Title
Clinical, biochemical and molecular findings in a patient with X-linked liver glycogenosis followed for 40 years Clinical, biochemical and molecular findings in a patient with X-linked liver glycogenosis followed for 40 years
Author
Faculty/Department
Faculty of Pharmaceutical, Biomedical and Veterinary Sciences. Pharmacy
Faculty of Medicine and Health Sciences
Publication type
article
Publication
Berlin ,
Subject
Human medicine
Source (journal)
European journal of pediatrics. - Berlin
Volume/pages
157(1998) :11 , p. 919-923
ISSN
0340-6199
ISI
000076919700010
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
Affiliation
University of Antwerp
Abstract
Phosphorylase kinase (PHK) is a regulatory enzyme in glycogen metabolism. Mutations in the gene encoding the alpha subunit of PHK (PHKA2) have been shown to be responsible for X-linked liver glycogenosis (XLG). XLG,a frequent type of glycogen storage disease, is characterised by hepatomegaly and growth retardation. Two subtypes of XLG have been described: XLG type I patients have a clear-cut PHK deficiency in liver and blood cells, whereas XLG type II patients have a normal or residual activity. Here, we present clinical, biochemical and molecular findings on a liver glycogenosis patient in whom the diagnosis XLG II only became clear after enzyme assays in the liver and identification of the disease-causing mutation. A missense mutation replacing arginine at amino acid position 186 by histidine (R186H) was identified in the PHKA2 gene. Mutations of the same arginine residue have been previously found in at least four other unrelated XLG II patients. Conclusion Arginine at position 186 of the alpha subunit seems to play an important role in the structure or the regulation of PHK. In patients with XLG having normal or residual PHK activity where XLG II is suspected, the identification of mutations in PHKA2 leads to the final classification.
E-info
https://repository.uantwerpen.be/docman/iruaauth/bdbf00/08e4260.pdf
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