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Identification of two novel sequence variants affecting thiopurine methyltransferase enzyme activity
Linköping University, Department of Medicine and Care, Clinical Pharmacology. Linköping University, Faculty of Health Sciences.ORCID iD: 0000-0002-2809-7591
Linköping University, Department of Molecular and Clinical Medicine, Gastroenterology and Hepatology. Linköping University, Faculty of Health Sciences.
Linköping University, Faculty of Health Sciences. Linköping University, Department of Molecular and Clinical Medicine, Gastroenterology and Hepatology. Östergötlands Läns Landsting, Centre for Medicine, Department of Endocrinology and Gastroenterology UHL.
Linköping University, Faculty of Health Sciences. Linköping University, Department of Medicine and Care, Clinical Pharmacology. Östergötlands Läns Landsting, Centre for Laboratory Medicine, Department of Clinical Pharmacology.
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2004 (English)In: Pharmacogenetics, ISSN 0960-314X, E-ISSN 1473-561X, Vol. 14, no 4, 261-265 p.Article in journal (Refereed) Published
Abstract [en]

The polymorphic enzyme thiopurine methyltransferase (TPMT) is involved in the methylation of thiopurines. On comparing the phenotype with the genotype in Swedish patients with inflammatory bowel disease and healthy individuals, we found two discordant cases with low TPMT enzyme activity (0.3 and 0.4 U/ml packed red blood cells (pRBC). Genotyping by pyrosequencing revealed that they carried the nucleotide substitutions 460G>A and 719A>G, giving two possible genotypes (TPMT*1/*3A or TPMT*3B/ *3C). DNA sequencing of exon III to X was performed in the patients and their parents. We identified an A>G transition in the start codon (exon III, 1A>G, Met>Val, TPMT*14) in one of the patients and her father (6.3 U/ml pRBC). The mother in this family carried the 460G>A and 719A>G nucleotide substitutions (TPMT*3A, 5.0 U/ml pRBC). In the second family, sequencing revealed a G>A transition in the acceptor splice site in intron VII/exon VIII (IVS7 - 1G>A, TPMT*15) in the patient and his mother (6.9 U/ml pRBC). His father was genotyped as TPMT*1/*3A (6.0 U/ml pRBC). Hence, we report the identification of two novel sequence variants, present in highly conserved nucleotide positions of the human TPMT gene, resulting in a loss of enzyme activity.

Place, publisher, year, edition, pages
2004. Vol. 14, no 4, 261-265 p.
Keyword [en]
drug metabolizing enzyme, polymorphism, thiopurine methyltransferase
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Medical and Health Sciences
Identifiers
URN: urn:nbn:se:liu:diva-23408DOI: 10.1097/00008571-200404000-00006Local ID: 2855OAI: oai:DiVA.org:liu-23408DiVA: diva2:243722
Available from: 2009-10-07 Created: 2009-10-07 Last updated: 2017-12-13

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Lindqvist Appell, MalinHaglund, SofieAlmer, SvenPeterson, CurtSöderkvist, Peter

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Lindqvist Appell, MalinHaglund, SofieAlmer, SvenPeterson, CurtSöderkvist, Peter
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Clinical PharmacologyFaculty of Health SciencesGastroenterology and HepatologyDepartment of Endocrinology and Gastroenterology UHLDepartment of Clinical PharmacologyDivision of cell biology
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