Human Insulin And Porcine Insulin In The Treatment Of Diabetic Children: Comparison Of Metabolic Control And Insulin Antibody Production.
Semisynthetic human insulin and highly purified porcine insulin were compared in a double blind crossover study in 21 diabetic children. Glycosylated haemoglobin values at the end of four month treatment periods were higher after treatment with human insulin than after treatment with porcine insulin (mean 15.7% (SD 2.3%) v 14.2% (2.3%); p less than 0.01). Higher fasting blood glucose concentrations occurred during treatment with human insulin than with porcine insulin (mean 12.0 (SD 2.1) v 11.0 (2.4) mmol/1; mean 216 (SD 38) v 198 (43) mg/100 ml; p less than 0.05), but there were no significant differences at other time points during the day. The incidence of hypoglycaemia was similar for both treatment groups. Concentrations of antibody reactive with porcine and human insulins were similar for the two treatment groups, although greater fluctuation was observed in the amount of antibody reactive with human insulin. Semisynthetic human insulin is safe and effective in diabetic children, although further work is needed to devise regimens which achieve optimal blood glucose control. Full text Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (649K), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References. These references are in PubMed. This may not be the complete list of references from this article. Continue reading >>
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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 These days the use of animal insulin has largely been replaced by human insulin and human analogue insulin, however, animal insulin is still available on prescription.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 >>
Insulin Analog
An insulin analog is an altered form of insulin, different from any occurring in nature, but still available to the human body for performing the same action as human insulin in terms of glycemic control. Through genetic engineering of the underlying DNA, the amino acid sequence of insulin can be changed to alter its ADME (absorption, distribution, metabolism, and excretion) characteristics. Officially, the U.S. Food and Drug Administration (FDA) refers to these as "insulin receptor ligands", although they are more commonly referred to as insulin analogs. These modifications have been used to create two types of insulin analogs: those that are more readily absorbed from the injection site and therefore act faster than natural insulin injected subcutaneously, intended to supply the bolus level of insulin needed at mealtime (prandial insulin); and those that are released slowly over a period of between 8 and 24 hours, intended to supply the basal level of insulin during the day and particularly at nighttime (basal insulin). The first insulin analog approved for human therapy (insulin Lispro rDNA) was manufactured by Eli Lilly and Company. Fast acting[edit] Lispro[edit] Main article: Insulin lispro Eli Lilly and Company developed and marketed the first rapid-acting insulin analogue (insulin lispro rDNA) Humalog. It was engineered through recombinant DNA technology so that the penultimate lysine and proline residues on the C-terminal end of the B-chain were reversed. This modification did not alter the insulin receptor binding, but blocked the formation of insulin dimers and hexamers. This allowed larger amounts of active monomeric insulin to be available for postprandial (after meal) injections.[1] Aspart[edit] Main article: Insulin aspart Novo Nordisk created "aspart" and Continue reading >>
Two Tons Of Pig Parts: Making Insulin In The 1920s
To kick off National Diabetes Month, pharmacy curator Diane Wendt shares how the Smithsonian has covered the history of insulin manufacturing. I recently picked up a copy of Diabetes Forecast (The American Diabetes Association's healthy living magazine) featuring Supreme Court Justice Sonia Sotomayor on the cover. In her autobiography My Beloved World published earlier this year, Sotomayor recounts her experience living with diabetes since being diagnosed with Type 1 at the age of seven. The stories of successful and celebrated people like Sotomayor are inspirational for all of us, but especially meaningful to the millions of Americans also affected by diabetes. But what really caught my curatorial eye was the magazine's article about making insulin, because that happens to be the subject of a small display that opened last week at the museum called The Birth of Biotech. Both the magazine article and our display focus on the extraordinary technology developed in the late 1970s by which living microorganisms are genetically modified with a human gene in order to produce insulin for our use. Since the discovery of insulin in 1921-1922 by a team of Canadian researchers, making insulin for the treatment of diabetes has always depended on living organisms. However, before the advent of biotechnology, the organisms used were the pigs and cows destined for our dinner plates—specifically, their pancreas glands, a waste product of the meatpacking industry. According to the article in Diabetes Forecast, more than two tons of pig parts were needed to extract just eight ounces of purified insulin. Lucky for us, both pork- and beef-derived insulin are nearly identical to human insulin and can be utilized by our bodies to convert the carbohydrates we eat into energy. In the early 1 Continue reading >>
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Porcine Vs Bovine Insulins
Since no recombinant canine insulin is available, use of bovine or porcine insulin to treat diabetic dogs is common because the B chains of canine, bovine, and porcine insulin are identical. However,whereas canine and porcine A chains have identical amino acid sequences, canine and bovine insulins differ at positions 8 and 10. Therefore, porcine insulin can be considered a self-antigen in dogs,whereas bovine insulin is a heterologous protein. A prospective observational study was conducted in diabetic dogs to determine whether treatment with heterologous insulin is more likely to stimulate production of antiinsulin antibodies (AIA) than is treatment with homologous insulin. The objectives were to determine the prevalence of insulin autoantibodies in untreated dogs, test the hypothesis that heterologous insulin is more immunogenic than homologous insulin, and determine the subunit specificity and isotype of AIA in insulin-treated dogs.Test groups were 1) diabetic dogs sampled before insulin therapy; 2) diabetic dogs sampled after treatment with porcine (homologous) insulin, bovine (heterologous) lente insulin, or bovine protamine zinc insulin; and 3) nondiabetic control dogs. Sera were analyzed for antibodies against porcine insulin; bovine insulin; insulin A, B, or C peptides; and control antigens (canine distemper virus [CDV] and canine thyroglobulin [TG]). Canine isotype-specific antibodies were used to determine total and antiinsulin IgG1:IgG2 ratios. CDV and TG reactivity did not differ among the groups.There was no significant difference in AIA between control and porcine insulin–treated diabetic dogs.A small proportion of dogs demonstrated AIA before diagnosis, consistent with an autoimmune response. Antibody development after treatment was most predominant in d Continue reading >>
Comparison Of Human Versus Porcine Insulin In Treatment Of Diabetes In Children.
The blood glucose control obtained when using semi-synthetic monocomponent human insulin (insulin A) was compared with that using standard monocomponent porcine insulin (insulin B) in 14 children in a double blind crossover study. At the start of the study age, duration of diabetes, insulin dose, and daily carbohydrate intake were the same in both groups. After a one month run in period of standard treatment with porcine insulin the children were randomly divided into group 1 (three months of insulin A followed by three months of insulin B) and group 2 (three months of insulin B followed by three months of insulin A). During each treatment period blood glucose control was assessed by clinical symptoms, glycosylated haemoglobin, and home blood glucose monitoring. Although a significant difference in the period after lunch during 24 hour blood glucose profiles suggested a shorter onset time and faster peak action time of human insulin, no significant difference in the overall diabetic control was seen between the two types of insulin. There was a trend towards improved blood glucose control (irrespective of insulin) as the trial progressed. No clinical reactions to human insulin occurred, and there was no significant difference in the daily insulin dose between porcine and human insulin. Full text Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (411K), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References. These references are in PubMed. This may not be the complete list of references from this article. Articles from British Medical Journal (Clinical Research Ed.) are provided here courtesy of BMJ Publishing Group Continue reading >>
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Insulin Allergy: Differences In The Binding Of Porcine, Bovine, And Human Insulins With Anti-insulin Ige
We investigated in vitro binding of insulins of various species sources (bovine, porcine, and human) with anti-insulin reaginic immunoglobulins (IgE) in 10 patients with systemic insulin allergy and in 5 nonallergic but insulin-resistant cases. Anti-insulin IgE had a higher avidity for bovine compared with porcine insulin in both groups. Avidity for bovine insulin was also significantly higher compared with human or desalanine porcine insulin in the insulin-allergic patients. These observations provide a rationale for using porcine insulin in the treatment of systemic insulin allergy. The efficacy of diet therapy used for one patient with the newly classified maturity-onset diabetes of the young (MODY) is reported. Using the conventional American Diabetes Association's food exchange system with appropriate caloric restriction, the patient's weight was reduced from 25% to 6% above ideal body weight in the 14-wk study. Results of three meal tolerance tests compared with a group of lean, normal subjects revealed a steady improvement from baseline and postprandial hyperglycemia, with concomitant normalization of the counterregulatory hormones as well as hemoglobin A1, free fatty acids, and subsequent euglycemia. This case demonstrates the effectiveness of dietary manipulation as the major therapy in MODY with obesity. Pay Per Article - You may access this article (from the computer you are currently using) for 1 day for US$35.00 Regain Access - You can regain access to a recent Pay per Article purchase if your access period has not yet expired. Numerous studies have shown that patients with diabetes mellitus have accelerated atherosclerotic vascular disease, and major advances in understanding its pathogenesis have been made. Current suggestions are that endothelial injury Continue reading >>
Semi-synthesis Of Human Insulin By Trypsin-catalysed Replacement Of Ala-b30 By Thr In Porcine Insulin
HUMAN insulin differs from porcine insulin by a single amino acid (Thr instead of Ala) at the C-terminal residue of the B-chain. Inouye et al.1 have established a procedure for the semi-synthesis of human insulin, in which trypsin is used as a catalyst for the coupling of desoctapeptide-(B23–B30)-insulin (DOI) with a synthetic octapeptide corresponding to positions B23–B30 of human insulin. DOI was prepared by tryptic digestion of porcine insulin. The enzymatic method has many advantages, in particular, better yields and simple operation, over the chemical methods originally used by Ruttenberg2 and Obermeier and Geiger3. Here we report a more simple and economical method for the semi-synthesis, in which trypsin can catalyse the coupling between desalanine-B30-insulin (DAI) and Thr-OBut to generate human insulin in good yield. Continue reading >>
Porcine Insulin Zinc Suspension In The Management Of Feline Diabetes Mellitus (sponsored By Intervet Schering-plough Animal Health)
Vetsulin (porcine insulin zinc suspension) is approved by the FDA for reducing hyperglycemia and hyperglycemia-associated clinical signs in cats with diabetes mellitus. Internationally, it was first approved for use in the early 1990s and is registered for dogs and cats as Caninsulin in more than 30 other countries. Vetsulin is supplied as a sterile injectable suspension in multidose vials of either 2.5 ml or 10 ml of 40 U/ml (U-40) porcine insulin zinc suspension. Vials are supplied in cartons of one 10-ml vial and cartons containing ten 2.5-ml vials. Vetsulin should be administered using a U-40 insulin syringe. Use of a syringe other than a U-40 will result in incorrect dosing. Vetsulin should be kept refrigerated. It is good clinical practice to replace opened vials on a monthly basis. Species differences in insulin Pork insulin is a protein composed of 51 amino acids, arranged in two chains (an acidic A chain and a basic B chain) cross-linked by disulphide bridges.1 The amino acid sequence of insulin is highly conserved among vertebrates, with little variation in the amino acid sequence of the 21 amino acid A chain and the 30 amino acid B chain. Pork insulin has the same A-chain structure as canine and human insulin but differs slightly from feline insulin, as shown in Table 1. Pork insulin has the same B-chain structure as canine, feline, and bovine insulin but differs slightly from human insulin, as shown in Table 1. Insulin from one mammal is biologically active in another. All mammalian insulins, irrespective of species origin, bind with a similar affinity to insulin receptors at the three sites of action—muscle, adipocyte, and hepatocyte—and initiate post receptor events in terms of autophosphorylation.2 Pork insulin is used effectively and safely in long-t Continue reading >>
Control Of Diabetes Mellitus In Cats With Porcine Insulin Zinc Suspension
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Porcine
Porcine insulin (from pigs) is an exact amino acid match to that of dogs. It differs from human insulin in one position. At B #30 on the B insulin chain, dogs and pigs have Alanine, while people have Threonine. It differs from bovine in two positions, both on the A insulin chain: pigs have Threonine at A #8 while cows have Alanine. At the #10 position on the A insulin chain, pigs have Isoleucine--cows have Valine. Cats, like cows, both have Alanine in the A #8 and Valine in the A #10 positions. But cats have Histidine in the A #18 position--pork or pig insulin has Asparagine--making 3 amino acid differences between porcine insulin and feline[2]. Though this shows CP Pharma's Hypurin pork insulins[3], this information would also apply to Novo's Pork Insulatard, Pork Actrapid, and Pork Mixtard 30[4][5]. They can also be applied to compare these to Lilly's former Iletin II R and Iletin II NPH. The study at the link below found that pork R/Neutral is suitable to be used intravenously in cats[6] These insulins are natural and entirely or partly derived from pork (pig) sources. Only Iletin I R shown on the list below was a mixture of bovine and porcine insulins; it was composed primarily of beef (apx. 85/90%). This means that they are identical to canine natural insulin, and a bit closer to feline than human insulin is. Many humans also prefer porcine-based insulins, which are claimed by some to give a clearer warning of impending low blood sugar than the comparable human GE and analog insulins. Porcine Insulins Short Acting Soluble R/Neutral Hypurin Porcine Neutral Hypurin Pork Regular R/Neutral Pork Actrapid R/Neutral Iletin II R (No longer produced.) Short Acting Cloudy Semilente Novo Semilente MC Intermediate Acting Non-Mixed NPH/isophane Hypurin Porcine Isophane Hypurin Continue reading >>
Insulin Porcine
Injection of protein drugs can cause an IgE-sensitization even in individuals without obvious atopic constitution. Allergen Exposure Subcutaneous injection. Potential Cross-Reactivity Crossreactivity between human insulin and insulin of animal origin has been reported (3, 10-15). A major problem is the cross-reactivity that occurs between anti-insulin antibodies and the various animal and human insulin preparations in patients presenting with allergy to animal insulin (3). Clinical Experience Immunological complications of insulin therapy have been evident since animal insulin became available for the treatment of diabetes mellitus in 1922 (1). In insulin-allergic patients treated with conventional insulin preparations, the insulin-specific IgE values are often 10- to 20-fold higher than in patients without allergy (2). It has been shown that human insulin is less immunogenic than animal insulin. Porcine insulin is most similar to human insulin. Review Insulin is a small protein hormone produced by the beta cells in the Islets of Langerhans. Immunological complications of insulin therapy have been evident since animal insulin became available for the treatment of diabetes mellitus in 1922 (1). In insulin-allergic patients treated with conventional insulin preparations, the insulin-specific IgE values are often 10- to 20-fold higher than in patients without allergy (2). It has been shown that human insulin is less immunogenic than animal insulin. Porcine insulin is most similar to human insulin. The primary amino acid sequences of bovine and porcine insulin differ from that of human insulin by three and one amino acid, respectively. This greater dissimilarity between human and bovine insulin has been postulated to be the explanation for the greater antigenicity of bovine Continue reading >>
Differences Between Human And Porcine Insulin Investigated By Linear Prediction Carbon-13 Nmr
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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 >>
Evidence That Human And Porcine Insulin Differently Affect The Human Insulin Receptor: Studies With Monoclonal Anti-insulin Receptor Antibodies
Abstract Binding studies have been carried out with radioiodinated monoclonal antibodies directed to various epitopes of the insulin receptor in order to detect differences between human and porcine insulin in the interaction with the human insulin receptor. Human insulin was more effective that porcine insulin at inhibiting the binding of 125I-MA-5 to IM-9 cells, Hep-2 human larynx cells and human placenta membranes. On the contrary, human and porcine insulin showed similar inhibitory effect on the binding of two other labeled anti-insulin receptor monoclonal antibodies, thus ruling out the possibility that results were due to experimental artifacts. Although several interpretations are possible, data reported suggest that human insulin and porcine insulin might differently affect the insulin receptor, even if, the biological significance of these findings remains unknown. Preview Unable to display preview. Download preview PDF. Continue reading >>
