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Statements

Subject Item
n2:DB01309
rdf:type
n5:Drug
n5:description
Insulin glulisine is a biosynthetic, rapid-acting human insulin analogue produced in a non-pathogenic laboratory strain of _Escherichia coli_ (K12). This recombinant hormone differs from native human insulin in that the amino acid arginine at position B3 is replaced by lysine and the lysine at position B29 is replaced by glutamic acid. These structural modifications decrease hexamer formation, stabilize insulin glulisine monomers and increase the rate of absorption and onset of action compared to human insulin.
n5:dosage
n7:271B64A8-363D-11E5-9242-09173F13E4C5
n5:generalReferences
# Arnolds S, Rave K, Hovelmann U, Fischer A, Sert-Langeron C, Heise T: Insulin Glulisine Has a Faster Onset of Action Compared with Insulin Aspart in Healthy Volunteers. Exp Clin Endocrinol Diabetes. 2010 Apr 28. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/20429049 # Becker RH: Insulin glulisine complementing basal insulins: a review of structure and activity. Diabetes Technol Ther. 2007 Feb;9(1):109-21. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17316105 # Becker RH, Frick AD: Clinical pharmacokinetics and pharmacodynamics of insulin glulisine. Clin Pharmacokinet. 2008;47(1):7-20. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/18076215 # Cox SL: Insulin glulisine. Drugs Today (Barc). 2005 Jul;41(7):433-40. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/16193096 # Garnock-Jones KP, Plosker GL: Insulin glulisine: a review of its use in the management of diabetes mellitus. Drugs. 2009 May 29;69(8):1035-57. doi: 10.2165/00003495-200969080-00006. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/19496630 # Horvath K, Bock G, Regittnig W, Bodenlenz M, Wutte A, Plank J, Magnes C, Sinner F, Furst-Recktenwald S, Theobald K, Pieber TR: Insulin glulisine, insulin lispro and regular human insulin show comparable end-organ metabolic effects: an exploratory study. Diabetes Obes Metab. 2008 Jun;10(6):484-91. Epub 2007 Aug 30. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17764465 # Insuline glusine (Apidra): a new rapid-acting insulin. Med Lett Drugs Ther. 2006 Apr 24;48(1233):33-4. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/16625142 # Robinson DM, Wellington K: Insulin glulisine. Drugs. 2006;66(6):861-9. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/16706558 # Ulrich H, Snyder B, Garg SK: Combining insulins for optimal blood glucose control in type I and 2 diabetes: focus on insulin glulisine. Vasc Health Risk Manag. 2007;3(3):245-54. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17703632
n5:group
approved
n5:halfLife
Elimination half life= 42 minutes (following subcutaneous injection)
n5:indication
For the treatment of Type 1 and 2 diabetes mellitus. Should be used in regimens including a long-acting or basal insulin analogue unless it is used in a continuous infusion pump. May be used with oral antidiabetic agents.
owl:sameAs
n14:DB01309 n21:DB01309
dcterms:title
Insulin Glulisine
adms:identifier
n4:DB01309 n6:D04540 n19:Insulin_glulisine n23:0088-2502-05 n25:PA164760859
n5:mechanismOfAction
Insulin glulisine binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor autophosphorylates and phosphorylates numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. Activation of these proteins leads to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC), both of which play critical roles in metabolism and catabolism. In humans, insulin is stored in the form of hexamers; however, only insulin monomers are able to interact with IR. Substitution of the arginine at position B3 for lysine and replacement of the B29 lysine with glutamic acid decreases the propensity to form hexamers, stabilizes the hormone in monomeric form and results in a rapid rate of absorption and short duration of action.
n5:packager
n8:271B64A3-363D-11E5-9242-09173F13E4C5
n5:patent
n17:6221633 n17:6960561
n5:toxicity
Inappropriately high dosages relative to food intake and/or energy expenditure may result in severe and sometimes prolonged and life-threatening hypoglycemia. Neurogenic (autonomic) signs and symptoms of hypoglycemia include trembling, palpitations, sweating, anxiety, hunger, nausea and tingling. Neuroglycopenic signs and symptoms of hypoglycemia include difficulty concentrating, lethargy/weakness, confusion, drowsiness, vision changes, difficulty speaking, headache, and dizziness. Mild hypoglycemia is characterized by the presence of autonomic symptoms. Moderate hypoglycemia is characterized by the presence of autonomic and neuroglycopenic symptoms. Individuals may become unconscious in severe cases of hypoglycemia.
n5:volumeOfDistribution
13 L
n9:hasAHFSCode
n10:68-20-08
foaf:page
n12:apidra-drug.htm n22:insulin-glulisine.html n24:rx-mono.aspx?contentFileName=api1806.html&contentName=Apidra&contentId=70
n5:Molecular-Formula
n15:271B64AA-363D-11E5-9242-09173F13E4C5
n5:Molecular-Weight
n15:271B64A9-363D-11E5-9242-09173F13E4C5
n9:hasATCCode
n20:A10AB06
n5:absorption
Compared to regular human insulin, insulin glulisine is faster absorbed. When 0.15 units/kg was subcutaneously administered to type 1 diabetes patients, the pharmacokinetic parameters are as follows: Tmax = 60 minutes (range of 40 - 120 minutes); Cmax = 83 microUnits/mL (range of 40 - 131 microUnits/mL). Absolute bioavailability following subcutaneous administration is approximately 70%, regardless of site of injection.
n5:affectedOrganism
Humans and other mammals
n5:casRegistryNumber
207748-29-6
n5:category
n5:containedIn
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