AOAH

From Wikipedia, the free encyclopedia

Acyloxyacyl hydrolase (neutrophil)

Identifiers

External IDs

OMIM: 102593 MGI: 1350928 HomoloGene: 1238

Gene ontology
Molecular Function:	• lipoprotein lipase activity • hydrolase activity, acting on ester bonds • acyloxyacyl hydrolase activity
Biological Process:	• lipid metabolic process • inflammatory response • lipopolysaccharide metabolic process • negative regulation of inflammatory response

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001637 (mRNA)
NP_001628 (protein)

NM_012054 (mRNA)
NP_036184 (protein)

Location

Chr 7: 36.52 - 36.73 Mb

Chr 13: 20.8 - 21.03 Mb

Pubmed search

[1]

[2]

Acyloxyacyl hydrolase (neutrophil), also known as AOAH, is a human gene.^[1]

Acyloxyacyl hydrolase (AOAH) is a 2-subunit lipase which selectively hydrolyzes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial endotoxins. AOAH may modulate host inflammatory responses to gram-negative bacterial invasion. The 2 subunits are encoded by a single mRNA.^[1]

[edit] References

^ ^a ^b Entrez Gene: AOAH acyloxyacyl hydrolase (neutrophil).

[edit] Further reading

Hagen FS, Grant FJ, Kuijper JL, et al. (1991). "Expression and characterization of recombinant human acyloxyacyl hydrolase, a leukocyte enzyme that deacylates bacterial lipopolysaccharides.". Biochemistry 30 (34): 8415-23. PMID 1883828.
McDermott CM, Cullor JS, Fenwick BW (1991). "Intracellular and extracellular enzymatic deacylation of bacterial endotoxin during localized inflammation induced by Escherichia coli.". Infect. Immun. 59 (2): 478-85. PMID 1987068.
Whitmore TE, Mathewes SL, O'Hara PJ, Durnam DM (1994). "Chromosomal localization of the acyloxyacyl hydrolase (AOAH) gene to 7p14-p12 using fluorescence in situ hybridization.". Genomics 21 (2): 457-8. doi:10.1006/geno.1994.1298. PMID 8088847.
Staab JF, Ginkel DL, Rosenberg GB, Munford RS (1994). "A saposin-like domain influences the intracellular localization, stability, and catalytic activity of human acyloxyacyl hydrolase.". J. Biol. Chem. 269 (38): 23736-42. PMID 8089145.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171-4. PMID 8125298.
Coulthard MG, Swindle J, Munford RS, et al. (1996). "Adenovirus-mediated transfer of a gene encoding acyloxyacyl hydrolase (AOAH) into mice increases tissue and plasma AOAH activity.". Infect. Immun. 64 (5): 1510-5. PMID 8613354.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149-56. PMID 9373149.
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. PMID 12477932.
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. PMID 15489334.