ArticleThe protein journal2004
Aryl acylamidase activity on acetylcholinesterase is high during early chicken brain development.
Article in The protein journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 28 citations in OpenAlex.
- Erythrocyte acetylcholinesterase as biomarker of pesticide exposure: new and forgotten insights.Environmental science and pollution research international · 2018Review
- The significance of aryl acylamidase activity of acetylcholinesterase in osteoblast differentiation and mineralization.Molecular and cellular biochemistry · 2018Article
- Acetylcholinesterase Regulates Skeletal In Ovo Development of Chicken Limbs by ACh-Dependent and -Independent Mechanisms.PloS one · 2016Article
- Cloning of a novel arylamidase gene from Paracoccus sp. strain FLN-7 that hydrolyzes amide pesticides.Applied and environmental microbiology · 2012Article
- N-acetylanthranilate amidase from Arthrobacter nitroguajacolicus Rü61a, an alpha/beta-hydrolase-fold protein active towards aryl-acylamides and -esters, and properties of its cysteine-deficient variant.Journal of bacteriology · 2006Article
- Differential localization of acetylcholinesterase in neuronal and non-neuronal cells.Journal of cellular biochemistry · 2005Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) are known to exhibit aryl acylamidase activities (here called AAA(AChe) and AAA(BChe), respectively), which have been suggested to be involved in developmental and pathological processes. We here have investigated the developmental profiles of both AAA(AChe) and AAA(BChe) activities along with their AChE and BChE activities from embryonic days E3 to hatching (E21) in Triton-extracted homogenates from chicken embryonic brains. AAA(AChe) follows continuously an increase that is typical for AChE expression itself, whereas AAA(BChe) was relatively high before E10 to then become negligible toward hatching. Sucrose gradient centrifugation of both homogenized and immunopurified samples from E6-E18 brains showed that all globular forms (G1, G2, G4) of AChE present AAA(AChe) activity. Interestingly, the ratio of AAA(AChe) to AChE is highest at E6, and here again higher on G1/G2- over the G4-form. Noticeably, the sensitivity of AAA(AChe) toward the specific AChE inhibitor BW284c51 at all stages is higher than that of AChE itself. These data of high ratios of AAA associated at young stages with cholinesterases strongly indicate a role of AAA in early brain development.
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