. What is Humulin? Humulin is synthetic human insulin prepared by using genetic engineering. Humulin is manufactured from DNA sources in laboratory, using recombinant DNA technology. Synthetic insulin is also called genetically engineered insulin. The synthetic insulin (humulin) is as effective as hormone insulin secreted by human pancreas. Synthesis of Humulin In 1978, scientists synthesized human insulin from E.coli bacteria using recombinant DNA technology, by preparing two DNA sequences for A and B chains of human insulin and introduced them in plasmid of E.coli. This led to production of human insulin chain. Eli Lilly, an American company marketed the first human insulin called humulin in 1983. Eli Lilly and Ranbaxy launched a new insulin project namely Humalog (an analog of 5, 6 human insulin), which is more expensive than human insulin products, but have good absorption in body, as compared to other insulin products. Genetically engineered Insulin : Humulin, preferred over old animal based products Structure of Insulin Insulin is a proteinaceous hormone secreted by beta-cells of islets of langerhans of pancreas. Insulin controls, blood sugar level and when there is less secretion of insulin, it results in diabetes (high blood- sugar level). In 1954, Frederick Sanger determined primary structure of Insulin. Insulin is a protein formed by two polypeptide chains: A-chain and B-chain, interlinked by two sulphide bonds (see fig). A-chain is formed of 2 Continue reading >>

Animal-cell Culture Media: History, Characteristics, And Current Issues

Animal-cell Culture Media: History, Characteristics, And Current Issues

Abstract Cell culture technology has spread prolifically within a century, a variety of culture media has been designed. This review goes through the history, characteristics and current issues of animal-cell culture media. A literature search was performed on PubMed and Google Scholar between 1880 and May 2016 using appropriate keywords. Results At the dawn of cell culture technology, the major components of media were naturally derived products such as serum. The field then gradually shifted to the use of chemical-based synthetic media because naturally derived ingredients have their disadvantages such as large batch-to-batch variation. Today, industrially important cells can be cultured in synthetic media. Nevertheless, the combinations and concentrations of the components in these media remain to be optimized. In addition, serum-containing media are still in general use in the field of basic research. In the fields of assisted reproductive technologies and regenerative medicine, some of the medium components are naturally derived in nearly all instances. Conclusions Further improvements of culture media are desirable, which will certainly contribute to a reduction in the experimental variation, enhance productivity among biopharmaceuticals, improve treatment outcomes of assisted reproductive technologies, and facilitate implementation and popularization of regenerative medicine. 1 Introduction The influence of cell culture technology on human society has been immeasurable. Progress in biology in recent years, for example, has depended heavily on cell culture technology.[1] In addition, cell culture-based practical technologies have been developed in various areas, including the assessment of the efficacy and toxicity of new drugs, manufacture of vaccines and biophar Continue reading >>

Gm Vs Animal Insulin

Gm Vs Animal Insulin

Home » About Diabetes » GM Vs Animal Insulin Choices – The Evidence Evidence from people with diabetes A little bit of history Facts Action and duration times of animal and GM ‘human’ insulins Hypoglycaemia and loss of warnings ‘Dead in Bed Syndrome’ The concerns of patients are justified Availability of animal insulins in the UK Changing your insulin What to do if your consultant refuses to change your insulin Availability of animal insulin if admitted to hospital Frequently asked questions Allergic reactions to insulin Choices – The Evidence The NHS has always allowed patients to have an informed choice of treatment before they make their treatment decisions and this includes information about risks and benefits. In recent years, greater emphasis has been placed on informed choice as a result of NHS policy which puts patients at the centre of care and encourages involvement in their treatment decisions so that in the ideal world, patients and their doctors make decisions jointly. The treatment of diabetes is no exception and therefore people with insulin-requiring diabetes, whether Type 1 or Type 2 diabetes should have an informed choice of insulins and should be given information about risks and benefits. IDDT has always argued that this should be the case and so if people have a preference for natural pork or beef insulins, whether this is due to adverse reactions to GM synthetic insulins or simply personal preference, then their views should be respected. IDDT advocates the same principles should apply to the newer insulin analogues. The importance of high quality evidence to inform our decisions When new drugs, including new insulins, reach the market the research has been in limited numbers of people. Often this early research only involves a highly Continue reading >>

'human' Insulin Versus Animal Insulin In People With Diabetes Mellitus

'human' Insulin Versus Animal Insulin In People With Diabetes Mellitus

Human insulin has become the insulin of choice for newly diagnosed patients with diabetes mellitus. Insulin companies are eventually not going to maintain different species formulations for a declining proportion of the population with diabetes using animal insulin. Concerns exist about increased hypoglycaemia following transfer to human insulin and availability of animal insulin especially in developing countries. In our systematic review we could not identify substantial differences in the safety and efficacy between insulin species. Many important patient-oriented outcomes like health-related quality of life and effects on diabetic complications and mortality were never investigated. Human insulin was introduced into the market without scientific proof of advantage over existing purified animal insulins, especially porcine insulin. A comparison of the effects of human and animal insulin as well as of the adverse reaction profile did not show clinically relevant differences. Many patient-oriented outcomes like health-related quality of life or diabetes complications and mortality were never investigated in high-quality randomised clinical trials. The story of the introduction of human insulin might be repeated by contemporary launching campaigns to introduce pharmaceutical and technological innovations that are not backed up by sufficient proof of their advantages and safety. Continue reading >>

Animal Insulin Vs Synthetic Insulin: Similar Genes, Different Origins

Animal Insulin Vs Synthetic Insulin: Similar Genes, Different Origins

Humans with diabetes started using insulin extracted from the pancreas of cows or pigs in 1922. Some people developed allergies to animal (or natural) insulin, but its use saved countless lives. Today, most people who need it use synthetic or human insulin, first manufactured in the early 1980s. Though many individuals complained of side effects after switching from animal to synthetic insulin, the synthetic type is now prescribed almost exclusively in many parts of the world. Whether natural or synthetic, the therapeutic use of insulin by humans depends on our similarity to nonhuman creatures. Our Genetic Cousins Proteins are similar to a string of beads, and the “beads” are called amino acids. The amino acids that make up our human insulin protein are nearly identical to the string of amino acids in cow and pig insulin. Pork insulin is different by one amino acid, and bovine insulin by three – similar enough for most humans to use. In the 1950s, when the complete protein structure of insulin was deciphered, some companies began modifying animal insulin. They removed the different amino acid from pig insulin, replacing it with the human counterpart. So, other than its origin, the pig insulin was made human. Although insulin was being modified before the creation of the synthetics, the production of synthetic insulin has nothing to do with altering the proteins of other mammals. It involves life forms much smaller. Synthetic Soup A protein, such as insulin, is created when its amino acid sequence (genetic information) is copied and then reproduced. Scientists who have learned the genetic sequence of human insulin create copies of it by splicing together pieces of genetic material in the proper order. Circular strands of DNA, called plasmids, are extracted from bac Continue reading >>

How Insulin Is Made - Material, Manufacture, History, Used, Parts, Components, Structure, Steps, Product

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 >>

Human Insulin And Recombinant Dna Technology

Human Insulin And Recombinant Dna Technology

Impaired insulin production in the beta cells of pancreas leads to the condition known as Diabetes Miletus. To treat the diabetic patient researchers produced Humulin using recombinant DNA technology by inserting human insulin gene into a vector (E. coli)... Introduction: Impaired insulin production in the beta cells of pancreas leads to the condition known as Diabetes Miletus. The bovine and porcine insulin are used to treat Patients with diabetes mellitus. But the composition of bovine and porcine insulin are slightly different from the human insulin, consequently the patient's immune system produced antibodies against animal origin insulin and also these antibodies induced inflammatory response at injection sites. Antibodies also neutralised the biological action of animal origin insulin. To overcome all these problems researchers produced Humulin using recombinant DNA technology by inserting human insulin gene into a vector (E. coli). Humulin Production Method: 1. DNA coding for A and B polypeptide chains of insulin are chemically synthesised a in the lab. Sixty three nucleotides are sequenced to produce A chain of insulin and ninety nucleotide long DNA designed to produce B chain of insulin, plus terminator codon is added at the end of each chain sequence. Anti-codon for methionine is added at the beginning of the sequence to distinguish humulin from the other bacterial proteins. 2. Chemically synthesized A and B chain DNA sequence are inserted into one of the marker gene which are present in the plasmid vector. Genes are inserted into the plasmid with the help of enzymes known as endonuclease and ligase. 3. The vector plasmids with the insulin gene are then introduced into the E. coli bacterial cell. These cells are then allowed to replicate by mitosis, along with Continue reading >>

Porcine Insulin

Porcine Insulin

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 >>

Insulin Side Effects

Insulin Side Effects

Applies to insulin: injectable liquid, injectable solution, subcutaneous suspension Endocrine Hypoglycemia is the most common and serious side effect of insulin, occurring in approximately 16% of type 1 and 10% of type II diabetic patients (the incidence varies greatly depending on the populations studied, types of insulin therapy, etc). Although there are counterregulatory endocrinologic responses to hypoglycemia, some responses are decreased, inefficient, or absent in some patients. Severe hypoglycemia usually presents first as confusion, sweating, or tachycardia, and can result in coma, seizures, cardiac arrhythmias, neurological deficits, and death. Blood or urine glucose monitoring is recommended in patients who are at risk of hypoglycemia or who do not recognize the signs and symptoms of hypoglycemia. The risk for developing hypoglycemia is higher in patients receiving intensive or continuous infusion insulin therapy. The association between insulin and dyslipidemia is currently being evaluated.[Ref] Permanent neuropsychological impairment has been associated with recurrent episodes of severe hypoglycemia. In one retrospective study of 600 randomly selected patients with insulin-treated diabetes mellitus, the only reliable predictors of severe hypoglycemia were a history of hypoglycemia, a history of hypoglycemia-related injury or convulsion, and the duration of insulin therapy. Those with a history of hypoglycemia had been treated with insulin for 17.4 years, which was significantly longer than the 14.3 years in the insulin-treated patients without a history of hypoglycemia. Human insulin does not appear to be associated with hypoglycemic episodes more often than animal insulin. Caution is recommended when switching from animal (either bovine or pork) to purified Continue reading >>

[advantages And Drawbacks Of Human Insulin].

[advantages And Drawbacks Of Human Insulin].

Abstract Insulin (I) preparations used formerly contained a large number of protein contaminants which are thought to be immunogenic and, hence, caused lipodystrophy, I-allergy and sometimes antibody-mediated I-resistance in many patients. Monocomponent (MC)-I and human I (HI) are virtually free of these peptides and are, therefore, very rarely accompanied by the above mentioned immunologic side effects. In this respect, however, HI offers only little advantage over MC-I although HI is the least immunogenic I. On the other hand, the formation of antibody to I in the diabetic mother is an important determinant of fetal outcome. And since children from diabetic mothers treated with HI are less frequently macrosomic, the use of HI is strongly recommended in women with diabetes before and during their childbearing years. Neutral HI action is somewhat shorter, although clinically not to a relevant extent and, furthermore, metabolic control is not improved by using HI compared wtih MC-I. These findings have been regarded as disadvantages of HI, together with the fact that about 20% of HI-treated patients experience a change of hypoglycemia symptoms during the course of their illness. While autonomic symptoms become weaker or disappear, patients have to react to neuroglycogenic symptoms which normally remain constant. However, the incidence of hypoglycemic events does not change during treatment with HI. Several reasons for this change of symptoms are discussed, such as long duration of diabetes, intensified therapy with near-normoglycemia, development of autonomic neuropathy, alcoholic beverages, and often insufficient instruction of patients.(ABSTRACT TRUNCATED AT 250 WORDS). Continue reading >>

Gmo Cheerios Vs. Gmo Insulin

Gmo Cheerios Vs. Gmo Insulin

The recent decision of General Mills to produce GMO-free Cheerios is interesting from marketing, political, and biological angles. However, what I am interested in most is if GMO Inside and other anti-GMO groups will realize that the process of producing the GMO ingredients in Cheerios (corn starch and sugar) is identical in principle to the way insulin—and many other drugs, like your dog’s rabies shot—is made. If they adamantly insist on GMO-free food products, how can they not extend their request to all pharmaceutical products made with the same genetic engineering technology? If we must have GMO-free Cheerios, then we must have GMO-free insulin, right? Insulin is made, in principle, the same way the GMO corn starch and GMO sugar in Cheerios is. To start, the DNA sequence for human insulin is inserted into the bacteria E. coli, which creates an organism that now has DNA from two very different species in it. This new E. coli is a genetically modified organism (GMO) and serves as a cheap factory for mass-producing the human insulin protein. After a while, the E. coli bacteria has produced large amounts of the human protein to the point where the protein can be extracted from the bacteria cells and purified before being packaged into insulin shots. The insulin protein produced via genetic engineering is chemically identical to the insulin protein made in a healthy human body. Genetically engineered plants are made through a very similar process. A gene of particular interest is inserted into a plant. (For details on how exactly this happens, check out this video from GMO Answers.) This gene may be useful for insect resistance, like the Bt genes, or useful for other agricultural purposes. Eventually the plant is harvested and processed for its crop. The actual pla Continue reading >>

Host Cells For The Production Of Biopharmaceuticals

Host Cells For The Production Of Biopharmaceuticals

Many of biopharmaceuticals, especially proteins : produced by recombinant DNA technology using various expression systems Expression systems : E. coli, Bacillus, Yeast(Saccharomyces cerevisiae) , Fungi(Aspergillus), animal cells (CHO), plant cells, insect cells ïƒ E. coli and mammalian cells : most widely used Typical biopharmaceuticals produced by recombinant DNA technology : Cytokines, therapeutic proteins, etc. Use of appropriate expression system for specific biopharmaceuticals : - Each expression system displays its own unique set of advantages and disadvantages - Expression level (soluble form), Glycosylation, Easy purification, cultivation process, cell density ïƒ Cost effectivenessïƒ feasibility Production system for therapeutic proteins - Cultured in large quantity, inexpensively and in a short time by standard cultivation methods Eschericia coil Most common microbial species to produce heterologous proteins of therapeutic interest - Heterologous protein : protein that does not occur in host cells ex) The first therapeutic protein produced by E. coli : Human insulin (Humulin) in 1982, tPA (tissue plasminogen activator) in 1996 Major advantages of E. coli - Served as the model system for prokaryotic genetics ïƒ Its molecular biology is well characterized - High level expression of heterologous proteins : - High expression promoters (~30 % of total cellular protein - Easy and simple process : Rapid growth, simple and inexpensive media, appropriate fermentation technology, large scale cultivation Intracellular accumulation of proteins in the cytoplasm Complicate downstream processing compared to extracellular production Additional primary processing steps : cellular homogenization, subsequent removal of cell debris by filtration or centrifugation Extensive Continue reading >>

Animal Insulin

Animal Insulin

Tweet Animal insulin was the first type of insulin to be administered to humans to control diabetes. Animal insulin is derived from cows and pigs. Until the 1980s, animal insulin was the only treatment for insulin dependent diabetes. These days the use of animal insulin has largely been replaced by human insulin and human analogue insulin, however, animal insulin is still available on prescription. How is animal insulin produced? As the name suggests animal insulin is taken from the pancreases of animals, usually pigs (porcine or pork insulin) and cows (bovine or beef insulin). The insulin is purified which reduces the chance of the insulin user developing a reaction to the insulin. Can animal insulin be prescribed? Animal insulin, under the name Hypurin, is being produced by Wockhardt UK and is available on prescription. What types of animal insulin are available? Animal insulins are available in 3 different types of action and durations, short acting, intermediate and long acting: Short acting: Hypurin Porcine Neutral, Hypurin Bovine Neutral Intermediate acting: Hypurin Porcine Isophane, Hypurin Bovine Isophane Long acting: Hypurin Bovine lente, Hypurin Bovine PZI (protamine zinc insulin) Premixed: Hypurin Porcine 30/70 What are premixed animal insulins? Premixed animal insulins combine a ratio of short acting and intermediate insulin. For example, Hypurin Porcine consists of 30% short acting and 70% intermediate acting insulin. How quickly do animal insulins act? Short acting animal insulin starts to act from about 30 minutes after injecting, with their peak action occurring between 3 and 4 hours after injecting. The duration is up to 8 hours. Intermediate acting animal insulin takes about 4 to 6 hours to start acting, has its peak activity between 8 and 14 hours and Continue reading >>

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