Home LiteratureArticle Details
PMID: 17573812 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Adult-onset glycogen storage disease type 2: clinico-pathological phenotype revisited.

Neuropathology and applied neurobiology ·Vol. 33 ·No. 5 ·2007-10-00 ·Pages 544-59

Schoser BG, Müller-Höcker J, Horvath R, Gempel K, Pongratz D, Lochmüller H, Müller-Felber W

Abstract

The need for clinical awareness and diagnostic precision of glycogen storage disease type 2 (GSD2) has increased, as enzyme replacement therapy has become available. So far, only small series have reported the muscle pathology of late-onset GSD2. We reassessed 43 muscle biopsies of 38 GSD2 patients. In all patients the diagnosis of GSD2 has been established by biochemistry and/or mutational analysis of the GAA gene. Additionally to the expected morphological features, ultrastructural analysis revealed a high incidence of autophagic vacuoles, lipofuscin debris, structural Z-line disorganization and histological neurogenic-like pattern that were not thoroughly appreciated, previously. Comparing age at onset and morphology, excessive vacuolar and autophagic myopathy and mitochondrial disorganization of virtually all fibres is common in infants. At juvenile onset, a more moderate vacuolization without significant differences in overall morphology is notable. At late-onset, the spectrum of vacuolar myopathy is more divergent, ranging from almost normal to severe. Here pronounced secondary alterations are observed that include lipofuscin debris, autophagic vacuoles with residual lysosomal bodies and granular inclusions, structural mitochondrial and Z-line texture alterations. Moreover, there is a high incidence of subtle neurogenic-like alteration in all subtypes. Nineteen patients were genetically tested; in 15 patients the common leaky splicing mutation c.-45T>G (or IVS1-13T>G) in intron1 of the GAA gene was found on at least one allele, facilitating genetic screening. In our patients, GAA genotype appears not to be associated with secondary alterations such as autophagic vacuoles, structural alterations or neurogenic-like changes. These findings may have implications for our understanding of the pathogenesis of GSD2 and for assessing therapeutic success of enzyme replacement therapy.

MeSH Terms
Adolescent Adult Age Factors Age of Onset Aged Biopsy Child Child, Preschool DNA Mutational Analysis Female Genotype Glycogen Storage Disease Type II/genetics,metabolism,pathology Humans Immunohistochemistry Infant Male Microscopy, Electron, Transmission Middle Aged Muscle, Skeletal/metabolism,ultrastructure Mutation Phenotype alpha-Glucosidases/genetics
Chemicals
GAA protein, human alpha-Glucosidases
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Schoser B G H
Friedrich-Baur-Institute, Department of Neurology, Ludwig-Maximilians-University, Munich, Germany. bschoser@med.uni-muenchen.de
Müller-Höcker J
Horvath R
Gempel K
Pongratz D
Lochmüller H
Müller-Felber W
Article Info
Journal
Neuropathology and applied neurobiology
Abbr.
Neuropathol Appl Neurobiol
ISSN
0305-1846
Published
2007-10-00
Epub
2007-00-15
Pages
544-59
Language
English
Region
England
NLM ID
7609829
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com