
Health Dictionary
Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.
ASAHL
Introduction
N-acylethanolamine-hydrolyzing acid amidase is an enzyme that in humans is encoded by the NAAA gene.[1][2][3]
This gene encodes an N-acylethanolamine–hydrolyzing enzyme which is highly similar to acid ceramidase. Multiple transcript variants encoding different isoforms have been found for this gene.[3]
References
References
- ↑ Hong SB, Li CM, Rhee HJ, Park JH, He X, Levy B, Yoo OJ, Schuchman EH (Feb 2000). “Molecular cloning and characterization of a human cDNA and gene encoding a novel acid ceramidase-like protein”. Genomics. 62 (2): 232–41. doi:10.1006/geno.1999.5953. PMID 10610717.
- ↑ Goodchild NL, Wilkinson DA, Mager DL (Dec 1992). “A human endogenous long terminal repeat provides a polyadenylation signal to a novel, alternatively spliced transcript in normal placenta”. Gene. 121 (2): 287–94. doi:10.1016/0378-1119(92)90133-A. PMID 1446826.
- ↑ 3.0 3.1 “Entrez Gene: ASAHL N-acylsphingosine amidohydrolase (acid ceramidase)-like”.
External links
External links
- Human NAAA genome location and NAAA gene details page in the UCSC Genome Browser.
Further reading
Further reading
- Schulze H, Schepers U, Sandhoff K (2008). “Overexpression and mass spectrometry analysis of mature human acid ceramidase”. Biol. Chem. 388 (12): 1333–43. doi:10.1515/BC.2007.152. PMID 18020949.
- Zhao LY, Tsuboi K, Okamoto Y, et al. (2008). “Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism”. Biochim. Biophys. Acta. 1771 (11): 1397–405. doi:10.1016/j.bbalip.2007.10.002. PMID 17980170.
- Oh JH, Yang JO, Hahn Y, et al. (2006). “Transcriptome analysis of human gastric cancer”. Mamm. Genome. 16 (12): 942–54. doi:10.1007/s00335-005-0075-2. PMID 16341674.
- Tsuboi K, Sun YX, Okamoto Y, et al. (2005). “Molecular characterization of N-acylethanolamine-hydrolyzing acid amidase, a novel member of the choloylglycine hydrolase family with structural and functional similarity to acid ceramidase”. J. Biol. Chem. 280 (12): 11082–92. doi:10.1074/jbc.M413473200. PMID 15655246.
- Huang Y, Tanimukai H, Liu F, et al. (2005). “Elevation of the level and activity of acid ceramidase in Alzheimer’s disease brain”. Eur. J. Neurosci. 20 (12): 3489–97. doi:10.1111/j.1460-9568.2004.03852.x. PMID 15610181.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)”. Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Bonaldo MF, Lennon G, Soares MB (1997). “Normalization and subtraction: two approaches to facilitate gene discovery”. Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
