Sandbox Reserved 1332
From Proteopedia
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{{Sandbox_Reserved_HLSC322}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_HLSC322}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
| - | ==The Structure of <scene name='77/777652/Original_insulin_image/1'>Human Insulin</scene>== | ||
<Structure load='3I40' size='350' frame='true' align='right' caption='Image of Human Insulin' scene='Insert optional scene name here' /> | <Structure load='3I40' size='350' frame='true' align='right' caption='Image of Human Insulin' scene='Insert optional scene name here' /> | ||
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| - | This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
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== Function == | == Function == | ||
| - | + | Insulin regulates how the body uses and stores glucose and fat. Many of the body's cells rely on insulin to take glucose form the blood for energy. Insulin helps control blood glucose levels and prevent hyperglycemia, a condition with too much glucose in the blood stream. Insulin encourages the storage of glucose as glycogen in the liver, muscle, and fat cells and decreases the amount of glucose in the blood stream returning levels to normal. | |
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| - | == Relevance == | ||
== Structural highlights == | == Structural highlights == | ||
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There are several disulfide bonds that hold the molecule together and this general amino acid sequence and structure doesn't vary much from species to species. This is the reason why pig insulin was once produced for human use. | There are several disulfide bonds that hold the molecule together and this general amino acid sequence and structure doesn't vary much from species to species. This is the reason why pig insulin was once produced for human use. | ||
| - | Insulin molecules often form dimers or hexamers in solution because of hydrogen bonding between molecules | + | Insulin molecules often form dimers or <scene name='77/777652/Insulin_hexamer/2'>hexamers</scene> in solution because of hydrogen bonding between molecules. This has clinical significance as monomers and dimers of insulin are more readily accepted into the bloodstream than hexamers are. Hexamers would take longer to diffuse and could be detrimental to the immediate sugar needs of diabetics. |
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| + | == Genetic and Historical Relevance == | ||
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| + | Prior to the manufacturing of insulin, physicians generally recommended dieting to control starch and sugar intake. Without proper treatment, patients with diabetes notably children would have lower life expectancies with high risk of coma, glucosuria, acidosis, and death. | ||
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| + | Insulin was first discovered in 1922 after many failed attempts at isolating pancreatic extracts to lower blood sugar. This success came by isolating pancreatic islet extracts using dogs and an injection of the islet extracts were first tested on a 14 year old boy in January of 1922 who showed a good prognosis soon after. The scientists involved, Frederick Banting, John Macleod, and Charles Best were awarded the Nobel Prize in 1923. | ||
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| + | Amid many changes over time to the maintenance and production of the protein, it became the first human protein to be manufactured through biotechnology in 1978. Recombinant DNA techniques were used to produce synthetic human insulin. This was more useful than older attempts to produce and use pig insulin since this synthetic insulin was less likely to result in allergic reactions than animal insulin. | ||
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| + | Insulin has come a long way since then, being placed in pumps, pens, and even islet cell transplantations to help diabetes patients manage the disease. A very exciting new development in 2015, was the iLet: a bionic pancreas that provides insulin and glucagon as required. | ||
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| + | == Disease == | ||
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| - | </StructureSection> | ||
== References == | == References == | ||
| - | + | http://www.vivo.colostate.edu/hbooks/pathphys/endocrine/pancreas/insulin_struct.html | |
Revision as of 21:03, 20 February 2018
| This Sandbox is Reserved from January through July 31, 2018 for use in the course HLSC322: Principles of Genetics and Genomics taught by Genevieve Houston-Ludlam at the University of Maryland, College Park, USA. This reservation includes Sandbox Reserved 1311 through Sandbox Reserved 1430. |
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More help: Help:Editing |
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You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Contents |
Function
Insulin regulates how the body uses and stores glucose and fat. Many of the body's cells rely on insulin to take glucose form the blood for energy. Insulin helps control blood glucose levels and prevent hyperglycemia, a condition with too much glucose in the blood stream. Insulin encourages the storage of glucose as glycogen in the liver, muscle, and fat cells and decreases the amount of glucose in the blood stream returning levels to normal.
Structural highlights
Insulin is made up of two peptide chains: the and the
There are several disulfide bonds that hold the molecule together and this general amino acid sequence and structure doesn't vary much from species to species. This is the reason why pig insulin was once produced for human use.
Insulin molecules often form dimers or in solution because of hydrogen bonding between molecules. This has clinical significance as monomers and dimers of insulin are more readily accepted into the bloodstream than hexamers are. Hexamers would take longer to diffuse and could be detrimental to the immediate sugar needs of diabetics.
Genetic and Historical Relevance
Prior to the manufacturing of insulin, physicians generally recommended dieting to control starch and sugar intake. Without proper treatment, patients with diabetes notably children would have lower life expectancies with high risk of coma, glucosuria, acidosis, and death.
Insulin was first discovered in 1922 after many failed attempts at isolating pancreatic extracts to lower blood sugar. This success came by isolating pancreatic islet extracts using dogs and an injection of the islet extracts were first tested on a 14 year old boy in January of 1922 who showed a good prognosis soon after. The scientists involved, Frederick Banting, John Macleod, and Charles Best were awarded the Nobel Prize in 1923.
Amid many changes over time to the maintenance and production of the protein, it became the first human protein to be manufactured through biotechnology in 1978. Recombinant DNA techniques were used to produce synthetic human insulin. This was more useful than older attempts to produce and use pig insulin since this synthetic insulin was less likely to result in allergic reactions than animal insulin.
Insulin has come a long way since then, being placed in pumps, pens, and even islet cell transplantations to help diabetes patients manage the disease. A very exciting new development in 2015, was the iLet: a bionic pancreas that provides insulin and glucagon as required.
Disease
References
http://www.vivo.colostate.edu/hbooks/pathphys/endocrine/pancreas/insulin_struct.html
