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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:08:22
Primary Accession Number DB00790
Secondary Accession Number
  • APRD01178
Name Perindopril
Drug Type
  • Approved
  • Small Molecule
Description An angiotensin-converting enzyme inhibitor. It is used in patients with hypertension and heart failure. [PubChem]
Synonyms
  1. Perindopril Erbumine
Brand Names
  1. Aceon
Brand Mixtures
  1. Coversyl Plus (Indapamide + Perindopril Erbumine)
  2. Preterax (Indapamide + Perindopril Erbumine)
Chemical IUPAC Name (2S,3aS,7aS)-1-[(2S)-2-[[(2S)-1-ethoxy-1-oxopentan-2-yl]amino]propanoyl]-2,3,3a,4,5,6,7,7a-octahydroindole-2-carboxylic acid
Chemical Formula C19H32N2O5
Chemical Structure Structure
CAS Registry Number 107133-36-8
InChI Identifier InChI=1/C19H32N2O5/c1-4-8-14(19(25)26-5-2)20-12(3)17(22)21-15-10-7-6-9-13(15)11-16(21)18(23)24/h12-16,20H,4-11H2,1-3H3,(H,23,24)/t12-,13-,14-,15-,16-/m0/s1/f/h23H
InChI Key IPVQLZZIHOAWMC-ZILWVIQXDO
KEGG Drug D00624 Link Image
KEGG Compound C07707 Link Image
PubChem Compound 107807 Link Image
PubChem Substance 7854486 Link Image
ChEBI ID 8025 Link Image
PharmGKB ID PA450878 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02246624 Link Image
RxList Link http://www.rxlist.com/cgi/generic/aceon.htm Link Image
PDRhealth Link http://www.pdrhealth.com/drug_info/rxdrugprofiles/drugs/ace1543.shtml Link Image
Wikipedia Link http://en.wikipedia.org/wiki/Perindopril Link Image
FDA Label
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 368.4678
Monoisotopic Molecular Weight 368.2311
State Solid
Melting Point Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.22e+00 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 2.6 Source: PhysProp
Predicted LogP 0.56 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -2.48 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 CCC[C@H](N[C@@H](C)C(=O)N1[C@H]2CCCC[C@H]2C[C@H]1C(O)=O)C(=O)OCC
Canonical SMILES CCCC(NC(C)C(=O)N1C2CCCCC2CC1C(O)=O)C(=O)OCC
Drug Category
  • Angiotensin-converting Enzyme Inhibitors
  • Antihypertensive Agents
ATC Codes
AHFS Codes
  • 24:32.04
Indication Used in patients with stable coronary artery disease to reduce the risk of cardiovascular mortality or nonfatal myocardial infarction.
Pharmacology Perindopril is indicated in patients with stable coronary artery disease to reduce the risk of cardiovascular mortality or nonfatal myocardial infarction. It can be used with conventional treatment for management of coronary artery disease, such as antiplatelet, antihypertensive or lipid-lowering therapy. It is also indicated for the treatment of patients with essential hypertension. Perindopril belongs to a group of medicines called ACE inhibitors which block the action of a chemical in the body called angiotensin converting enzyme (ACE). Normally ACE produces another chemical, angiotensin. Thus perindopril reduces the amount of angiotensin in the blood. Angiotensin has two actions. Firstly it acts on blood vessels to make them narrow and secondly it acts on the kidney to produce less urine. As perindopril stops the production of angiotensin, these actions are reversed. Therefore more urine is produced by the kidneys, which results in less fluid in the blood vessels. The blood vessels also widen. The overall effect of this is a drop in blood pressure and a decrease in the workload of the heart.
Mechanism of Action The mechanism through which perindopril lowers blood pressure is believed to be primarily inhibition of angiotensin converting enzyme (ACE) activity. ACE is a peptidyl dipeptidase that catalyzes conversion of the inactive decapeptide, angiotensin I, to the vasoconstrictor, angiotensin II. Angiotensin II is a potent peripheral vasoconstrictor, which stimulates aldosterone secretion by the adrenal cortex, and provides negative feedback on renin secretion. Inhibition of ACE results in decreased plasma angiotensin II, leading to decreased vasoconstriction, increased plasma renin activity and decreased aldosterone secretion. The latter results in diuresis and natriuresis and may be associated with a small increase of serum potassium.
Absorption Rapid
Toxicity Not Available
Protein Binding Approximately 60% of circulating perindopril is bound to plasma proteins.
Biotransformation Perindopril is extensively metabolized following oral administration, with only 4 to 12% of the dose recovered unchanged in the urine.
Half Life Approximately 0.8 to 1.0 hours
Dosage Forms
Form Route
Tablet Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Amiloride Increased risk of hyperkaliemia
Drospirenone Increased risk of hyperkaliemia
Lithium The ACE inhibitor increases serum levels of lithium
Potassium Increased risk of hyperkaliemia
Spironolactone Increased risk of hyperkaliemia
Tizanidine Tizanidine increases the risk of hypotension with the ACE inhibitor
Triamterene Increased risk of hyperkaliemia
Food Interactions
  • Take without regard to meals.
Pathways
Name SMPDB Link KEGG Link
Perindopril Pathway SMP00152 Link Image
General References
  1. Wikipedia Link Image
  2. RxList Link Image
  3. PDRhealth Link Image
Organisms Affected
  • Humans and other mammals
Targets
  1. Angiotensin-converting enzyme, somatic isoform
  2. Islet amyloid polypeptide
Drug Target 1 [top]
Target 1 ID 244
Target 1 Name Angiotensin-converting enzyme, somatic isoform
Target 1 Synonyms
  1. Angiotensin-converting enzyme, somatic isoform precursor
  2. CD143 antigen
  3. Dipeptidyl carboxypeptidase I
  4. EC 3.4.15.1
  5. Kininase II
Target 1 Gene Name ACE
Target 1 Protein Sequence >Angiotensin-converting enzyme, somatic isoform precursor 
MGAASGRRGPGLLLPLPLLLLLPPQPALALDPGLQPGNFSADEAGAQLFAQSYNSSAEQV
LFQSVAASWAHDTNITAENARRQEEAALLSQEFAEAWGQKAKELYEPIWQNFTDPQLRRI
IGAVRTLGSANLPLAKRQQYNALLSNMSRIYSTAKVCLPNKTATCWSLDPDLTNILASSR
SYAMLLFAWEGWHNAAGIPLKPLYEDFTALSNEAYKQDGFTDTGAYWRSWYNSPTFEDDL
EHLYQQLEPLYLNLHAFVRRALHRRYGDRYINLRGPIPAHLLGDMWAQSWENIYDMVVPF
PDKPNLDVTSTMLQQGWNATHMFRVAEEFFTSLELSPMPPEFWEGSMLEKPADGREVVCH
ASAWDFYNRKDFRIKQCTRVTMDQLSTVHHEMGHIQYYLQYKDLPVSLRRGANPGFHEAI
GDVLALSVSTPEHLHKIGLLDRVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFS
GRTPPSRYNFDWWYLRTKYQGICPPVTRNETHFDAGAKFHVPNVTPYIRYFVSFVLQFQF
HEALCKEAGYEGPLHQCDIYRSTKAGAKLRKVLQAGSSRPWQEVLKDMVGLDALDAQPLL
KYFQPVTQWLQEQNQQNGEVLGWPEYQWHPPLPDNYPEGIDLVTDEAEASKFVEEYDRTS
QVVWNEYAEANWNYNTNITTETSKILLQKNMQIANHTLKYGTQARKFDVNQLQNTTIKRI
IKKVQDLERAALPAQELEEYNKILLDMETTYSVATVCHPNGSCLQLEPDLTNVMATSRKY
EDLLWAWEGWRDKAGRAILQFYPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLER
LFQELQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDLVVPFPS
APSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWNKSMLEKPTDGREVVCHAS
AWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQYFMQYKDLPVALREGANPGFHEAIGD
VLALSVSTPKHLHSLNLLSSEGGSDEHDINFLMKMALDKIAFIPFSYLVDQWRWRVFDGS
ITKENYNQEWWSLRLKYQGLCPPVPRTQGDFDPGAKFHIPSSVPYIRYFVSFIIQFQFHE
ALCQAAGHTGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPNMSASAMLSY
FKPLLDWLRTENELHGEKLGWPQYNWTPNSARSEGPLPDSGRVSFLGLDLDAQQARVGQW
LLLFLGIALLVATLGLSQRLFSIRHRSLHRHSHGPQFGSEVELRHS
Target 1 Number of Residues 1327
Target 1 Molecular Weight 149716
Target 1 Theoretical pI 6.36
Target 1 GO Classification
Function
peptidyl-dipeptidase A activity
binding
ion binding
cation binding
transition metal ion binding
zinc ion binding
catalytic activity
hydrolase activity
peptidase activity
metallopeptidase activity
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
cellular protein metabolism
proteolysis
Component
cell
membrane
Target 1 General Function Involved in metallopeptidase activity
Target 1 Specific Function Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator
Target 1 Pathways Not Available
Target 1 Reactions
  • Release of a C-terminal dipeptide, oligopeptide!Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II COFACTOR Zinc INHIBITOR (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(mercaptomethyl)-1-oxoprolyl]g lycine; (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(mercaptomethyl)-1-oxoprolyl]- (S)-alanine; (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(acetylthio)methyl-1-oxoprolyl ]glycine benzyl ester; (S)-N-[3-(3,4-Methylenedioxyphenyl)-2-(acetylthio)methyl-1-oxoprolyl ]-(S)-alanine benzyl ester EFFECTOR Chloride
Target 1 Pfam Domain Function
Target 1 Signals
  • 1-29
Target 1 Transmembrane Regions
  • 1260-1276
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 178286 Link Image
Target 1 UniProtKB/Swiss-Prot ID P12821 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name ACE_HUMAN Link Image
Target 1 PDB ID 1UZF Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Cell membrane
  • single-pass type I membrane protein. Processed form:Secreted protein. A soluble form
Target 1 Gene Sequence >3921 bp 
ATGGGGGCCGCCTCGGGCCGCCGGGGGCCGGGGCTGCTGCTGCCGCTGCCGCTGCTGTTG
CTGCTGCCGCCGCAGCCCGCCCTGGCGTTGGACCCCGGGCTGCAGCCCGGCAACTTTTCT
GCTGACGAGGCCGGGGCGCAGCTCTTCGCGCAGAGCTACAACTCCAGCGCCGAACAGGTG
CTGTTCCAGAGCGTGGCCGCCAGCTGGGCGCACGACACCAACATCACCGCGGAGAATGCA
AGGCGCCAGGAGGAAGCAGCCCTGCTCAGCCAGGAGTTTGCGGAGGCCTGGGGCCAGAAG
GCCAAGGAGCTGTATGAACCGATCTGGCAGAACTTCACGGACCCGCAGCTGCGCAGGATC
ATCGGAGCTGTGCGAACCCTGGGCTCTGCCAACCTGCCCCTGGCTAAGCGGCAGCAGTAC
AACGCCCTGCTAAGCAACATGAGCAGGATCTACTCCACCGCCAAGGTCTGCCTCCCCAAC
AAGACTGCCACCTGCTGGTCCCTGGACCCAGATCTCACCAACATCCTGGCTTCCTCGCGA
AGCTACGCCATGCTCCTGTTTGCCTGGGAGGGCTGGCACAACGCTGCGGGCATCCCGCTG
AAACCGCTGTACGAGGATTTCACTGCCCTCAGCAATGAAGCCTACAAGCAGGACGGCTTC
ACAGACACGGGGGCCTACTGGCGCTCCTGGTACAACTCCCCCACCTTCGAGGACGATCTG
GAACACCTCTACCAACAGCTAGAGCCCCTCTACCTGAACCTCCATGCCTTCGTCCGCCGC
GCACTGCATCGCCGATACGGAGACAGATACATCAACCTCAGGGGACCCATCCCTGCTCAT
CTGCTGGGAGACATGTGGGCCCAGAGCTGGGAAAACATCTACGACATGGTGGTGCCTTTC
CCAGACAAGCCCAACCTCGATGTCACCAGTACTATGCTGCAGCAGGGCTGGAACGCCACG
CACATGTTCCGGGTGGCAGAGGAGTTCTTCACCTCCCTGGAGCTCTCCCCCATGCCTCCC
GAGTTCTGGGAAGGGTCGATGCTGGAGAAGCCGGCCGACGGGCGGGAAGTGGTGTGCCAC
GCCTCGGCTTGGGACTTCTACAACAGGAAAGACTTCAGGATCAAGCAGTGCACACGGGTC
ACGATGGACCAGCTCTCCACAGTGCACCATGAGATGGGCCATATACAGTACTACCTGCAG
TACAAGGATCTGCCCGTCTCCCTGCGTCGGGGGGCCAACCCCGGCTTCCATGAGGCCATT
GGGGACGTGCTGGCGCTCTCGGTCTCCACTCCTGAACATCTGCACAAAATCGGCCTGCTG
GACCGTGTCACCAATGACACGGAAAGTGACATCAATTACTTGCTAAAAATGGCACTGGAA
AAAATTGCCTTCCTGCCCTTTGGCTACTTGGTGGACCAGTGGCGCTGGGGGGTCTTTAGT
GGGCGTACCCCCCCTTCCCGCTACAACTTCGACTGGTGGTATCTTCGAACCAAGTATCAG
GGGATCTGTCCTCCTGTTACCCGAAACGAAACCCACTTTGATGCTGGAGCTAAGTTTCAT
GTTCCAAATGTGACACCATACATCAGGTACTTTGTGAGTTTTGTCCTGCAGTTCCAGTTC
CATGAAGCCCTGTGCAAGGAGGCAGGCTATGAGGGCCCACTGCACCAGTGTGACATCTAC
CGGTCCACCAAGGCAGGGGCCAAGCTCCGGAAGGTGCTGCAGGCTGGCTCCTCCAGGCCC
TGGCAGGAGGTGCTGAAGGACATGGTCGGCTTAGATGCCCTGGATGCCCAGCCGCTGCTC
AAGTACTTCCAGCCAGTCACCCAGTGGCTGCAGGAGCAGAACCAGCAGAACGGCGAGGTC
CTGGGCTGGCCCGAGTACCAGTGGCACCCGCCGTTGCCTGACAACTACCCGGAGGGCATA
GACCTGGTGACTGATGAGGCTGAGGCCAGCAAGTTTGTGGAGGAATATGACCGGACATCC
CAGGTGGTGTGGAACGAGTATGCCGAGGCCAACTGGAACTACAACACCAACATCACCACA
GAGACCAGCAAGATTCTGCTGCAGAAGAACATGCAAATAGCCAACCACACCCTGAAGTAC
GGCACCCAGGCCAGGAAGTTTGATGTGAACCAGTTGCAGAACACCACTATCAAGCGGATC
ATAAAGAAGGTTCAGGACCTAGAACGGGCAGCGCTGCCTGCCCAGGAGCTGGAGGAGTAC
AACAAGATCCTGTTGGATATGGAAACCACCTACAGCGTGGCCACTGTGTGCCACCCGAAT
GGCAGCTGCCTGCAGCTCGAGCCAGATCTGACGAATGTGATGGCCACATCCCGGAAATAT
GAAGACCTGTTATGGGCATGGGAGGGCTGGCGAGACAAGGCGGGGAGAGCCATCCTCCAG
TTTTACCCGAAATACGTGGAACTCATCAACCAGGCTGCCCGGCTCAATGGCTATGTAGAT
GCAGGGGACTCGTGGAGGTCTATGTACGAGACACCATCCCTGGAGCAAGACCTGGAGCGG
CTCTTCCAGGAGCTGCAGCCACTCTACCTCAACCTGCATGCCTACGTGCGCCGGGCCCTG
CACCGTCACTACGGGGCCCAGCACATCAACCTGGAGGGGCCCATTCCTGCTCACCTGCTG
GGGAACATGTGGGCGCAGACCTGGTCCAACATCTATGACTTGGTGGTGCCCTTCCCTTCA
GCCCCCTCGATGGACACCACAGAGGCTATGCTAAAGCAGGGCTGGACGCCCAGGAGGATG
TTTAAGGAGGCTGATGATTTCTTCACCTCCCTGGGGCTGCTGCCCGTGCCTCCTGAGTTC
TGGAACAAGTCGATGCTGGAGAAGCCAACCGACGGGCGGGAGGTGGTCTGCCACGCCTCG
GCCTGGGACTTCTACAACGGCAAGGACTTCCGGATCAAGCAGTGCACCACCGTGAACTTG
GAGGACCTGGTGGTGGCCCACCACGAAATGGGCCACATCCAGTATTTCATGCAGTACAAA
GACTTACCTGTGGCCTTGAGGGAGGGTGCCAACCCCGGCTTCCATGAGGCCATTGGGGAC
GTGCTAGCCCTCTCAGTGTCTACGCCCAAGCACCTGCACAGTCTCAACCTGCTGAGCAGT
GAGGGTGGCAGCGACGAGCATGACATCAACTTTCTGATGAAGATGGCCCTTGACAAGATC
GCCTTTATCCCCTTCAGCTACCTCGTCGATCAGTGGCGCTGGAGGGTATTTGATGGAAGC
ATCACCAAGGAGAACTATAACCAGGAGTGGTGGAGCCTCAGGCTGAAGTACCAGGGCCTC
TGCCCCCCAGTGCCCAGGACTCAAGGTGACTTTGACCCAGGGGCCAAGTTCCACATTCCT
TCTAGCGTGCCTTACATCAGGTACTTTGTCAGCTTCATCATCCAGTTCCAGTTCCACGAG
GCACTGTGCCAGGCAGCTGGCCACACGGGCCCCCTGCACAAGTGTGACATCTACCAGTCC
AAGGAGGCCGGGCAGCGCCTGGCGACCGCCATGAAGCTGGGCTTCAGTAGGCCGTGGCCG
GAAGCCATGCAGCTGATCACGGGCCAGCCCAACATGAGCGCCTCGGCCATGTTGAGCTAC
TTCAAGCCGCTGCTGGACTGGCTCCGCACGGAGAACGAGCTGCATGGGGAGAAGCTGGGC
TGGCCGCAGTACAACTGGACGCCGAACTCCGCTCGCTCAGAAGGGCCCCTCCCAGACAGC
GGCCGCGTCAGCTTCCTGGGCCTGGACCTGGATGCGCAGCAGGCCCGCGTGGGCCAGTGG
CTGCTGCTCTTCCTGGGCATCGCCCTGCTGGTAGCCACCCTGGGCCTCAGCCAGCGGCTC
TTCAGCATCCGCCACCGCAGCCTCCACCGGCACTCCCACGGGCCCCAGTTCGGCTCCGAG
GTGGAGCTGAGACACTCCTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID ACE Link Image
Target 1 GenAtlas ID ACE Link Image
Target 1 HGNC ID HGNC:2707 Link Image
Target 1 Chromosome Location 17
Target 1 Locus 17q23.3
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Rieder MJ, Taylor SL, Clark AG, Nickerson DA: Sequence variation in the human angiotensin converting enzyme. Nat Genet. 1999 May;22(1):59-62. [PubMed Link Image]
  2. 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]
  3. Tipnis SR, Hooper NM, Hyde R, Karran E, Christie G, Turner AJ: A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase. J Biol Chem. 2000 Oct 27;275(43):33238-43. [PubMed Link Image]
  4. Donoghue M, Hsieh F, Baronas E, Godbout K, Gosselin M, Stagliano N, Donovan M, Woolf B, Robison K, Jeyaseelan R, Breitbart RE, Acton S: A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9. Circ Res. 2000 Sep 1;87(5):E1-9. [PubMed Link Image]
  5. Harmer D, Gilbert M, Borman R, Clark KL: Quantitative mRNA expression profiling of ACE 2, a novel homologue of angiotensin converting enzyme. FEBS Lett. 2002 Dec 4;532(1-2):107-10. [PubMed Link Image]
  6. Ehlers MR, Riordan JF: Angiotensin-converting enzyme: zinc- and inhibitor-binding stoichiometries of the somatic and testis isozymes. Biochemistry. 1991 Jul 23;30(29):7118-26. [PubMed Link Image]
  7. Takeuchi K, Shimizu T, Ohishi N, Seyama Y, Takaku F, Yotsumoto H: Purification of human lung angiotensin-converting enzyme by high-performance liquid chromatography: properties and N-terminal amino acid sequence. J Biochem (Tokyo). 1989 Sep;106(3):442-5. [PubMed Link Image]
  8. Soubrier F, Alhenc-Gelas F, Hubert C, Allegrini J, John M, Tregear G, Corvol P: Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning. Proc Natl Acad Sci U S A. 1988 Dec;85(24):9386-90. [PubMed Link Image]
Target 1 Drug References
  1. Yoshiji H, Kuriyama S, Kawata M, Yoshii J, Ikenaka Y, Noguchi R, Nakatani T, Tsujinoue H, Fukui H: The angiotensin-I-converting enzyme inhibitor perindopril suppresses tumor growth and angiogenesis: possible role of the vascular endothelial growth factor. Clin Cancer Res. 2001 Apr;7(4):1073-8. [PubMed Link Image]
  2. Yasumatsu R, Nakashima T, Masuda M, Ito A, Kuratomi Y, Nakagawa T, Komune S: Effects of the angiotensin-I converting enzyme inhibitor perindopril on tumor growth and angiogenesis in head and neck squamous cell carcinoma cells. J Cancer Res Clin Oncol. 2004 Oct;130(10):567-73. Epub 2004 Jul 27. [PubMed Link Image]
  3. Jastrzebskal M, Widecka K, Naruszewicz M, Ciechanowicz A, Janczak-Bazan A, Foltynska A, Goracy I, Chetstowski K, Wesotowska T: Effects of perindopril treatment on hemostatic function in patients with essential hypertension in relation to angiotensin converting enzyme (ACE) and plasminogen activator inhibitor-1 (PAI-1) gene polymorphisms. Nutr Metab Cardiovasc Dis. 2004 Oct;14(5):259-69. [PubMed Link Image]
  4. Bray L, Lartaud I, Muller F, Atkinson J, Capdeville C: Effects of the angiotensin I converting enzyme inhibitor perindopril on cerebral blood flow in awake hypertensive rats. Am J Hypertens. 1991 Mar;4(3 Pt 2):246S-252S. [PubMed Link Image]
  5. Charpiot P, Rolland PH, Friggi A, Piquet P, Scalbert E, Bodard H, Barlatier A, Latrille V, Tranier P, Mercier C, et al.: ACE inhibition with perindopril and atherogenesis-induced structural and functional changes in minipig arteries. Arterioscler Thromb. 1993 Aug;13(8):1125-38. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 1170
Target 2 Name Islet amyloid polypeptide
Target 2 Synonyms
  1. Amylin
  2. DAP
  3. Diabetes-associated peptide
  4. Insulinoma amyloid peptide
  5. Islet amyloid polypeptide precursor
Target 2 Gene Name IAPP
Target 2 Protein Sequence >Islet amyloid polypeptide precursor 
MGILKLQVFLIVLSVALNHLKATPIESHQVEKRKCNTATCATQRLANFLVHSSNNFGAIL
SSTNVGSNTYGKRNAVEVLKREPLNYLPL
Target 2 Number of Residues 90
Target 2 Molecular Weight 9807
Target 2 Theoretical pI 10.39
Target 2 GO Classification
Function
signal transducer activity
receptor binding
hormone activity
Process
Not Available
Component
extracellular region
Target 2 General Function Involved in hormone activity
Target 2 Specific Function Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • 1-22
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 457131 Link Image
Target 2 UniProtKB/Swiss-Prot ID P10997 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name IAPP_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Secreted protein
Target 2 Gene Sequence >190 bp 
TCATCAGGTGGAAAAGCGGAAATGCAACACTGCCACATGTGCAACGCAGCGCCTGGCAAA
TTTTTTAGTTCATTCCAGCAACAACTTTGGTGCCATTCTCTCATCTACCAACGTGGGATC
CAATACATATGGCAAGAGGAATGCAGTAGAGGTTTTAAAGAGAGAGCCACTGAATTACTT
GCCCCTTTAG
Target 2 GenBank Gene ID
Target 2 GeneCard ID IAPP Link Image
Target 2 GenAtlas ID IAPP Link Image
Target 2 HGNC ID HGNC:5329 Link Image
Target 2 Chromosome Location Not Available
Target 2 Locus Not Available
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Hoppener JW, Oosterwijk C, Visser-Vernooy HJ, Lips CJ, Jansz HS: Characterization of the human islet amyloid polypeptide/amylin gene transcripts: identification of a new polyadenylation site. Biochem Biophys Res Commun. 1992 Dec 30;189(3):1569-77. [PubMed Link Image]
  2. Hubbard JA, Martin SR, Chaplin LC, Bose C, Kelly SM, Price NC: Solution structures of calcitonin-gene-related-peptide analogues of calcitonin-gene-related peptide and amylin. Biochem J. 1991 May 1;275 ( Pt 3):785-8. [PubMed Link Image]
  3. van Mansfeld AD, Mosselman S, Hoppener JW, Zandberg J, van Teeffelen HA, Baas PD, Lips CJ, Jansz HS: Islet amyloid polypeptide: structure and upstream sequences of the IAPP gene in rat and man. Biochim Biophys Acta. 1990 Oct 23;1087(2):235-40. [PubMed Link Image]
  4. Christmanson L, Rorsman F, Stenman G, Westermark P, Betsholtz C: The human islet amyloid polypeptide (IAPP) gene. Organization, chromosomal localization and functional identification of a promoter region. FEBS Lett. 1990 Jul 2;267(1):160-6. [PubMed Link Image]
  5. Nishi M, Sanke T, Seino S, Eddy RL, Fan YS, Byers MG, Shows TB, Bell GI, Steiner DF: Human islet amyloid polypeptide gene: complete nucleotide sequence, chromosomal localization, and evolutionary history. Mol Endocrinol. 1989 Nov;3(11):1775-81. [PubMed Link Image]
  6. Mosselman S, Hoppener JW, Lips CJ, Jansz HS: The complete islet amyloid polypeptide precursor is encoded by two exons. FEBS Lett. 1989 Apr 10;247(1):154-8. [PubMed Link Image]
  7. Roberts AN, Leighton B, Todd JA, Cockburn D, Schofield PN, Sutton R, Holt S, Boyd Y, Day AJ, Foot EA, et al.: Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus. Proc Natl Acad Sci U S A. 1989 Dec;86(24):9662-6. [PubMed Link Image]
  8. Westermark P, Wernstedt C, Wilander E, Hayden DW, O'Brien TD, Johnson KH: Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells. Proc Natl Acad Sci U S A. 1987 Jun;84(11):3881-5. [PubMed Link Image]
  9. Sanke T, Bell GI, Sample C, Rubenstein AH, Steiner DF: An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing. J Biol Chem. 1988 Nov 25;263(33):17243-6. [PubMed Link Image]
  10. Mosselman S, Hoppener JW, Zandberg J, van Mansfeld AD, Geurts van Kessel AH, Lips CJ, Jansz HS: Islet amyloid polypeptide: identification and chromosomal localization of the human gene. FEBS Lett. 1988 Nov 7;239(2):227-32. [PubMed Link Image]
  11. 3535798 Westermark P, Wernstedt C, Wilander E, Sletten K: A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas. Biochem Biophys Res Commun. 1986 Nov 14;140(3):827-31.
  12. 8772735 Sakagashira S, Sanke T, Hanabusa T, Shimomura H, Ohagi S, Kumagaye KY, Nakajima K, Nanjo K: Missense mutation of amylin gene (S20G) in Japanese NIDDM patients. Diabetes. 1996 Sep;45(9):1279-81.
  13. 9794116 Chuang LM, Lee KC, Huang CN, Wu HP, Tai TY, Lin BJ: Role of S20G mutation of amylin gene in insulin secretion, insulin sensitivity, and type II diabetes mellitus in Taiwanese patients. Diabetologia. 1998 Oct;41(10):1250-1.
Target 2 Drug References
  1. Cao Z, Wookey PJ, Wu LL, Voskuil M, van Geenen RC, Cooper ME: Renal amylin binding in normotensive and hypertensive rats: effects of angiotensin converting enzyme inhibition with perindopril. J Hypertens. 1997 Nov;15(11):1245-52. [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.