The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Gaa  -  glucosidase, alpha, acid

Mus musculus

Synonyms: Acid maltase, E430018M07Rik, Lysosomal alpha-glucosidase
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Gaa


High impact information on Gaa

  • A mouse model of this disease was obtained by targeted disruption of the murine acid alpha-glucosidase gene (Gaa) in embryonic stem cells [4].
  • Furthermore, functional correction of the soleus skeletal muscle was also observed compared to age-matched untreated Gaa(-/-) control animals [2].
  • However, in skeletal muscle-a major organ affected in infantile and in milder, late-onset variants in humans-induction of GAA expression in young Gaa(-/-) mice to levels greatly exceeding wildtype values did not result in full phenotypic correction, and some muscle fibers showed little or no glycogen clearance [1].
  • Mice defective in the GAA gene encoding lysosomal alpha-glucosidase (acid maltase) overaccumulate glycogen in the lysosome but did not have elevated laforin [5].
  • Inheritance in recombinant inbred (RI) strains of restriction fragment length variants (RFLVs) detected by probes specific for Gaa and Tk-1 showed tight linkage of both to Es-3 on mouse Chromosome (Chr) 11 [6].

Associations of Gaa with chemical compounds

  • In freely fed mice the glycogen-hydrolysing activity (acid amyloglucosidase) was only 50% of the maltose-hydrolysing activity (acid maltase) [7].


  1. Glycogen stored in skeletal but not in cardiac muscle in acid alpha-glucosidase mutant (Pompe) mice is highly resistant to transgene-encoded human enzyme. Raben, N., Jatkar, T., Lee, A., Lu, N., Dwivedi, S., Nagaraju, K., Plotz, P.H. Mol. Ther. (2002) [Pubmed]
  2. Sustained correction of glycogen storage disease type II using adeno-associated virus serotype 1 vectors. Mah, C., Cresawn, K.O., Fraites, T.J., Pacak, C.A., Lewis, M.A., Zolotukhin, I., Byrne, B.J. Gene Ther. (2005) [Pubmed]
  3. Hyaluronidase increases the biodistribution of acid alpha-1,4 glucosidase in the muscle of Pompe disease mice: An approach to enhance the efficacy of enzyme replacement therapy. Matalon, R., Surendran, S., Campbell, G.A., Michals-Matalon, K., Tyring, S.K., Grady, J., Cheng, S., Kaye, E. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  4. Generalized glycogen storage and cardiomegaly in a knockout mouse model of Pompe disease. Bijvoet, A.G., van de Kamp, E.H., Kroos, M.A., Ding, J.H., Yang, B.Z., Visser, P., Bakker, C.E., Verbeet, M.P., Oostra, B.A., Reuser, A.J., van der Ploeg, A.T. Hum. Mol. Genet. (1998) [Pubmed]
  5. Relationship between glycogen accumulation and the laforin dual specificity phosphatase. Wang, W., Parker, G.E., Skurat, A.V., Raben, N., Depaoli-Roach, A.A., Roach, P.J. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  6. Linkage of acid alpha-glucosidase (Gaa) and thymidine kinase (Tk-1) to esterase-3 (Es-3) on mouse chromosome 11. Martiniuk, F., Hirschhorn, R., D'Eustachio, P. Mamm. Genome (1991) [Pubmed]
  7. Glycogen and glycogen-hydrolysing lysosomal enzyme activity in mouse liver: effects of fasting, adrenoceptor antagonism and insulin-induced hypoglycaemia. Skoglund, G., Ahrén, B., Rerup, C., Stenström, A., Lundquist, I. Acta Physiol. Scand. (1987) [Pubmed]
WikiGenes - Universities