S. KeeratichamroenJ. R Ketudat CairnsD. WattanasirichaigoonP. WasantL. NgiwsaraP. SuwannaratS. PangkanonJ. KuptanonP. TanpaiboonT. RujirawatS. LiammongkolkulJ. SvastiChulabhorn Research InstituteSuranaree University of TechnologyMahidol UniversityQueen Sirikit National Institute of Child HealthChiang Mai University2018-07-122018-07-122008-01-01Journal of Inherited Metabolic Disease. Vol.31, No.SUPPL. 2 (2008)15732665014189552-s2.0-84855585793https://repository.li.mahidol.ac.th/handle/123456789/19012Molecular defects in the gene encoding the enzyme iduronate-2-sulfatase (IDS) result in Hunter disease (mucopolysaccharidosis type II, MPS II). To determine the molecular basis of MPS II in Thailand, the IDS gene was analysed in 20 Thai patients with Hunter syndrome from 18 unrelated families. A total of 19 different mutations, including 9 missense mutations, 3 nonsense mutations, 3 splice site alterations, 1 deletion, 2 indels, and 1 rearrangement were identified, 8 of which were novel (p.R101C, p.D148V, p.G224A, p.K227E, p.E254X, p.W337X, c.440-442delinsTT and c.720-731delinsTTTCAGATGTTCTCCCCAG). Evaluation of the IDS activity of two hemizygous variants identified in the same patient, p.R101C and p.R468Q, by expression of IDS with the individual mutations in COS 7 cells indicated that only the p.R468Q mutation affected IDS protein activity. Two exonic mutations, c.257C>T (p.P86L) and c.418G>A, were found to activate multiple cryptic splice sites, resulting in aberrantly spliced transcripts. Thus, MPS II in Thailand is caused by a diverse set of defects affecting both IDS protein production and activity. © SSIEM and Springer 2008.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyMedicineArticleSCOPUS10.1007/s10545-008-0876-z