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Minoru Okubo – One of the best experts on this subject based on the ideXlab platform.
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Egyptian glycogen storage disease type III – identification of six novel AGL mutations, including a large 1.5 kb deletion and a missense mutation p.L620P with subtype IIId
Clinical Chemistry and Laboratory Medicine, 2009Co-Authors: Yoriko Endo, Ekram Fateen, Mortada El Shabrawy, Yoshiko Aoyama, Tetsu Ebara, Toshio Murase, Teodor Podskarbi, Yoon S. Shin, Minoru OkuboAbstract:Background: Glycogen storage disease type III (GSD III) is caused by mutations in AGL which encodes for a single protein with two enzyme activities: oligo-1, 4-1, 4-glucantransferase (transferase) and Amylo–1, 6-glucosidase. Activity of both enzymes is lost in most patients with GSD III, but in the very rare subtype IIId, transferase activity is deficient. Since the spectrum of AGL mutations is dependent on the ethnic group, we investigated the clinical and molecular characteristics in Egyptian patients with GSD III. Methods: Clinical features were examined in five Egyptian patients. AGL was sequenced and AGL haplotypes were determined. Results: Six novel AGL mutations were identified: a large deletion (c.3481―3588+1417de11525 bp), two insertions (c.1389insG and c.2368insA), two small deletions (c.2223-2224delGT and c.4041deIT), and a missense mutation (p.L620P). p.L620P was found in a patient with IIId. Each mutation was located on a different AGL haplotype. Conclusions: Our results suggest that there is allelic and phenotypic heterogeneity of GSD III in Egypt. This is the second description of a large deletion in AGL. p.L620P is the second mutation found in GSD IIId.
Okubo Minoru – One of the best experts on this subject based on the ideXlab platform.
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Egyptian glycogen storage disease type III – identification of six novel AGL mutations, including a large 1.5 kb deletion and a missense mutation p.L620P with subtype IIId
'Walter de Gruyter GmbH', 2009Co-Authors: Endo Yoriko, Fateen Ekram, Aoyama Yoshiko, Ebara Tetsu, Murase Toshio, Podskarbi Teodor, Shin, Yoon S., Okubo MinoruAbstract:Background: Glycogen storage disease type III (GSD III) is caused by mutations in AGL which encodes for a single protein with two enzyme activities: oligo-1, 4-1, 4-glucantransferase (transferase) and Amylo–1, 6-glucosidase. Activity of both enzymes is lost in most patients with GSD III, but in the very rare subtype IIId, transferase activity is deficient. Since the spectrum of AGL mutations is dependent on the ethnic group, we investigated the clinical and molecular characteristics in Egyptian patients with GSD III. Methods: Clinical features were examined in five Egyptian patients. AGL was sequenced and AGL haplotypes were determined. Results: Six novel AGL mutations were identified: a large deletion (c.3481–3588+1417del1525 bp), two insertions (c.1389insG and c.2368insA), two small deletions (c.2223–2224delGT and c.4041delT), and a missense mutation (p.L620P). p.L620P was found in a patient with IIId. Each mutation was located on a different AGL haplotype. Conclusions: Our results suggest that there is allelic and phenotypic heterogeneity of GSD III in Egypt. This is the second description of a large deletion in AGL. p.L620P is the second mutation found in GSD IIId. Clin Chem Lab Med 2009;47:1233–8.Peer Reviewe
Yoriko Endo – One of the best experts on this subject based on the ideXlab platform.
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Egyptian glycogen storage disease type III – identification of six novel AGL mutations, including a large 1.5 kb deletion and a missense mutation p.L620P with subtype IIId
Clinical Chemistry and Laboratory Medicine, 2009Co-Authors: Yoriko Endo, Ekram Fateen, Mortada El Shabrawy, Yoshiko Aoyama, Tetsu Ebara, Toshio Murase, Teodor Podskarbi, Yoon S. Shin, Minoru OkuboAbstract:Background: Glycogen storage disease type III (GSD III) is caused by mutations in AGL which encodes for a single protein with two enzyme activities: oligo-1, 4-1, 4-glucantransferase (transferase) and Amylo–1, 6-glucosidase. Activity of both enzymes is lost in most patients with GSD III, but in the very rare subtype IIId, transferase activity is deficient. Since the spectrum of AGL mutations is dependent on the ethnic group, we investigated the clinical and molecular characteristics in Egyptian patients with GSD III. Methods: Clinical features were examined in five Egyptian patients. AGL was sequenced and AGL haplotypes were determined. Results: Six novel AGL mutations were identified: a large deletion (c.3481―3588+1417de11525 bp), two insertions (c.1389insG and c.2368insA), two small deletions (c.2223-2224delGT and c.4041deIT), and a missense mutation (p.L620P). p.L620P was found in a patient with IIId. Each mutation was located on a different AGL haplotype. Conclusions: Our results suggest that there is allelic and phenotypic heterogeneity of GSD III in Egypt. This is the second description of a large deletion in AGL. p.L620P is the second mutation found in GSD IIId.