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Showing drug card for Repaglinide (DB00912)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:06:44
Primary Accession Number DB00912
Secondary Accession Number
  • APRD00439
Name Repaglinide
Drug Type
  • Approved
  • Investigational
  • Small Molecule
Description Repaglinide is a blood-glucose lowering drug. It lowers blood glucose by stimulating the release of insulin from the pancreas. It achieves this by closing ATP-dependent potassium channels in the membrane of the beta cells. This depolarizes the beta cells, opening the cells' calcium channels, and the resulting calcium influx induces insulin secretion.
Synonyms
  1. AG-EE 388 ZW
  2. AG-EE 623 ZW
  3. Repaglinida [INN-Spanish]
  4. Repaglinidum [INN-Latin]
  5. repaglinide
Brand Names
  1. Prandin
Brand Mixtures Not Available
Chemical IUPAC Name 2-ethoxy-4-[2-[[(1S)-3-methyl-1-(2-piperidin-1-ylphenyl)butyl]amino]-2-oxoethyl]benzoic acid
Chemical Formula C27H36N2O4
Chemical Structure Structure
CAS Registry Number 135062-02-1
InChI Identifier InChI=1/C27H36N2O4/c1-4-33-25-17-20(12-13-22(25)27(31)32)18-26(30)28-23(16-19(2)3)21-10-6-7-11-24(21)29-14-8-5-9-15-29/h6-7,10-13,17,19,23H,4-5,8-9,14-16,18H2,1-3H3,(H,28,30)(H,31,32)/t23-/m0/s1/f/h28,31H
InChI Key FAEKWTJYAYMJKF-DUDVQEBDDW
KEGG Drug D00594 Link Image
KEGG Compound C07670 Link Image
PubChem Compound 65981 Link Image
PubChem Substance 208038 Link Image
ChEBI ID Not Available
PharmGKB ID PA451234 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02239925 Link Image
RxList Link http://www.rxlist.com/cgi/generic/prandin.htm Link Image
PDRhealth Link http://www.pdrhealth.com/drug_info/rxdrugprofiles/drugs/pra1343.shtml Link Image
Wikipedia Link http://en.wikipedia.org/wiki/Repaglinide Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference W. Grell et al., PCT Int. pat. Appl. WO 93 00,337
Average Molecular Weight 452.5857
Monoisotopic Molecular Weight 452.2675
State Solid
Melting Point 130-131 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 2.94e-03 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 5.9 Source: PhysProp
Predicted LogP 5.05 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -5.19 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Isomeric SMILES CCOC1=C(C=CC(CC(=O)N[C@@H](CC(C)C)C2=CC=CC=C2N2CCCCC2)=C1)C(O)=O
Canonical SMILES CCOC1=C(C=CC(CC(=O)NC(CC(C)C)C2=CC=CC=C2N2CCCCC2)=C1)C(O)=O
Drug Category
  • Hypoglycemic Agents
  • Meglitinides
ATC Codes
AHFS Codes
  • 68:20.16
Indication For the treatment of Type II diabetes mellitus.
Pharmacology Repaglinide is an oral blood glucose-lowering drug of the meglitinide class used in the management of type 2 diabetes mellitus (also known as non-insulin dependent diabetes mellitus or NIDDM). Repaglinide lowers blood glucose levels by stimulating the release of insulin from the pancreas. This action is dependent upon functioning beta cells in the pancreatic islets. Insulin release is glucose-dependent and diminishes at low glucose concentrations.
Mechanism of Action Repaglinide closes ATP-dependent potassium channels in the b-cell membrane by binding at characterizable sites. This potassium channel blockade depolarizes the b-cell, which leads to an opening of calcium channels. The resulting increased calcium influx induces insulin secretion. The ion channel mechanism is highly tissue selective with low affinity for heart and skeletal muscle.
Absorption Rapid (bioavailability is 56%)
Toxicity LD50 >1 g/kg (rat) (W. Grell)
Protein Binding >98%
Biotransformation Repaglinide is completely metabolized by oxidative biotransformation and direct conjugation with glucuronic acid after either an IV or oral dose.
Half Life 1 hour
Dosage Forms
Form Route
Tablet Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Acebutolol The beta-blocker decreases the symptoms of hypoglycemia
Acetohexamide Similar mode of action - questionable association
Atenolol The beta-blocker decreases the symptoms of hypoglycemia
Betaxolol The beta-blocker decreases the symptoms of hypoglycemia
Bevantolol The beta-blocker decreases the symptoms of hypoglycemia
Bisoprolol The beta-blocker decreases the symptoms of hypoglycemia
Carteolol The beta-blocker decreases the symptoms of hypoglycemia
Carvedilol The beta-blocker decreases the symptoms of hypoglycemia
Chlorpropamide Similar mode of action - questionable association
Clarithromycin Clarithromycin increases the effect of repaglinide
Cyclosporine Cyclosporine increases the effect of repaglinide
Erythromycin The macrolide increases the effect of repaglinide
Esmolol The beta-blocker decreases the symptoms of hypoglycemia
Gemfibrozil Gemfibrozil increases the effect and toxicity of repaglinide
Glibenclamide Similar mode of action - questionable association
Gliclazide Similar mode of action - questionable association
Glimepiride Similar mode of action - questionable association
Glipizide Similar mode of action - questionable association
Glisoxepide Similar mode of action - questionable association
Glucosamine Possible hyperglycemia
Glycodiazine Similar mode of action - questionable association
Josamycin The macrolide increases the effect of repaglinide
Labetalol The beta-blocker decreases the symptoms of hypoglycemia
Metoprolol The beta-blocker decreases the symptoms of hypoglycemia
Nadolol The beta-blocker decreases the symptoms of hypoglycemia
Oxprenolol The beta-blocker decreases the symptoms of hypoglycemia
Penbutolol The beta-blocker decreases the symptoms of hypoglycemia
Pindolol The beta-blocker decreases the symptoms of hypoglycemia
Practolol The beta-blocker decreases the symptoms of hypoglycemia
Propranolol The beta-blocker decreases the symptoms of hypoglycemia
Rifampin Rifampin decreases the effect of repaglinide
Sotalol The beta-blocker decreases the symptoms of hypoglycemia
Timolol The beta-blocker decreases the symptoms of hypoglycemia
Tolazamide Similar mode of action - questionable association
Tolbutamide Similar mode of action - questionable association
Food Interactions
  • Take upto 30 minutes before meals.
Pathways Not Available
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. RxList Link Image
  4. PDRhealth Link Image
Organisms Affected
  • Humans and other mammals
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 2C8 (CYP2C8)
Targets
  1. ATP-binding cassette transporter sub-family C member 8
  2. ATP-sensitive inward rectifier potassium channel 1
  3. ATP-sensitive inward rectifier potassium channel 11
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 2C8 (CYP2C8)
Enzyme 1 Gene Name CYP2C8
Enzyme 1 SwissProt ID P10632 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P10632|CP2C8_HUMAN Cytochrome P450 2C8 (EC 1.14.14.1) 
MEPFVVLVLCLSFMLLFSLWRQSCRRRKLPPGPTPLPIIGNMLQIDVKDICKSFTNFSKV
YGPVFTVYFGMNPIVVFHGYEAVKEALIDNGEEFSGRGNSPISQRITKGLGIISSNGKRW
KEIRRFSLTTLRNFGMGKRSIEDRVQEEAHCLVEELRKTKASPCDPTFILGCAPCNVICS
VVFQKRFDYKDQNFLTLMKRFNENFRILNSPWIQVCNNFPLLIDCFPGTHNKVLKNVALT
RSYIREKVKEHQASLDVNNPRDFIDCFLIKMEQEKDNQKSEFNIENLVGTVADLFVAGTE
TTSTTLRYGLLLLLKHPEVTAKVQEEIDHVIGRHRSPCMQDRSHMPYTDAVVHEIQRYSD
LVPTGVPHAVTTDTKFRNYLIPKGTTIMALLTSVLHDDKEFPNPNIFDPGHFLDKNGNFK
KSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNLKSVDDLKNLNTTAVTKGIVSLP
PSYQICFIPV
Drug Target 1 [top]
Target 1 ID 230
Target 1 Name ATP-binding cassette transporter sub-family C member 8
Target 1 Synonyms
  1. Sulfonylurea receptor 1
Target 1 Gene Name ABCC8
Target 1 Protein Sequence >ATP-binding cassette transporter sub-family C member 8 
PLAFCGSENHSAAYRVDQGVLNNGCFVDALNVVPHVFLLFITFPILFIGWGSQSSKVHIH
HSTWLHFPGHNLRWILTFMLLFVLVCEIAEGILSDGVTESHHLHLYMPAGMAFMAAVTSV
VYYHNIETSNFPKLLIALLVYWTLAFITKTIKFVKFLDHAIAFSQLRFCLTGLLVILYGM
LLLVEVNVIRVRRYIFFKTPREVKPPEDLQDLGVRFLQPFVNLLSKGTYWWMNAFIKTAH
KKPIDLRAIGKLPIAMRALTNYQRLCEAFDAQVRKDIQGTQGARAIWQALSHAFGRRLVL
SSTFRILADLLGFAGPLCIFGIVDHLGKENDVFQPKTQFLGVYFVSSQEFLANAYVLAVL
LFLALLLQRTFLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSNLSMGEMTAGQICNLV
AIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKL
SQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAIYTS
ISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTV
KALVSVQKLSEFLSSAEIREEQCAPHEPTPQGPASKYQAVPLRVVNRKRPAREDCRGLTG
PLQSLVPSADGDADNCCVQIMGGYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSS
LLLAALGEMQKVSGAVFWSSLPDSEIGEDPSPERETATDLDIRKRGPVAYASQKPWLLNA
TVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVAR
ALYQHANVVFLDDPFSALDIHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIA
MKDGTIQREGTLKDFQRSECQLFEHWKTLMNRQDQELEKETVTERKATEPPQGLSRAMSS
RDGLLQDEEEEEEEAAESEEDDNLSSMLHQRAEIPWRACAKYLSSAGILLLSLLVFSQLL
KHMVLVAIDYWLAKWTDSALTLTPAARNCSLSQECTLDQTVYAMVFTVLCSLGIVLCLVT
SVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLEC
LSRSTLLCVSALAVISYVTPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLS
HFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLI
AAVTSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIHGLLKTE
AESYEGLLAPSLIPKNWPDQGKIQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTG
SGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDP
ERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSI
FIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDK
PEKLLSRKDSVFASFVRADK
Target 1 Number of Residues 1606
Target 1 Molecular Weight 176893
Target 1 Theoretical pI 7.86
Target 1 GO Classification
Function
signal transducer activity
receptor activity
transmembrane receptor activity
sulfonylurea receptor activity
ATPase activity
hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
ATPase activity, coupled to transmembrane movement of substances
purine nucleotide binding
adenyl nucleotide binding
ATP binding
catalytic activity
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
pyrophosphatase activity
nucleoside-triphosphatase activity
binding
nucleotide binding
Process
ion transport
cation transport
monovalent inorganic cation transport
potassium ion transport
physiological process
cellular physiological process
transport
Component
cell
membrane
intrinsic to membrane
integral to membrane
Target 1 General Function Insulin and ion channel regulation
Target 1 Specific Function Putative subunit of the beta-cell ATP-sensitive potassium channel (KATP). Regulator of ATP-sensitive K+ channels and insulin release
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • 34-54
  • 75-95
  • 101-121
  • 134-153
  • 167-193
  • 311-330
  • 355-375
  • 434-454
  • 458-478
  • 541-561
  • 584-604
  • 1004-1024
  • 1072-1092
  • 1137-1157
  • 1159-1179
  • 1251-1271
  • 1276-1296
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 1374919 Link Image
Target 1 UniProtKB/Swiss-Prot ID Q09428 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name ABCC8_HUMAN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 1 Gene Sequence >4746 bp 
ATGCCCCTGGCCTTCTGCGGCAGCGAGAACCACTCGGCCGCCTACCGGGTGGACCAGGGG
GTCCTCAACAACGGCTGCTTTGTGGACGTCCTCAACGTGGTGCCGCACGTCTTCCTACTC
TTCATCACCTTCCCCATCCTCTTCATTGGATGGGGAAGTCAGAGCTCCAAGGTGCACATC
CACCACAGCACATGGCTTCATTTCCCTGGGCACAACCTGCGGTGGATCCTGACCTTCATG
CTGCTCTTCGTCCTGGTGTGTGAGATTGCAGAGGGCATCCTGTCTGATGGGGTGACCGAA
TCCCACCATCTGCACCTGTACATGCCAGCCGGGATGGCGTTCATGGCTGCTGTCACCTCC
GTGGTCTACTATCACAACATCGAGACTTCCAACTTCCCCAAGCTGCTAATTGCCCTGCTG
GTGTATTGGACCCTGGCCTTCATCACCAAGACCATCAAGTTTGTCAAGTTCTTGGACCAC
GCCATCGCGTTCTCGCAGGTACGCTTCTGCCTCACAGGGCTGCTGGTGATCCTCTATGGG
ATGCTGCTCCTCGTGGAGGTCAATGTCATCAGGGTGAGGAGATACATCTTCTTCAAGACA
CCGAGGGAGGTGAAGCCTCCCGAGGACCTGCAAGACCTGGGGGTACGCTTCCTGCAGCCC
TTCGTGAATCTGCTGTCCAAAGGCACCTACTGGTGGATGAACGCCTTCATCAAGACTGCC
CACAAGAAGCCCATCGACTTGCGAGCCATCGGGAAGCTGCCCATCGCCATGAGGGCCCTC
ACCAACTACCAACGGCTCTGCGAGGCCTTTGACGCCCAGGTGCGGAAGGACATTCAGGGC
ACTCAAGGTGCCCGGGCCATCTGGCAGGCACTCAGCCATGCCTTCGGGAGGCGCCTGGTC
CTCAGCAGCACTTTCCGCATCTTGGCCGACCTGCTGGGCTTCGCCGGGCCACTGTGCATC
TTTGGGATCGTGGACCACCTTGGGAAGGAGAACGACGTCTTCCAGCCCAAGACACAATTT
CTCGGGGTTTACTTTGTCTCATCCCAAGAGTTCCTTGCCAATGCCTACGTCTTAGCTGTG
CTTCTGTTCCTTGCCCTCCTACTGCAAAGGACATTTCTGCAAGCATCCTACTATGTGGCC
ATTGAAACTGGAATTAACTTGAGAGGAGCAATACAGACCAAGATTTACAATAAAATTATG
CACCTGTCCACCTCCAACCTGTCCATGGGAGAAATGACTGCTGGACAGATCTGTAATCTG
GTTGCCATCGACACCAATCAGCTCATGTGGTTTTTCTTCTTGTGCCCAAACCTCTGGGCT
ATGCCAGTACAGATCATTGTGGGTGTGATTCTCCTCTACTACATACTCGGAGTCAGTGCC
TTAATTGGAGCAGCTGTCATCATTCTACTGGCTCCTGTCCAGTACTTCGTGGCCACCAAG
CTGTCTCAGGCCCAGCGGACGACACTGGAGTATTCCAATGAGCGGCTGAAGCAGACCAAC
GAGATGCTCCGCGGCATCAAGCTGCTGAAGCTGTACGCCTGGGAGAACATCTTCCGCACG
CGGGTGGAGACGACCCGCAGGAAGGAGATGACCAGCCTCAGGGCCTTTGCCATCTATACC
TCCATCTCCATTTTCATGAACACGGCCATCCCCATTGCAGCTGTCCTCATAACTTTCGTG
GGCCATGTCAGCTTCTTCAAAGAGGCCGACTTCTCGCCCTCCGTGGCCTTTGCCTCCCTC
TCCCTCTTCCATATCTTGGTCACACCGCTGTTCCTGCTGTCCAGTGTGGTCCGATCTACC
GTCAAAGCTCTAGTGAGCGTGCAAAAGCTAAGCGAGTTCCTGTCCAGTGCAGAGATCCGT
GAGGAGCAGTGTGCCCCCCATGAGCCCACACCTCAGGGCCCAGCCAGCAAGTACCAGGCG
GTGCCCCTCAGGGTTGTGAACCGCAAGCGTCCAGCCCGGGAGGATTGTCGGGGCCTCACC
GGCCCACTGCAGAGCCTGGTCCCCAGTGCAGATGGCGATGCTGACAACTGCTGTGTCCAG
ATCATGGGAGGCTACTTCACGTGGACCCCAGATGGAATCCCCACACTGTCCAACATCACC
ATTCGTATCCCCCGAGGCCAGCTGACTATGATCGTGGGGCAGGTGGGCTGCGGCAAGTCC
TCGCTCCTTCTAGCCGCACTGGGGGAGATGCAGAAGGTCTCAGGGGCTGTCTTCTGGAGC
AGCCTTCCTGACAGCGAGATAGGAGAGGACCCCAGCCCAGAGCGGGAGACAGCGACCGAC
TTGGATATCAGGAAGAGAGGCCCCGTGGCCTATGCTTCGCAGAAACCATGGCTGCTAAAT
GCCACTGTGGAGGAGAACATCATCTTTGAGAGTCCCTTCAACAAACAACGGTACAAGATG
GTCATTGAAGCCTGCTCTCTGCAGCCAGACATCGACATCCTGCCCCATGGAGACCAGACC
CAGATTGGGGAACGGGGCATCAACCTGTCTGGTGGTCAACGCCAGCGAATCAGTGTGGCC
CGAGCCCTCTACCAGCACGCCAACGTTGTCTTCTTGGATGACCCCTTCTCAGCTCTGGAT
ATCCATCTGAGTGACCACTTAATGCAGGCCGGCATCCTTGAGCTGCTCCGGGACGACAAG
AGGACAGTGGTCTTAGTGACCCACAAGCTACAGTACCTGCCCCATGCAGACTGGATCATT
GCCATGAAGGATGGCACCATCCAGAGGGAGGGTACCCTCAAGGACTTCCAGAGGTCTGAA
TGCCAGCTCTTTGAGCACTGGAAGACCCTCATGAACCGACAGGACCAAGAGCTGGAGAAG
GAGACTGTCACAGAGAGAAAAGCCACAGAGCCACCCCAGGGCCTATCTCGTGCCATGTCC
TCGAGGGATGGCCTTCTGCAGGATGAGGAAGAGGAGGAAGAGGAGGCAGCTGAGAGCGAG
GAGGATGACAACCTGTCGTCCATGCTGCACCAGCGTGCTGAGATCCCATGGCGAGCCTGC
GCCAAGTACCTGTCCTCCGCCGGCATCCTGCTCCTGTCGTTGCTGGTCTTCTCACAGCTG
CTCAAGCACATGGTCCTGGTGGCCATCGACTACTGGCTGGCCAAGTGGACCGACAGCGCC
CTGACCCTGACCCCTGCAGCCAGGAACTGCTCCCTCAGCCAGGAGTGCACCCTCGACCAG
ACTGTCTATGCCATGGTGTTCACGGCTGTCTGCAGCCTGGGCATTGTGCTGTGCCTCGTC
ACGTCTGTCACTGTGGAGTGGACAGGGCTGAAGGTGGCCAAGAGACTGCACCGCAGCCTG
CTAAACCGGATCATCCTAGCCCCCATGAGGTTTTTTGAGACCACGCCCCTTGGGAGCATC
CTGAACAGATTTTCATCTGACTGTAACACCATCGACCAGCACATCCCATCCACGCTGGAG
TGCCTGAGCCGCTCCACCCTGCTCTGTGTCTCAGCCCTGGCCGTCATCTCCTATGTCACA
CCTGTGTTCCTCGTGGCCCTCTTGCCCCTGGCCATCGTGTGCTACTTCATCCAGAAGTAC
TTCCGGGTGGCGTCCAGGGACCTGCAGCAGCTGGATGACACCACCCAGCTTCCACTTCTC
TCACACTTTGCCGAAACCGTAGAAGGACTCACCACCATCCGGGCCTTCAGGTATGAGGCC
CGGTTCCAGCAGAAGCTTCTCGAATACACAGACTCCAACAACATTGCTTCCCTCTTCCTC
ACAGCTGCCAACAGATGGCTGGAAGTCCGAATGGAGTACATCGGTGCATGTGTGGTGCTC
ATCGCAGCGGTGACCTCCATCTCCAACTCCCTGCACAGGGAGCTCTCTGCTGGCCTGGTG
GGCCTGGGCCTTACCTACGCCCTAATGGTCTCCAACTACCTCAACTGGATGGTGAGGAAC
CTGGCAGACATGGAGCTCCAGCTGGGGGCTGTGAAGCGCATCCATGGGCTCCTGAAAACC
GAGGCAGAGAGCTACGAGGGACTCCTGGCACCATCGCTGATCCCAAAGAACTGGCCAGAC
CAAGGGAAGATCCAGATCCAGAACCTGAGCGTGCGCTACGACAGCTCCCTGAAGCCGGTG
CTGAAGCACGTCAATGCCCTCATCTCCCCTGGACAGAAGATCGGGATCTGCGGCCGCACC
GGCAGTGGGAAGTCCTCCTTCTCTCTTGCCTTCTTCCGCATGGTGGACACGTTCGAAGGG
CACATCATCATTGATGGCATTGACATCGCCAAACTGCCGCTGCACACCCTGCGCTCACGC
CTCTCCATCATCCTGCAGGACCCCGTCCTCTTCAGCGGCACCATCCGATTTAACCTGGAC
CCTGAGAGGAAGTGCTCAGATAGCACACTGTGGGAGGCCCTGGAAATCGCCCAGCTGAAG
CTGGTGGTGAAGGCACTGCCAGGAGGCCTCGATGCCATCATCACAGAAGGCGGGGAGAAT
TTCAGCCAGGGACAGAGGCAGCTGTTCTGCCTGGCCCGGGCCTTCGTGAGGAAGACCAGC
ATCTTCATCATGGACGAGGCCACGGCTTCCATTGACATGGCCACGGAAAACATCCTCCAA
AAGGTGGTGATGACAGCCTTCGCAGACCGCACTGTGGTCACCATCGCGCATCGAGTGCAC
ACCATCCTGAGTGCAGACCTGGTGATCGTCCTGAAGCGGGGTGCCATCCTTGAGTTCGAT
AAGCCAGAGAAGCTGCTCAGCCGGAAGGACAGCGTCTTCGCCTCCTTCGTCCGTGCAGAC
AAGTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID ABCC8 Link Image
Target 1 GenAtlas ID ABCC8 Link Image
Target 1 HGNC ID HGNC:59 Link Image
Target 1 Chromosome Location 11
Target 1 Locus 11p15.1
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Aguilar-Bryan L, Bryan J: Molecular biology of adenosine triphosphate-sensitive potassium channels. Endocr Rev. 1999 Apr;20(2):101-35. [PubMed Link Image]
  2. Otonkoski T, Ammala C, Huopio H, Cote GJ, Chapman J, Cosgrove K, Ashfield R, Huang E, Komulainen J, Ashcroft FM, Dunne MJ, Kere J, Thomas PM: A point mutation inactivating the sulfonylurea receptor causes the severe form of persistent hyperinsulinemic hypoglycemia of infancy in Finland. Diabetes. 1999 Feb;48(2):408-15. [PubMed Link Image]
  3. Meissner T, Beinbrech B, Mayatepek E: Congenital hyperinsulinism: molecular basis of a heterogeneous disease. Hum Mutat. 1999;13(5):351-61. [PubMed Link Image]
  4. Glaser B, Furth J, Stanley CA, Baker L, Thornton PS, Landau H, Permutt MA: Intragenic single nucleotide polymorphism haplotype analysis of SUR1 mutations in familial hyperinsulinism. Hum Mutat. 1999;14(1):23-9. [PubMed Link Image]
  5. Raab-Graham KF, Cirilo LJ, Boettcher AA, Radeke CM, Vandenberg CA: Membrane topology of the amino-terminal region of the sulfonylurea receptor. J Biol Chem. 1999 Oct 8;274(41):29122-9. [PubMed Link Image]
  6. Tanizawa Y, Matsuda K, Matsuo M, Ohta Y, Ochi N, Adachi M, Koga M, Mizuno S, Kajita M, Tanaka Y, Tachibana K, Inoue H, Furukawa S, Amachi T, Ueda K, Oka Y: Genetic analysis of Japanese patients with persistent hyperinsulinemic hypoglycemia of infancy: nucleotide-binding fold-2 mutation impairs cooperative binding of adenine nucleotides to sulfonylurea receptor 1. Diabetes. 2000 Jan;49(1):114-20. [PubMed Link Image]
  7. Huopio H, Reimann F, Ashfield R, Komulainen J, Lenko HL, Rahier J, Vauhkonen I, Kere J, Laakso M, Ashcroft F, Otonkoski T: Dominantly inherited hyperinsulinism caused by a mutation in the sulfonylurea receptor type 1. J Clin Invest. 2000 Oct;106(7):897-906. [PubMed Link Image]
  8. Cartier EA, Conti LR, Vandenberg CA, Shyng SL: Defective trafficking and function of KATP channels caused by a sulfonylurea receptor 1 mutation associated with persistent hyperinsulinemic hypoglycemia of infancy. Proc Natl Acad Sci U S A. 2001 Feb 27;98(5):2882-7. [PubMed Link Image]
  9. Taschenberger G, Mougey A, Shen S, Lester LB, LaFranchi S, Shyng SL: Identification of a familial hyperinsulinism-causing mutation in the sulfonylurea receptor 1 that prevents normal trafficking and function of KATP channels. J Biol Chem. 2002 May 10;277(19):17139-46. Epub 2002 Feb 26. [PubMed Link Image]
  10. Thomas PM, Cote GJ, Wohllk N, Haddad B, Mathew PM, Rabl W, Aguilar-Bryan L, Gagel RF, Bryan J: Mutations in the sulfonylurea receptor gene in familial persistent hyperinsulinemic hypoglycemia of infancy. Science. 1995 Apr 21;268(5209):426-9. [PubMed Link Image]
  11. 8635661 Inoue H, Ferrer J, Welling CM, Elbein SC, Hoffman M, Mayorga R, Warren-Perry M, Zhang Y, Millns H, Turner R, Province M, Bryan J, Permutt MA, Aguilar-Bryan L: Sequence variants in the sulfonylurea receptor (SUR) gene are associated with NIDDM in Caucasians. Diabetes. 1996 Jun;45(6):825-31.
  12. 8650576 Nichols CG, Shyng SL, Nestorowicz A, Glaser B, Clement JP 4th, Gonzalez G, Aguilar-Bryan L, Permutt MA, Bryan J: Adenosine diphosphate as an intracellular regulator of insulin secretion. Science. 1996 Jun 21;272(5269):1785-7.
  13. 8751851 Thomas PM, Wohllk N, Huang E, Kuhnle U, Rabl W, Gagel RF, Cote GJ: Inactivation of the first nucleotide-binding fold of the sulfonylurea receptor, and familial persistent hyperinsulinemic hypoglycemia of infancy. Am J Hum Genet. 1996 Sep;59(3):510-8.
  14. 8923011 Nestorowicz A, Wilson BA, Schoor KP, Inoue H, Glaser B, Landau H, Stanley CA, Thornton PS, Clement JP 4th, Bryan J, Aguilar-Bryan L, Permutt MA: Mutations in the sulonylurea receptor gene are associated with familial hyperinsulinism in Ashkenazi Jews. Hum Mol Genet. 1996 Nov;5(11):1813-22.
  15. 9519757 Ohta Y, Tanizawa Y, Inoue H, Hosaka T, Ueda K, Matsutani A, Repunte VP, Yamada M, Kurachi Y, Bryan J, Aguilar-Bryan L, Permutt MA, Oka Y: Identification and functional analysis of sulfonylurea receptor 1 variants in Japanese patients with NIDDM. Diabetes. 1998 Mar;47(3):476-81.
  16. 9568693 Hansen T, Echwald SM, Hansen L, Moller AM, Almind K, Clausen JO, Urhammer SA, Inoue H, Ferrer J, Bryan J, Aguilar-Bryan L, Permutt MA, Pedersen O: Decreased tolbutamide-stimulated insulin secretion in healthy subjects with sequence variants in the high-affinity sulfonylurea receptor gene. Diabetes. 1998 Apr;47(4):598-605.
  17. 9618169 Nestorowicz A, Glaser B, Wilson BA, Shyng SL, Nichols CG, Stanley CA, Thornton PS, Permutt MA: Genetic heterogeneity in familial hyperinsulinism. Hum Mol Genet. 1998 Jul;7(7):1119-28.
  18. 9648840 Shyng SL, Ferrigni T, Shepard JB, Nestorowicz A, Glaser B, Permutt MA, Nichols CG: Functional analyses of novel mutations in the sulfonylurea receptor 1 associated with persistent hyperinsulinemic hypoglycemia of infancy. Diabetes. 1998 Jul;47(7):1145-51.
  19. 9769320 Verkarre V, Fournet JC, de Lonlay P, Gross-Morand MS, Devillers M, Rahier J, Brunelle F, Robert JJ, Nihoul-Fekete C, Saudubray JM, Junien C: Paternal mutation of the sulfonylurea receptor (SUR1) gene and maternal loss of 11p15 imprinted genes lead to persistent hyperinsulinism in focal adenomatous hyperplasia. J Clin Invest. 1998 Oct 1;102(7):1286-91.
Target 1 Drug References
  1. Hu S, Wang S, Fanelli B, Bell PA, Dunning BE, Geisse S, Schmitz R, Boettcher BR: Pancreatic beta-cell K(ATP) channel activity and membrane-binding studies with nateglinide: A comparison with sulfonylureas and repaglinide. J Pharmacol Exp Ther. 2000 May;293(2):444-52. [PubMed Link Image]
  2. Sunaga Y, Gonoi T, Shibasaki T, Ichikawa K, Kusama H, Yano H, Seino S: The effects of mitiglinide (KAD-1229), a new anti-diabetic drug, on ATP-sensitive K+ channels and insulin secretion: comparison with the sulfonylureas and nateglinide. Eur J Pharmacol. 2001 Nov 9;431(1):119-25. [PubMed Link Image]
  3. Hansen AM, Christensen IT, Hansen JB, Carr RD, Ashcroft FM, Wahl P: Differential interactions of nateglinide and repaglinide on the human beta-cell sulphonylurea receptor 1. Diabetes. 2002 Sep;51(9):2789-95. [PubMed Link Image]
  4. Wangler B, Schneider S, Thews O, Schirrmacher E, Comagic S, Feilen P, Schwanstecher C, Schwanstecher M, Shiue CY, Alavi A, Hohnemann S, Piel M, Rosch F, Schirrmacher R: Synthesis and evaluation of (S)-2-(2-[18F]fluoroethoxy)-4-([3-methyl-1-(2-piperidin-1-yl-phenyl)-butyl -carbamoyl]-methyl)-benzoic acid ([18F]repaglinide): a promising radioligand for quantification of pancreatic beta-cell mass with positron emission tomography (PET). Nucl Med Biol. 2004 Jul;31(5):639-47. [PubMed Link Image]
  5. Wangler B, Beck C, Shiue CY, Schneider S, Schwanstecher C, Schwanstecher M, Feilen PJ, Alavi A, Rosch F, Schirrmacher R: Synthesis and in vitro evaluation of (S)-2-([11C]methoxy)-4-[3-methyl-1-(2-piperidine-1-yl-phenyl)-butyl-carbam oyl]-benzoic acid ([11C]methoxy-repaglinide): a potential beta-cell imaging agent. Bioorg Med Chem Lett. 2004 Oct 18;14(20):5205-9. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 709
Target 2 Name ATP-sensitive inward rectifier potassium channel 1
Target 2 Synonyms
  1. ATP-regulated potassium channel ROM-K
  2. Kir1.1
  3. Potassium channel, inwardly rectifying subfamily J member 1
Target 2 Gene Name KCNJ1
Target 2 Protein Sequence >ATP-sensitive inward rectifier potassium channel 1 
MNASSRNVFDTLIRVLTESMFKHLRKWVVTRFFGHSRQRARLVSKDGRCNIEFGNVEAQS
RFIFFVDIWTTVLDLKWRYKMTIFITAFLGSWFFFGLLWYAVAYIHKDLPEFHPSANHTP
CVENINGLTSAFLFSLETQVTIGYGFRCVTEQCATAIFLLIFQSILGVIINSFMCGAILA
KISRPKKRAKTITFSKNAVISKRGGKLCLLIRVANLRKSLLIGSHIYGKLLKTTVTPEGE
TIILDQININFVVDAGNENLFFISPLTIYHVIDHNSPFFHMAAETLLQQDFELVVFLDGT
VESTSATCQVRTSYVPEEVLWGYRFAPIVSKTKEGKYRVDFHNFSKTVEVETPHCAMCLY
NEKDVRARMKRGYDNPNFILSEVNETDDTKM
Target 2 Number of Residues 397
Target 2 Molecular Weight 44795
Target 2 Theoretical pI 9.04
Target 2 GO Classification
Function
transporter activity
ion transporter activity
ion channel activity
voltage-gated ion channel activity
voltage-gated potassium channel activity
inward rectifier potassium channel activity
Process
physiological process
cellular physiological process
transport
ion transport
cation transport
monovalent inorganic cation transport
potassium ion transport
Component
cell
membrane
Target 2 General Function Involved in inward rectifier potassium channel activity
Target 2 Specific Function In the kidney, probably plays a major role in potassium homeostasis. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This channel is activated by internal ATP and can be blocked by external barium
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • 78-102
  • 156-177
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 529313 Link Image
Target 2 UniProtKB/Swiss-Prot ID P48048 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name IRK1_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 2 Gene Sequence >1176 bp 
ATGAATGCTTCCAGTCGGAATGTGTTTGACACGTTGATCAGGGTGTTGACAGAAAGTATG
TTCAAACATCTTCGGAAATGGGTCGTCACTCGCTTTTTTGGGCATTCTCGGCAAAGAGCA
AGGCTAGTCTCCAAAGATGGAAGGTGCAACATAGAATTTGGCAATGTGGAGGCACAGTCA
AGGTTTATATTCTTTGTGGACATCTGGACAACGGTACTTGACCTCAAGTGGAGATACAAA
ATGACCATTTTCATCACAGCCTTCTTGGGGAGTTGGTTTTTCTTTGGTCTCCTGTGGTAT
GCAGTAGCGTACATTCACAAAGACCTCCCGGAATTCCATCCTTCTGCCAATCACACTCCC
TGTGTGGAGAATATTAATGGCTTGACCTCAGCTTTTCTGTTTTCTCTGGAGACTCAAGTG
ACCATTGGATATGGATTCAGGTGTGTGACAGAACAGTGTGCCACTGCCATTTTTCTGCTT
ATCTTTCAGTCTATACTTGGAGTTATAATCAATTCTTTCATGTGTGGGGCCATCTTAGCC
AAGATCTCCAGGCCCAAAAAACGTGCCAAGACCATTACGTTCAGCAAGAACGCAGTGATC
AGCAAACGGGGAGGGAAGCTTTGCCTCCTAATCCGAGTGGCTAATCTCAGGAAGAGCCTT
CTTATTGGCAGTCACATTTATGGAAAGCTTCTGAAGACCACAGTCACTCCTGAAGGAGAG
ACCATTATTTTGGACCAGATCAATATCAACTTTGTAGTTGACGCTGGGAATGAAAATTTA
TTCTTCATCTCCCCATTGACAATTTACCATGTCATTGATCACAACAGCCCTTTCTTCCAC
ATGGCAGCGGAGACCCTTCTCCAGCAGGACTTTGAATTAGTGGTGTTTTTAGATGGCACA
GTGGAGTCCACCAGTGCTACCTGCCAAGTCCGGACATCCTATGTCCCAGAGGAGGTGCTT
TGGGGCTACCGTTTTGCTCCCATAGTATCCAAGACAAAGGAAGGGAAATACCGAGTGGAT
TTCCATAACTTTAGCAAGACAGTGGAAGTGGAGACCCCTCACTGTGCCATGTGCCTTTAT
AATGAGAAAGATGTTAGAGCCAGGATGAAGAGAGGCTATGACAACCCCAACTTCATCTTG
TCAGAAGTCAATGAAACAGATGACACCAAAATGTAA
Target 2 GenBank Gene ID
Target 2 GeneCard ID KCNJ1 Link Image
Target 2 GenAtlas ID KCNJ1 Link Image
Target 2 HGNC ID HGNC:6255 Link Image
Target 2 Chromosome Location 11
Target 2 Locus 11q24
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Krishnan SN, Desai T, Ward DC, Haddad GG: Isolation and chromosomal localization of a human ATP-regulated potassium channel. Hum Genet. 1995 Aug;96(2):155-60. [PubMed Link Image]
  2. Shuck ME, Bock JH, Benjamin CW, Tsai TD, Lee KS, Slightom JL, Bienkowski MJ: Cloning and characterization of multiple forms of the human kidney ROM-K potassium channel. J Biol Chem. 1994 Sep 30;269(39):24261-70. [PubMed Link Image]
  3. Yano H, Philipson LH, Kugler JL, Tokuyama Y, Davis EM, Le Beau MM, Nelson DJ, Bell GI, Takeda J: Alternative splicing of human inwardly rectifying K+ channel ROMK1 mRNA. Mol Pharmacol. 1994 May;45(5):854-60. [PubMed Link Image]
  4. Mutations in the gene encoding the inwardly-rectifying renal potassium channel, ROMK, cause the antenatal variant of Bartter syndrome: evidence for genetic heterogeneity. International Collaborative Study Group for Bartter-like Syndromes. Hum Mol Genet. 1997 Jan;6(1):17-26. [PubMed Link Image]
Target 2 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 781
Target 3 Name ATP-sensitive inward rectifier potassium channel 11
Target 3 Synonyms
  1. IKATP
  2. Inward rectifier K(+) channel Kir6.2
  3. Potassium channel, inwardly rectifying subfamily J member 11
Target 3 Gene Name KCNJ11
Target 3 Protein Sequence >ATP-sensitive inward rectifier potassium channel 11 
MLSRKGIIPEEYVLTRLAEDPAEPRYRARQRRARFVSKKGNCNVAHKNIREQGRFLQDVF
TTLVDLKWPHTLLIFTMSFLCSWLLFAMAWWLIAFAHGDLAPSEGTAEPCVTSIHSFSSA
FLFSIEVQVTIGFGGRMVTEECPLAILILIVQNIVGLMINAIMLGCIFMKTAQAHRRAET
LIFSKHAVIALRHGRLCFMLRVGDLRKSMIISATIHMQVVRKTTSPEGEVVPLHQVDIPM
ENGVGGNSIFLVAPLIIYHVIDANSPLYDLAPSDLHHHQDLEIIVILEGVVETTGITTQA
RTSYLADEILWGQRFVPIVAEEDGRYSVDYSKFGNTIKVPTPLCTARQLDEDHSLLEALT
LASARGPLRKRSVPMAKAKPKFSISPDSLS
Target 3 Number of Residues 396
Target 3 Molecular Weight 43541
Target 3 Theoretical pI 8.10
Target 3 GO Classification
Function
ATP-activated inward rectifier potassium channel activity
transporter activity
ion transporter activity
ion channel activity
voltage-gated ion channel activity
voltage-gated potassium channel activity
inward rectifier potassium channel activity
Process
physiological process
cellular physiological process
transport
ion transport
cation transport
monovalent inorganic cation transport
potassium ion transport
Component
cell
membrane
Target 3 General Function Involved in inward rectifier potassium channel activity
Target 3 Specific Function This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium
Target 3 Pathways Not Available
Target 3 Reactions Not Available
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • 69-93
  • 145-166
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 1088445 Link Image
Target 3 UniProtKB/Swiss-Prot ID Q14654 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name IRK11_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 3 Gene Sequence >1173 bp 
ATGCTGTCCCGCAAGGGCATCATCCCCGAGGAATACGTGCTGACACGCCTGGCAGAGGAC
CCTGCCGAGCCCAGGTACCGTGCCCGCCAGCGGAGGGCCCGCTTTGTGTCCAAGAAAGGC
AACTGCAACGTGGCCCACAAGAACATCCGGGAGCAGGGCCGCTTCCTGCAGGACGTGTTC
ACCACGCTGGTGGACCTCAAGTGGCCACACACATTGCTCATCTTCACCATGTCCTTCCTG
TGCAGCTGGCTGCTCTTCGCCATGGCCTGGTGGCTCATCGCCTTCGCCCACGGTGACCTG
GCCCCCAGCGAGGGCACTGCTGAGCCCTGTGTCACCAGCATCCACTCCTTCTCGTCTGCC
TTCCTTTTCTCCATTGAGGTCCAAGTGACTATTGGCTTTGGGGGGCGCATGGTGACTGAG
GAGTGCCCACTGGCCATCCTGAGCCTCATCGTGCAGAACATCGTGGGGCTCATGATCAAC
GCCATCATGCTTGGCTGCATCTTCATGAAGACTGCCCAAGCCCACCGCAGGGCTGAGACC
CTCATCTTCAGCAAGCATGCGGTGATCGCTCTGCGCCACGGCCGCCTCTGCTTCATGCTA
CGTGTGGGTGACCTCCGCAAGAGCATGATCATCAGCGCCACCATCCACATGCAGGTGGTA
CGCAAGACCACCAGCCCCGAGGGCGAGGTGGTGCCCCTCCACCAGGTGGACATCCCCATG
GAGAACGGCGTGGGTGGCAACAGCATCTTCCTGGTGGCCCCGCTGATCATCTACCATGTC
ATTGATGCCAACAGCCCACTCTACGACCTGGCACCCAGCGACCTGCACCACCACCAGGAC
CTCGAGATCATCGTCATCCTGGAAGGCGTGGTGGAAACCACGGGCATCACCACCCAGGCC
CGCACCTCCTACCTGGCCGATGAGATCCTGTGGGGCCAGCGCTTTGTGCCCATTGTAGCT
GAGGAGGACGGACGTTACTCTGTGGACTACTCCAAGTTTGGCAACACCATCAAAGTGCCC
ACACCACTCTGCACGGCCCGCCAGCTTGATGAGGACCACAGCCTACTGGAAGCTCTGACC
CTCGCCTCAGCCCGCGGGCCCCTGCGCAAGCGCAGCGTGCCCATGGCCAAGGCCAAGCCC
AAGTTCAGCATCTCTCCAGATTCCCTGTCCTGA
Target 3 GenBank Gene ID
Target 3 GeneCard ID KCNJ11 Link Image
Target 3 GenAtlas ID KCNJ11 Link Image
Target 3 HGNC ID HGNC:6257 Link Image
Target 3 Chromosome Location 11
Target 3 Locus 11p15.1
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Aguilar-Bryan L, Bryan J: Molecular biology of adenosine triphosphate-sensitive potassium channels. Endocr Rev. 1999 Apr;20(2):101-35. [PubMed Link Image]
  2. Meissner T, Beinbrech B, Mayatepek E: Congenital hyperinsulinism: molecular basis of a heterogeneous disease. Hum Mutat. 1999;13(5):351-61. [PubMed Link Image]
  3. Halushka MK, Fan JB, Bentley K, Hsie L, Shen N, Weder A, Cooper R, Lipshutz R, Chakravarti A: Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet. 1999 Jul;22(3):239-47. [PubMed Link Image]
  4. Inagaki N, Gonoi T, Clement JP 4th, Namba N, Inazawa J, Gonzalez G, Aguilar-Bryan L, Seino S, Bryan J: Reconstitution of IKATP: an inward rectifier subunit plus the sulfonylurea receptor. Science. 1995 Nov 17;270(5239):1166-70. [PubMed Link Image]
  5. Thomas PM, Cote GJ, Hallman DM, Mathew PM: Homozygosity mapping, to chromosome 11p, of the gene for familial persistent hyperinsulinemic hypoglycemia of infancy. Am J Hum Genet. 1995 Feb;56(2):416-21. [PubMed Link Image]
  6. Sakura H, Wat N, Horton V, Millns H, Turner RC, Ashcroft FM: Sequence variations in the human Kir6.2 gene, a subunit of the beta-cell ATP-sensitive K-channel: no association with NIDDM in while Caucasian subjects or evidence of abnormal function when expressed in vitro. Diabetologia. 1996 Oct;39(10):1233-6. [PubMed Link Image]
  7. Inoue H, Ferrer J, Warren-Perry M, Zhang Y, Millns H, Turner RC, Elbein SC, Hampe CL, Suarez BK, Inagaki N, Seino S, Permutt MA: Sequence variants in the pancreatic islet beta-cell inwardly rectifying K+ channel Kir6.2 (Bir) gene: identification and lack of role in Caucasian patients with NIDDM. Diabetes. 1997 Mar;46(3):502-7. [PubMed Link Image]
Target 3 Drug References
  1. Hansen AM, Christensen IT, Hansen JB, Carr RD, Ashcroft FM, Wahl P: Differential interactions of nateglinide and repaglinide on the human beta-cell sulphonylurea receptor 1. Diabetes. 2002 Sep;51(9):2789-95. [PubMed Link Image]
  2. Lim JG, Lee HY, Yun JE, Kim SP, Park JW, Suh SI, Jang BC, Cho CH, Bae JH, Kim SS, Han J, Park MJ, Song DK: Taurine block of cloned ATP-sensitive K+ channels with different sulfonylurea receptor subunits expressed in Xenopus laevis oocytes. Biochem Pharmacol. 2004 Sep 1;68(5):901-10. [PubMed Link Image]
  3. Hansen AM, Hansen JB, Carr RD, Ashcroft FM, Wahl P: Kir6.2-dependent high-affinity repaglinide binding to beta-cell K(ATP) channels. Br J Pharmacol. 2005 Feb;144(4):551-7. [PubMed Link Image]

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.