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Clinical Pharmacogenomics of Thiopurine S-methyltransferase

Current Clinical Pharmacology, 2006
Thiopurine methyltransferase (TPMT) catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine (6-MP), thioguanine and azathioprine (AZA). These drugs are used to treat conditions such as acute lymphoblastic leukemia, inflammatory bowel disease, rheumatoid arthritis, and organ transplant rejection. This review highlights the polymorphisms
Zhou, Shufeng, Brink
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The Clinical Impact of Thiopurine Methyltransferase Polymorphisms on Thiopurine Treatment

Nucleosides, Nucleotides and Nucleic Acids, 2004
Acute lymphoblastic leukaemia (ALL) is the most common malignancy of childhood. Although current treatment results in long term survival in over 70% of cases there is evidence that as many as 50% could have been cured using a less complex regimen with a lower incidence of long term side effects.
S A, Coulthard   +3 more
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The Effect of Thiopurine Methyltransferase Expression on Sensitivity to Thiopurine Drugs

Molecular Pharmacology, 2002
Although the thiopurine drugs 6-mercaptopurine (6-MP) and 6-thioguanine (6-TG) are well established agents for the treatment of leukemia, controversies remain regarding their main mode of action. Previous evidence has suggested that although 6-TG exerts a cytotoxic effect through incorporation of 6-thioguanine nucleotides into newly synthesized DNA ...
Coulthard   +13 more
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Individualization of Thiopurine Therapy: Thiopurine S -Methyltransferase and Beyond

Pharmacogenomics, 2009
The metabolism of a given drug depends, not solely on a particular enzyme, but rather on a complex metabolic network. Thiopurine S-methyltransferase (TPMT) catalyzes the methylation, and thus deactivation, of 6-mercaptopurine, a thiopurine used in the treatment of acute lymphoblastic leukemia.
Natasa, Karas-Kuzelicki   +1 more
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Pharmacogenetics of Thiopurine S-Methyltransferase and Thiopurine Therapy

Therapeutic Drug Monitoring, 2004
Most medications exhibit wide interpatient variability in their efficacy and toxicity. For many medications, these interindividual differences result in part from polymorphisms in genes encoding drug-metabolizing enzymes, drug transporters, and/or drug targets (eg, receptors, enzymes).
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Thiopurine S-methyltransferase as a target for drug interactions

European Journal of Clinical Pharmacology, 2005
The present study was undertaken to investigate the possible effects of various agents on thiopurine methyltransferase (TPMT) activity in red blood cells (RBCs) from patients with chronic inflammatory bowel disease (IBD).In three groups of patients with very high, normal and intermediate TPMT activity (each n=6), the inhibitory potential of furosemide,
Hua-Wen, Xin   +3 more
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Purine substrates for human thiopurine methyltransferase

Biochemical Pharmacology, 1994
Thiopurine methyltransferase (TPMT) catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine (6-MP) and 6-thioguanine (6-TG). A genetic polymorphism regulating TPMT activity in human tissue is an important factor responsible for individual differences in the toxicity and therapeutic efficacy of these drugs.
M, Deininger   +5 more
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Thiopurine S-methyltransferase activity in a Chinese population

Clinical Pharmacology and Therapeutics, 1993
Thiopurine S-methyltransferase is a cytosolic enzyme that catalyzes the S-methylation of thiopurine drugs. Although a genetic polymorphism has been recognized for this enzyme in populations of Caucasian descent, there has been scanty information about this polymorphism among Asians.
Lee, E.J.D., Kalow, W.
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