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Mutational analysis of the AGL gene: Five novel mutations in GSD III patients
Author(s) -
Lucchiari S.,
Donati M.A.,
Melis D.,
Filocamo M.,
Parini R.,
Bresolin N.,
Comi G.P.
Publication year - 2003
Publication title -
human mutation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 162
eISSN - 1098-1004
pISSN - 1059-7794
DOI - 10.1002/humu.9177
Subject(s) - glycogen storage disease , biology , glycogen debranching enzyme , glycogen , genetics , gene , genotype , phenotype , genetic heterogeneity , mutation , glycogen synthase , biochemistry
Total or partial lack of glycogen debranching enzyme (GDE or AGL, amylo‐1,6‐glucosidase, 4‐α‐glucanotransferase) is responsible for Glycogen Storage Disease type III (GSDIII), a rare autosomal recessive disorder of glycogen metabolism. The clinical and biochemical features of GSDIII subjects are quite heterogeneous, and this mirrors the genotype‐phenotype heterogeneity among patients. In this paper, we report the molecular characterisation of five unrelated subjects, four Italian and one Tunisian. The following new mutations are described and confirm the genetic heterogeneity of this disease: p.R864X, p.R428K, c.3911 insA, p.G1087R and c.3512_3549dup+c.3512_3519del. The functional relevance of these mutations is discussed on the basis of the recently acquired knowledge about the boundaries and structures of the two catalytic domains. © 2003 Wiley‐Liss, Inc.