Acid alpha-glucosidase

GAA
Identifiers
Aliases	GAA, LYAG, glucosidase alpha, acid, alpha glucosidase
External IDs	OMIM: 606800; MGI: 95609; HomoloGene: 37268; GeneCards: GAA; OMA:GAA - orthologs
Gene location (Human)
Chr.	Chromosome 17 (human)
End	80,119,881 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	119,176,280 bp
RNA expression pattern
	Top expressed in
	granulocyte; ; left testis; ; right testis; ; right uterine tube; ; monocyte; ; anterior pituitary; ; right lung; ; spleen; ; upper lobe of left lung; ; apex of heart;
	Top expressed in
	arcuate nucleus; ; paraventricular nucleus of hypothalamus; ; median eminence; ; dorsomedial hypothalamic nucleus; ; choroid plexus of fourth ventricle; ; ventromedial nucleus; ; suprachiasmatic nucleus; ; supraoptic nucleus; ; entorhinal cortex; ; central gray substance of midbrain;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	hydrolase activity, hydrolyzing O-glycosyl compounds; hydrolase activity, acting on glycosyl bonds; maltose alpha-glucosidase activity; catalytic activity; hydrolase activity; carbohydrate binding; oligo-1,6-glucosidase activity; alpha-1,4-glucosidase activity; alpha-glucosidase activity;
Cellular component	membrane; lysosomal membrane; lysosomal lumen; lysosome; extracellular exosome; plasma membrane; azurophil granule membrane; tertiary granule membrane; ficolin-1-rich granule membrane; integral component of membrane;
Biological process	vacuolar sequestering; cardiac muscle contraction; muscle cell cellular homeostasis; neuromuscular process controlling posture; locomotory behavior; neuromuscular process controlling balance; regulation of the force of heart contraction; diaphragm contraction; heart morphogenesis; maltose metabolic process; glycogen catabolic process; sucrose metabolic process; tissue development; glycogen metabolic process; metabolism; lysosome organization; striated muscle contraction; glucose metabolic process; neutrophil degranulation; carbohydrate metabolic process;
	Sources:Amigo / QuickGO
Orthologs
	2548
	14387
	ENSG00000171298
	ENSMUSG00000025579
	P10253
	P70699
	NM_000152; NM_001079803; NM_001079804
	NM_001159324; NM_008064
	NP_000143; NP_001073271; NP_001073272
	NP_001152796; NP_032090
	Wikidata
View/Edit Human	View/Edit Mouse

Acid alpha-glucosidase, also called acid maltase,^[5] is an enzyme that helps to break down glycogen in the lysosome. It is functionally similar to glycogen debranching enzyme, but is on a different chromosome, processed differently by the cell and is located in the lysosome rather than the cytosol.^[6] In humans, it is encoded by the GAA gene.^[5] Errors in this gene cause glycogen storage disease type II (Pompe disease).

Function

This gene encodes lysosomal alpha-glucosidase, which is essential for the degradation of glycogen to glucose in lysosomes. Different forms of acid alpha-glucosidase are obtained by proteolytic processing. Defects in this gene are the cause of glycogen storage disease II, also known as Pompe disease, which is an autosomal recessive disorder with a broad clinical spectrum. Three transcript variants encoding the same protein have been found for this gene.^[5]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000171298 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000025579 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b ^c "Entrez Gene: GAA glucosidase, alpha; acid (Pompe disease, glycogen storage disease type II)".
^ Adeva-Andany MM, González-Lucán M, Donapetry-García C, Fernández-Fernández C, Ameneiros-Rodríguez E (June 2016). "Glycogen metabolism in humans". BBA Clinical. 5: 85–100. doi:10.1016/j.bbacli.2016.02.001. PMC 4802397. PMID 27051594.

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Reuser AJ, Kroos MA, Hermans MM, Bijvoet AG, Verbeet MP, Van Diggelen OP, Kleijer WJ, Van der Ploeg AT (1995). "Glycogenosis type II (acid maltase deficiency)". Muscle & Nerve. Supplement. 3: S61-9. doi:10.1002/mus.880181414. hdl:1765/66923. PMID 7603530. S2CID 44030591.
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Zhong N, Martiniuk F, Tzall S, Hirschhorn R (September 1991). "Identification of a missense mutation in one allele of a patient with Pompe disease, and use of endonuclease digestion of PCR-amplified RNA to demonstrate lack of mRNA expression from the second allele". American Journal of Human Genetics. 49 (3): 635–45. PMC 1683123. PMID 1652892.
Fenouillet E, Gluckman JC (August 1991). "Effect of a glucosidase inhibitor on the bioactivity and immunoreactivity of human immunodeficiency virus type 1 envelope glycoprotein". The Journal of General Virology. 72 (8): 1919–26. doi:10.1099/0022-1317-72-8-1919. PMID 1678778.
Martiniuk F, Mehler M, Bodkin M, Tzall S, Hirschhorn K, Zhong N, Hirschhorn R (November 1991). "Identification of a missense mutation in an adult-onset patient with glycogenosis type II expressing only one allele". DNA and Cell Biology. 10 (9): 681–7. doi:10.1089/dna.1991.10.681. PMID 1684505.
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Hermans MM, Kroos MA, van Beeumen J, Oostra BA, Reuser AJ (July 1991). "Human lysosomal alpha-glucosidase. Characterization of the catalytic site". The Journal of Biological Chemistry. 266 (21): 13507–12. doi:10.1016/S0021-9258(18)92727-4. PMID 1856189.
Hermans MM, de Graaff E, Kroos MA, Wisselaar HA, Oostra BA, Reuser AJ (September 1991). "Identification of a point mutation in the human lysosomal alpha-glucosidase gene causing infantile glycogenosis type II". Biochemical and Biophysical Research Communications. 179 (2): 919–26. doi:10.1016/0006-291X(91)91906-S. PMID 1898413.
Murphy CI, Lennick M, Lehar SM, Beltz GA, Young E (October 1990). "Temporal expression of HIV-1 envelope proteins in baculovirus-infected insect cells: implications for glycosylation and CD4 binding". Genetic Analysis, Techniques and Applications. 7 (6): 160–71. doi:10.1016/0735-0651(90)90030-J. PMID 2076345.
Martiniuk F, Mehler M, Tzall S, Meredith G, Hirschhorn R (March 1990). "Sequence of the cDNA and 5'-flanking region for human acid alpha-glucosidase, detection of an intron in the 5' untranslated leader sequence, definition of 18-bp polymorphisms, and differences with previous cDNA and amino acid sequences". DNA and Cell Biology. 9 (2): 85–94. doi:10.1089/dna.1990.9.85. PMID 2111708.
Kalyanaraman VS, Rodriguez V, Veronese F, Rahman R, Lusso P, DeVico AL, Copeland T, Oroszlan S, Gallo RC, Sarngadharan MG (March 1990). "Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1". AIDS Research and Human Retroviruses. 6 (3): 371–80. doi:10.1089/aid.1990.6.371. PMID 2187500.
Martiniuk F, Bodkin M, Tzall S, Hirschhorn R (September 1990). "Identification of the base-pair substitution responsible for a human acid alpha glucosidase allele with lower "affinity" for glycogen (GAA 2) and transient gene expression in deficient cells". American Journal of Human Genetics. 47 (3): 440–5. PMC 1683879. PMID 2203258.
Hoefsloot LH, Hoogeveen-Westerveld M, Reuser AJ, Oostra BA (December 1990). "Characterization of the human lysosomal alpha-glucosidase gene". The Biochemical Journal. 272 (2): 493–7. doi:10.1042/bj2720493. PMC 1149727. PMID 2268276.
Shimizu H, Tsuchie H, Honma H, Yoshida K, Tsuruoka T, Ushijima H, Kitamura T (June 1990). "Effect of N-(3-phenyl-2-propenyl)-1-deoxynojirimycin on the lectin binding to HIV-1 glycoproteins". Japanese Journal of Medical Science & Biology. 43 (3): 75–87. doi:10.7883/yoken1952.43.75. PMID 2283726.
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Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP (June 1989). "Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport". Journal of Virology. 63 (6): 2452–6. doi:10.1128/jvi.63.6.2452-2456.1989. PMC 250699. PMID 2542563.