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) [1] Band 17q25.3 Start 80,101,556 bp [1] End 80,119,881 bp [1]
Gene location (Mouse) Chr. Chromosome 11 (mouse) [2] Band 11 E2|11 83.35 cM Start 119,158,713 bp [2] End 119,176,280 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) 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 BioGPS 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 Species Human Mouse Entrez 2548 14387 Ensembl ENSG00000171298 ENSMUSG00000025579 UniProt P10253 P70699 RefSeq (mRNA) NM_000152 NM_001079803 NM_001079804 NM_001159324 NM_008064 RefSeq (protein) NP_000143 NP_001073271 NP_001073272 NP_001152796 NP_032090 Location (UCSC) Chr 17: 80.1 – 80.12 Mb Chr 11: 119.16 – 119.18 Mb PubMed search [3] [4]
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

1. GRCh38: Ensembl release 89: ENSG00000171298 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000025579 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: GAA glucosidase, alpha; acid (Pompe disease, glycogen storage disease type II)".
6. 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.

Further reading

• Feizi T, Larkin M (September 1990). "AIDS and glycosylation". Glycobiology. 1 (1): 17–23. doi:10.1093/glycob/1.1.17. PMID   2136376.
• 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.
• Land A, Braakman I (August 2001). "Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum". Biochimie. 83 (8): 783–90. doi:10.1016/S0300-9084(01)01314-1. hdl: 1874/5091 . PMID   11530211. S2CID   13576808.
• 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.
• Ratner L, vander Heyden N, Dedera D (March 1991). "Inhibition of HIV and SIV infectivity by blockade of alpha-glucosidase activity". Virology. 181 (1): 180–92. doi:10.1016/0042-6822(91)90483-R. PMID   1704656.
• Dedera DA, Gu RL, Ratner L (March 1992). "Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function". Virology. 187 (1): 377–82. doi:10.1016/0042-6822(92)90331-I. PMID   1736542.
• 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.
• Leonard CK, Spellman MW, Riddle L, Harris RJ, Thomas JN, Gregory TJ (June 1990). "Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells". The Journal of Biological Chemistry. 265 (18): 10373–82. doi: 10.1016/S0021-9258(18)86956-3 . PMID   2355006.
• Pal R, Hoke GM, Sarngadharan MG (May 1989). "Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1". Proceedings of the National Academy of Sciences of the United States of America. 86 (9): 3384–8. Bibcode:1989PNAS...86.3384P. doi: 10.1073/pnas.86.9.3384 . PMC   287137 . PMID   2541446.
• 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.

External links

• GeneReview/NIH/UW entry on Glycogen Storage Disease Type II (Pompe Disease)
• Human GAA genome location and GAA gene details page in the UCSC Genome Browser .