ⓘ AOAH

                                     

ⓘ AOAH

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 lipopolysaccharides LPSs, also called endotoxins. This action inactivates LPSs that are sensed by MD-2--Toll-like Receptor 4 TLR 4 on animal cells and probably also by the cytosolic caspase-based sensors. The enzymes 2 disulfide-linked subunits are encoded by a single mRNA. The smaller subunit is a member of the saposin-like SAPLIP protein family and the larger subunit, which contains the active site serine, is a GDSL lipase.

AOAH is produced by neutrophils, macrophages and microglia, including the Copperhouse cells, dendritic cells, NK cells and proximal renal tubular cells. The absence of the enzyme in genetically modified mice was associated with characteristic phenotypes. AOAH-deficient animals do not inactivate even small amounts of LPS in most tissues, it remains biologically active and can move from cell to cell in vivo for many weeks. LPS-exposed mice develop a strikingly high titers of antibodies, polyclonal, prolonged hepatomegaly and innate immune "tolerance" that gives them the slow and inadequate response to bacterial problems. In contrast, the absence of the enzyme makes mice more susceptible to severe lung damage and die if they face intratracheally with LPS or gram-negative bacteria.

AOAH has been highly conserved during evolution, the amino acid sequence of the human enzyme is almost 50% identical to the AOAH found in It is, with 100% identity in the GDSL lipase consensus sequences. The enzyme has been found in many invertebrates and all vertebrates studied to date, except for the fish. Although it is likely that the enzyme and the substrates under natural conditions other than LPS may be phospholipase A1 / B and acyl transferase in vitro, none has been identified.

Polymorphism in the gene was associated with chronic rhinosinusitis in 2 different ethnic groups. Other studies have shown that AOAH mRNA abundance is associated with НLА-Dr alleles, which in turn were closely associated with colitis.

                                     
  • surfactant, playing a role in rearranging lipids. However, proteins like GNLY and AOAH do not carry a SapA domain. While GNLY is essentially a SapB with N - terminal
  • the active site serine and the other elements of the His - Asp - Ser triad AOAH is a GDSL lipase that has activity toward certain glycerolipids in addition
  • by the following genes on chromosome 7: EEPD1 MARK2P7 ANLN LOC111365168 AOAH The gene encoded for the KIAA0895 protein is 65, 975 nucleotides long, from
  • hydrolase AOAH that inactivates LPS by removing the two secondary acyl chains from lipid A. If they are given LPS parenterally, mice that lack AOAH develop
  • and cardoon. This is similar to the function of the SapB domain in human AOAH Like other members of the SAPLIP family, the PSI confers antimicrobial activity
  • HGNC: 534 Q9UJ72 783 ANXA11 HGNC: 535 P50995 784 ANXA13 HGNC: 536 P27216 785 AOAH HGNC: 548 P28039 786 AOC1 HGNC: 80 P19801 787 AOC2 HGNC: 549 O75106 788 AOC3