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Pathway Description
Pantoprazole Metabolism Pathway
Homo sapiens
Category:
Metabolite Pathway
Sub-Category:
Drug Metabolism
Created: 2013-09-11
Last Updated: 2019-09-12
Pantoprazole is a proton pump inhibitor (PPI) class drug that suppresses the final step in gastric acid production. In this pathway, pantoprazole is oxidized in the stomach to form the active metabolite of pantoprazole. This active metabolite then binds covalently to the potassium-transporting ATPase protein subunits, found at the secretory surface of the gastric parietal cell, preventing any stimulus. Because the drug binds covalently, its effects are dose-dependent and last much longer than similar drugs that bind to the protein non-covalently. This is because additional ATPase enzymes must be created to replace the ones covalently bound by pantoprazole.
Pantoprazole is used to manage gastroesophageal reflux disease, to prevent stomach ulcers, and can be used to help treat the effects of a H. pylori infection.
References
Pantoprazole Pathway References
DiPiro, J.T., Talbert, R.L., Yee, G.C., Matzke, G.R., Wells, B.G, & Posey, M.L. Pharmacotherapy: A pathologic approach. (6th ed) (2005) p.621-623. New York: McGraw-Hill Medical Publishing Division.
Horn J: The proton-pump inhibitors: similarities and differences. Clin Ther. 2000 Mar;22(3):266-80; discussion 265. doi: 10.1016/S0149-2918(00)80032-6.
Pubmed: 10963283
Pantoloc. (2009). e-CPS (online version of Compendium of Pharmaceuticals and Specialties). Retrieved July 1, 2009.
Ma JY, Song YH, Sjostrand SE, Rask L, Mardh S: cDNA cloning of the beta-subunit of the human gastric H,K-ATPase. Biochem Biophys Res Commun. 1991 Oct 15;180(1):39-45. doi: 10.1016/s0006-291x(05)81251-3.
Pubmed: 1656976
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Pubmed: 15057823
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. doi: 10.1101/gr.2596504.
Pubmed: 15489334
Maeda M, Oshiman K, Tamura S, Futai M: Human gastric (H+ + K+)-ATPase gene. Similarity to (Na+ + K+)-ATPase genes in exon/intron organization but difference in control region. J Biol Chem. 1990 Jun 5;265(16):9027-32.
Pubmed: 2160952
Newman PR, Greeb J, Keeton TP, Reyes AA, Shull GE: Structure of the human gastric H,K-ATPase gene and comparison of the 5'-flanking sequences of the human and rat genes. DNA Cell Biol. 1990 Dec;9(10):749-62. doi: 10.1089/dna.1990.9.749.
Pubmed: 2176086
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Pubmed: 15057824
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