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Identification
NameCaptopril
Accession NumberDB01197  (APRD00164)
Typesmall molecule
Groupsapproved
Description

Captopril is a potent, competitive inhibitor of angiotensin-converting enzyme (ACE), the enzyme responsible for the conversion of angiotensin I (ATI) to angiotensin II (ATII). ATII regulates blood pressure and is a key component of the renin-angiotensin-aldosterone system (RAAS). Captopril may be used in the treatment of hypertension.

Structure
Thumb
Synonyms
SynonymLanguageCode
CaptoprilumLatinINN
CaptoprylNot AvailableNot Available
L-CaptoprilNot AvailableNot Available
SaltsNot Available
Brand names
NameCompany
AcepressBernofarm (Indonesia), BMS (Italy)
AceprilBMS (United Kingdom)
AlopresinNot Available
ApoprilNot Available
CapotenBristol-Myers Squibb, Par
CaptolaneSanofi-Aventis (France)
CaptorilNovopharm (Canada)
CesplonEsteve (Spain)
DilabarQualigen (Spain)
GarranilAristegui (Spain)
HipertilNormal (Portugal)
HypertilNormal (Portugal)
LopirinBMS (Germany,Switzerland)
LoprilOrion (Finland), BMS (France)
TenosbonNot Available
TensoprelRubio (Spain)
Brand mixtures
Brand NameIngredients
Acediurcaptopril + hydrochlorothiazide
Acepluscaptopril + hydrochlorothiazide
Capozidecaptopril + hydrochlorothiazide
Categories
CAS number62571-86-2
WeightAverage: 217.285
Monoisotopic: 217.077264041
Chemical FormulaC9H15NO3S
InChI KeyInChIKey=FAKRSMQSSFJEIM-RQJHMYQMSA-N
InChI
InChI=1S/C9H15NO3S/c1-6(5-14)8(11)10-4-2-3-7(10)9(12)13/h6-7,14H,2-5H2,1H3,(H,12,13)/t6-,7+/m1/s1
IUPAC Name
(2S)-1-[(2S)-2-methyl-3-sulfanylpropanoyl]pyrrolidine-2-carboxylic acid
SMILES
C[C@H](CS)C(=O)N1CCC[C@H]1C(O)=O
Mass SpecNot Available
Taxonomy
KingdomOrganic Compounds
SuperclassOrganic Acids and Derivatives
ClassCarboxylic Acids and Derivatives
SubclassAmino Acids, Peptides, and Analogues
Direct parentN-acyl-alpha Amino Acids
Alternative parentsPyrrolidine Carboxylic Acids; Tertiary Carboxylic Acid Amides; Tertiary Amines; Polyamines; Enolates; Carboxylic Acids; Alkylthiols
Substituentspyrrolidine carboxylic acid or derivative; pyrrolidine carboxylic acid; tertiary carboxylic acid amide; pyrrolidine; carboxamide group; tertiary amine; alkylthiol; polyamine; enolate; carboxylic acid; amine; organonitrogen compound
Classification descriptionThis compound belongs to the n-acyl-alpha amino acids. These are compounds containing an alpha amino acid which bears an acyl group at his terminal nitrogen atom.
Pharmacology
IndicationFor the treatment of essential or renovascular hypertension (usually administered with other drugs, particularly thiazide diuretics). May be used to treat congestive heart failure in combination with other drugs (e.g. cardiac glycosides, diuretics, β-adrenergic blockers). May improve survival in patients with left ventricular dysfunction following myocardial infarction. May be used to treat nephropathy, including diabetic nephropathy.
PharmacodynamicsCaptopril, an ACE inhibitor, antagonizes the effect of the RAAS. The RAAS is a homeostatic mechanism for regulating hemodynamics, water and electrolyte balance. During sympathetic stimulation or when renal blood pressure or blood flow is reduced, renin is released from the granular cells of the juxtaglomerular apparatus in the kidneys. In the blood stream, renin cleaves circulating angiotensinogen to ATI, which is subsequently cleaved to ATII by ACE. ATII increases blood pressure using a number of mechanisms. First, it stimulates the secretion of aldosterone from the adrenal cortex. Aldosterone travels to the distal convoluted tubule (DCT) and collecting tubule of nephrons where it increases sodium and water reabsorption by increasing the number of sodium channels and sodium-potassium ATPases on cell membranes. Second, ATII stimulates the secretion of vasopressin (also known as antidiuretic hormone or ADH) from the posterior pituitary gland. ADH stimulates further water reabsorption from the kidneys via insertion of aquaporin-2 channels on the apical surface of cells of the DCT and collecting tubules. Third, ATII increases blood pressure through direct arterial vasoconstriction. Stimulation of the Type 1 ATII receptor on vascular smooth muscle cells leads to a cascade of events resulting in myocyte contraction and vasoconstriction. In addition to these major effects, ATII induces the thirst response via stimulation of hypothalamic neurons. ACE inhibitors inhibit the rapid conversion of ATI to ATII and antagonize RAAS-induced increases in blood pressure. ACE (also known as kininase II) is also involved in the enzymatic deactivation of bradykinin, a vasodilator. Inhibiting the deactivation of bradykinin increases bradykinin levels and may sustain its effects by causing increased vasodilation and decreased blood pressure.
Mechanism of actionThere are two isoforms of ACE: the somatic isoform, which exists as a glycoprotein comprised of a single polypeptide chain of 1277; and the testicular isoform, which has a lower molecular mass and is thought to play a role in sperm maturation and binding of sperm to the oviduct epithelium. Somatic ACE has two functionally active domains, N and C, which arise from tandem gene duplication. Although the two domains have high sequence similarity, they play distinct physiological roles. The C-domain is predominantly involved in blood pressure regulation while the N-domain plays a role in hematopoietic stem cell differentiation and proliferation. ACE inhibitors bind to and inhibit the activity of both domains, but have much greater affinity for and inhibitory activity against the C-domain. Captopril, one of the few ACE inhibitors that is not a prodrug, competes with ATI for binding to ACE and inhibits and enzymatic proteolysis of ATI to ATII. Decreasing ATII levels in the body decreases blood pressure by inhibiting the pressor effects of ATII as described in the Pharmacology section above. Captopril also causes an increase in plasma renin activity likely due to a loss of feedback inhibition mediated by ATII on the release of renin and/or stimulation of reflex mechanisms via baroreceptors. Captopril’s affinity for ACE is approximately 30,000 times greater than that of ATI.
Absorption60-75% in fasting individuals; food decreases absorption by 25-40% (some evidence indicates that this is not clinically significant)
Volume of distributionNot Available
Protein binding25-30% bound to plasma proteins, primarily albumin
Metabolism

Hepatic. Major metabolites are captopril-cysteine disulfide and the disulfide dimer of captopril. Metabolites may undergo reversible interconversion.

SubstrateEnzymesProduct
Captopril
    captopril-cysteine disulfideDetails
    Route of eliminationNot Available
    Half life2 hours
    ClearanceNot Available
    ToxicitySymptoms of overdose include emesis and decreased blood pressure. Side effects include dose-dependent rash (usually maculopapular), taste alterations, hypotension, gastric irritation, cough, and angioedema.
    Affected organisms
    • Humans and other mammals
    Pathways
    PathwayCategorySMPDB ID
    Captopril Action PathwayDrug actionSMP00146
    SNP Mediated EffectsNot Available
    SNP Mediated Adverse Drug ReactionsNot Available
    ADMET
    Predicted ADMET features
    Property Value Probability
    Human Intestinal Absorption + 0.97
    Blood Brain Barrier + 0.6467
    Caco-2 permeable + 0.8867
    P-glycoprotein substrate Non-substrate 0.6276
    P-glycoprotein inhibitor I Non-inhibitor 0.8448
    P-glycoprotein inhibitor II Non-inhibitor 0.7415
    Renal organic cation transporter Non-inhibitor 0.8073
    CYP450 2C9 substrate Non-substrate 0.7898
    CYP450 2D6 substrate Substrate 0.8918
    CYP450 3A4 substrate Non-substrate 0.6293
    CYP450 1A2 substrate Non-inhibitor 0.9045
    CYP450 2C9 substrate Non-inhibitor 0.9102
    CYP450 2D6 substrate Non-inhibitor 0.9537
    CYP450 2C19 substrate Non-inhibitor 0.9025
    CYP450 3A4 substrate Non-inhibitor 0.9049
    CYP450 inhibitory promiscuity Low CYP Inhibitory Promiscuity 0.8975
    Ames test Non AMES toxic 0.8164
    Carcinogenicity Non-carcinogens 0.9434
    Biodegradation Not ready biodegradable 0.6577
    Rat acute toxicity 1.7403 LD50, mol/kg Not applicable
    hERG inhibition (predictor I) Weak inhibitor 0.9604
    hERG inhibition (predictor II) Non-inhibitor 0.9118
    Pharmacoeconomics
    Manufacturers
    • Par pharmaceutical inc
    • Apotex inc
    • Apothecon inc div bristol myers squibb
    • Clonmel healthcare ltd
    • Egis pharmaceuticals ltd
    • Endo laboratories inc div dupont merck pharmaceutical co
    • Huahai us inc
    • Ivax pharmaceuticals inc sub teva pharmaceuticals usa
    • Mylan laboratories inc
    • Purepac pharmaceutical co
    • Sandoz inc
    • Stason industrial corp
    • Teva pharmaceuticals usa inc
    • Teva pharmaceuticals usa
    • Watson laboratories inc
    • West ward pharmaceutical corp
    • Wockhardt americas inc
    Packagers
    Dosage forms
    FormRouteStrength
    TabletOral100 mg
    TabletOral12.5 mg
    TabletOral25 mg
    TabletOral50 mg
    Prices
    Unit descriptionCostUnit
    Captopril powder22.03USDg
    Capoten 100 mg tablet4.53USDtablet
    Capoten 12.5 mg tablet1.8USDtablet
    Captopril 100 mg tablet1.53USDtablet
    Captopril 50 mg tablet1.14USDtablet
    Capoten 25 mg tablet1.13USDtablet
    Capoten 50 mg tablet1.13USDtablet
    Apo-Capto 100 mg Tablet1.09USDtablet
    Mylan-Captopril 100 mg Tablet1.09USDtablet
    Novo-Captoril 100 mg Tablet1.09USDtablet
    Nu-Capto 100 mg Tablet1.09USDtablet
    Captopril 25 mg tablet0.67USDtablet
    Captopril 12.5 mg tablet0.62USDtablet
    Apo-Capto 50 mg Tablet0.59USDtablet
    Mylan-Captopril 50 mg Tablet0.59USDtablet
    Novo-Captoril 50 mg Tablet0.59USDtablet
    Nu-Capto 50 mg Tablet0.59USDtablet
    Apo-Capto 25 mg Tablet0.31USDtablet
    Mylan-Captopril 25 mg Tablet0.31USDtablet
    Novo-Captoril 25 mg Tablet0.31USDtablet
    Nu-Capto 25 mg Tablet0.31USDtablet
    Apo-Capto 12.5 mg Tablet0.22USDtablet
    Mylan-Captopril 12.5 mg Tablet0.22USDtablet
    Novo-Captoril 12.5 mg Tablet0.22USDtablet
    Nu-Capto 12.5 mg Tablet0.22USDtablet
    DrugBank does not sell nor buy drugs. Pricing information is supplied for informational purposes only.
    Patents
    CountryPatent NumberApprovedExpires (estimated)
    United States52389241993-08-242010-08-24
    Properties
    Statesolid
    Experimental Properties
    PropertyValueSource
    melting point103-104Ondetti, M.A. and Cushman, D.W.; U.S. Patent 4,046,889; September 6, 1977; assigned t o E.R. Squibb & Sons, Inc. Ondetti, M.A. and Cushman, D.W.; U.S. Patent 4,105,776; August 8,1978; assigned to E.R. Squibb & Sons, Inc. Ondetti, M.A. and Cushman, D.W.; U.S. Patent 4,154,840; May 15,1979; assigned to E.R. Squibb & Sons, Inc.
    water solubilityFreely solubleNot Available
    logP0.34RANADIVE,SA ET AL. (1992)
    Predicted Properties
    PropertyValueSource
    water solubility4.52e+00 g/lALOGPS
    logP1.02ALOGPS
    logP0.73ChemAxon
    logS-1.7ALOGPS
    pKa (strongest acidic)4.02ChemAxon
    pKa (strongest basic)-1.2ChemAxon
    physiological charge-1ChemAxon
    hydrogen acceptor count3ChemAxon
    hydrogen donor count2ChemAxon
    polar surface area57.61ChemAxon
    rotatable bond count3ChemAxon
    refractivity54.63ChemAxon
    polarizability21.72ChemAxon
    number of rings1ChemAxon
    bioavailability1ChemAxon
    rule of fiveYesChemAxon
    Ghose filterYesChemAxon
    Veber's ruleNoChemAxon
    MDDR-like ruleNoChemAxon
    Spectra
    SpectraNot Available
    References
    Synthesis Reference

    Charles M. Zepp, “Methods for preparing captopril and its analogues.” U.S. Patent US5166361, issued July, 1981.

    US5166361
    General Reference
    1. Atkinson AB, Robertson JI: Captopril in the treatment of clinical hypertension and cardiac failure. Lancet. 1979 Oct 20;2(8147):836-9. Pubmed
    2. Patchett AA, Harris E, Tristram EW, Wyvratt MJ, Wu MT, Taub D, Peterson ER, Ikeler TJ, ten Broeke J, Payne LG, Ondeyka DL, Thorsett ED, Greenlee WJ, Lohr NS, Hoffsommer RD, Joshua H, Ruyle WV, Rothrock JW, Aster SD, Maycock AL, Robinson FM, Hirschmann R, Sweet CS, Ulm EH, Gross DM, Vassil TC, Stone CA: A new class of angiotensin-converting enzyme inhibitors. Nature. 1980 Nov 20;288(5788):280-3. Pubmed
    3. Smith CG, Vane JR: The discovery of captopril. FASEB J. 2003 May;17(8):788-9. Pubmed
    External Links
    ResourceLink
    KEGG DrugD00251
    PubChem Compound44093
    PubChem Substance46506879
    ChemSpider40130
    BindingDB21642
    ChEBI3380
    ChEMBLCHEMBL1560
    Therapeutic Targets DatabaseDAP000589
    PharmGKBPA448780
    Drug Product Database2242791
    RxListhttp://www.rxlist.com/cgi/generic/captop.htm
    Drugs.comhttp://www.drugs.com/captopril.html
    PDRhealthhttp://www.pdrhealth.com/drug_info/rxdrugprofiles/drugs/cap1064.shtml
    WikipediaCaptopril
    ATC CodesC09AA01
    AHFS Codes
    • 24:32.04
    PDB Entries
    FDA labelNot Available
    MSDSshow(37.6 KB)
    Interactions
    Drug Interactions
    Drug
    AmilorideIncreased risk of hyperkalemia
    AprotininIn study of nine patients with untreated hypertension, aprotinin infused intravenously in a dose of 2 million KIU over two hours blocked the acute hypotensive effect of 100mg of captopril.
    Azilsartan medoxomilPharmacodynamic synergism: dual blockade of renin-angiotensin system. Increases risks of hypotension, hyperkalemia, renal impairment.
    DrospirenoneIncreased risk of hyperkalemia
    IcatibantIcatibant may attenuate the antihypertensive effect of ACE inhibitors by pharmacodynamic antagonism. Monitor concomitant therapy closely.
    LithiumThe ACE inhibitor increases serum levels of lithium
    PotassiumIncreased risk of hyperkalemia
    SpironolactoneIncreased risk of hyperkalemia
    TerbinafineTerbinafine may reduce the metabolism and clearance of Captopril. Consider alternate therapy or monitor for therapeutic/adverse effects of Captopril if Terbinafine is initiated, discontinued or dose changed.
    TizanidineTizanidine increases the risk of hypotension with the ACE inhibitor
    TobramycinIncreased risk of nephrotoxicity
    TreprostinilAdditive hypotensive effect. Monitor antihypertensive therapy during concomitant use.
    TriamtereneIncreased risk of hyperkalemia
    Food Interactions
    • Captopril decreases the excretion of potassium. Salt substitutes containing potassium increase the risk of hyperkalemia.
    • Food decreases absorption by 25 - 40%. Clinical significance is debatable.
    • Herbs that may attenuate the antihypertensive effect of captopril include: bayberry, blue cohash, cayenne, ephedra, ginger, ginseng (American), kola and licorice.
    • High salt intake may attenuate the antihypertensive effect of captopril.

    1. Angiotensin-converting enzyme

    Kind: protein

    Organism: Human

    Pharmacological action: yes

    Actions: inhibitor

    Components

    Name UniProt ID Details
    Angiotensin-converting enzyme P12821 Details

    References:

    1. Andujar-Sanchez M, Jara-Perez V, Camara-Artigas A: Thermodynamic determination of the binding constants of angiotensin-converting enzyme inhibitors by a displacement method. FEBS Lett. 2007 Jul 24;581(18):3449-54. Epub 2007 Jun 27. Pubmed
    2. Dalkas GA, Marchand D, Galleyrand JC, Martinez J, Spyroulias GA, Cordopatis P, Cavelier F: Study of a lipophilic captopril analogue binding to angiotensin I converting enzyme. J Pept Sci. 2010 Feb;16(2):91-7. Pubmed
    3. Natesh R, Schwager SL, Evans HR, Sturrock ED, Acharya KR: Structural details on the binding of antihypertensive drugs captopril and enalaprilat to human testicular angiotensin I-converting enzyme. Biochemistry. 2004 Jul 13;43(27):8718-24. Pubmed
    4. Piepho RW: Overview of the angiotensin-converting-enzyme inhibitors. Am J Health Syst Pharm. 2000 Oct 1;57 Suppl 1:S3-7. Pubmed
    5. Song JC, White CM: Clinical pharmacokinetics and selective pharmacodynamics of new angiotensin converting enzyme inhibitors: an update. Clin Pharmacokinet. 2002;41(3):207-24. Pubmed
    6. Tzakos AG, Naqvi N, Comporozos K, Pierattelli R, Theodorou V, Husain A, Gerothanassis IP: The molecular basis for the selection of captopril cis and trans conformations by angiotensin I converting enzyme. Bioorg Med Chem Lett. 2006 Oct 1;16(19):5084-7. Epub 2006 Aug 2. Pubmed
    7. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. Pubmed

    2. 72 kDa type IV collagenase

    Kind: protein

    Organism: Human

    Pharmacological action: unknown

    Actions: inhibitor

    Components

    Name UniProt ID Details
    72 kDa type IV collagenase P08253 Details

    References:

    1. Brower GL, Levick SP, Janicki JS: Inhibition of matrix metalloproteinase activity by ACE inhibitors prevents left ventricular remodeling in a rat model of heart failure. Am J Physiol Heart Circ Physiol. 2007 Jun;292(6):H3057-64. Epub 2007 Feb 16. Pubmed
    2. Okada M, Kikuzuki R, Harada T, Hori Y, Yamawaki H, Hara Y: Captopril attenuates matrix metalloproteinase-2 and -9 in monocrotaline-induced right ventricular hypertrophy in rats. J Pharmacol Sci. 2008 Dec;108(4):487-94. Epub 2008 Dec 5. Pubmed
    3. Prontera C, Mariani B, Rossi C, Poggi A, Rotilio D: Inhibition of gelatinase A (MMP-2) by batimastat and captopril reduces tumor growth and lung metastases in mice bearing Lewis lung carcinoma. Int J Cancer. 1999 May 31;81(5):761-6. Pubmed
    4. Reinhardt D, Sigusch HH, Hensse J, Tyagi SC, Korfer R, Figulla HR: Cardiac remodelling in end stage heart failure: upregulation of matrix metalloproteinase (MMP) irrespective of the underlying disease, and evidence for a direct inhibitory effect of ACE inhibitors on MMP. Heart. 2002 Nov;88(5):525-30. Pubmed
    5. Williams RN, Parsons SL, Morris TM, Rowlands BJ, Watson SA: Inhibition of matrix metalloproteinase activity and growth of gastric adenocarcinoma cells by an angiotensin converting enzyme inhibitor in in vitro and murine models. Eur J Surg Oncol. 2005 Nov;31(9):1042-50. Epub 2005 Jul 1. Pubmed
    6. Yamamoto D, Takai S, Hirahara I, Kusano E: Captopril directly inhibits matrix metalloproteinase-2 activity in continuous ambulatory peritoneal dialysis therapy. Clin Chim Acta. 2010 May 2;411(9-10):762-4. Epub 2010 Feb 22. Pubmed

    3. Matrix metalloproteinase-9

    Kind: protein

    Organism: Human

    Pharmacological action: unknown

    Actions: inhibitor

    Components

    Name UniProt ID Details
    Matrix metalloproteinase-9 P14780 Details

    References:

    1. Okada M, Kikuzuki R, Harada T, Hori Y, Yamawaki H, Hara Y: Captopril attenuates matrix metalloproteinase-2 and -9 in monocrotaline-induced right ventricular hypertrophy in rats. J Pharmacol Sci. 2008 Dec;108(4):487-94. Epub 2008 Dec 5. Pubmed
    2. Reinhardt D, Sigusch HH, Hensse J, Tyagi SC, Korfer R, Figulla HR: Cardiac remodelling in end stage heart failure: upregulation of matrix metalloproteinase (MMP) irrespective of the underlying disease, and evidence for a direct inhibitory effect of ACE inhibitors on MMP. Heart. 2002 Nov;88(5):525-30. Pubmed
    3. Williams RN, Parsons SL, Morris TM, Rowlands BJ, Watson SA: Inhibition of matrix metalloproteinase activity and growth of gastric adenocarcinoma cells by an angiotensin converting enzyme inhibitor in in vitro and murine models. Eur J Surg Oncol. 2005 Nov;31(9):1042-50. Epub 2005 Jul 1. Pubmed
    4. Yamamoto D, Takai S, Miyazaki M: Inhibitory profiles of captopril on matrix metalloproteinase-9 activity. Eur J Pharmacol. 2008 Jul 7;588(2-3):277-9. Epub 2008 May 22. Pubmed

    1. Cytochrome P450 2D6

    Kind: protein

    Organism: Human

    Pharmacological action: unknown

    Actions: substrate

    Components

    Name UniProt ID Details
    Cytochrome P450 2D6 P10635 Details

    References:

    1. Preissner S, Kroll K, Dunkel M, Senger C, Goldsobel G, Kuzman D, Guenther S, Winnenburg R, Schroeder M, Preissner R: SuperCYP: a comprehensive database on Cytochrome P450 enzymes including a tool for analysis of CYP-drug interactions. Nucleic Acids Res. 2010 Jan;38(Database issue):D237-43. Epub 2009 Nov 24. Pubmed

    1. Serum albumin

    Kind: protein

    Organism: Human

    Pharmacological action: no

    Actions: other/unknown

    Components

    Name UniProt ID Details
    Serum albumin P02768 Details

    References:

    1. Keire DA, Mariappan SV, Peng J, Rabenstein DL: Nuclear magnetic resonance studies of the binding of captopril and penicillamine by serum albumin. Biochem Pharmacol. 1993 Sep 14;46(6):1059-69. Pubmed
    2. Lin SY, Wei YS, Li MJ, Wang SL: Effect of ethanol or/and captopril on the secondary structure of human serum albumin before and after protein binding. Eur J Pharm Biopharm. 2004 May;57(3):457-64. Pubmed
    3. Mariee AD, Al-Shabanah O: Protective ability and binding affinity of captopril towards serum albumin in an in vitro glycation model of diabetes mellitus. J Pharm Biomed Anal. 2006 May 3;41(2):571-5. Epub 2006 Feb 15. Pubmed
    4. Narazaki R, Harada K, Sugii A, Otagiri M: Kinetic analysis of the covalent binding of captopril to human serum albumin. J Pharm Sci. 1997 Feb;86(2):215-9. Pubmed

    1. Multidrug resistance protein 1

    Kind: protein

    Organism: Human

    Pharmacological action: unknown

    Actions: inhibitor

    Components

    Name UniProt ID Details
    Multidrug resistance protein 1 P08183 Details

    References:

    1. Takara K, Kakumoto M, Tanigawara Y, Funakoshi J, Sakaeda T, Okumura K: Interaction of digoxin with antihypertensive drugs via MDR1. Life Sci. 2002 Feb 15;70(13):1491-500. Pubmed

    2. Solute carrier family 15 member 1

    Kind: protein

    Organism: Human

    Pharmacological action: unknown

    Actions: inhibitor

    Components

    Name UniProt ID Details
    Solute carrier family 15 member 1 P46059 Details

    References:

    1. Watanabe K, Sawano T, Terada K, Endo T, Sakata M, Sato J: Studies on intestinal absorption of sulpiride (1): carrier-mediated uptake of sulpiride in the human intestinal cell line Caco-2. Biol Pharm Bull. 2002 Jul;25(7):885-90. Pubmed
    2. Temple CS, Boyd CA: Proton-coupled oligopeptide transport by rat renal cortical brush border membrane vesicles: a functional analysis using ACE inhibitors to determine the isoform of the transporter. Biochim Biophys Acta. 1998 Aug 14;1373(1):277-81. Pubmed

    3. Solute carrier family 22 member 6

    Kind: protein

    Organism: Human

    Pharmacological action: unknown

    Actions: inhibitor

    Components

    Name UniProt ID Details
    Solute carrier family 22 member 6 Q4U2R8 Details

    References:

    1. Kuze K, Graves P, Leahy A, Wilson P, Stuhlmann H, You G: Heterologous expression and functional characterization of a mouse renal organic anion transporter in mammalian cells. J Biol Chem. 1999 Jan 15;274(3):1519-24. Pubmed

    Comments
    Drug created on June 13, 2005 07:24 / Updated on September 16, 2013 17:13