A tryptophan amphiphilic tetramerization domain-containing acetylcholinesterase from the bovine lungworm,Dictyocaulus viviparus
| Autor: | Amanda J. Davidson, Murray E. Selkirk, Jacqueline B. Matthews, S. Warren, O. Lazari |
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| Rok vydání: | 2006 |
| Předmět: |
DNA
Complementary Time Factors Molecular Sequence Data Gene Expression Neurotransmission Polymerase Chain Reaction Electron Transport Complex IV chemistry.chemical_compound Complementary DNA medicine Animals Amino Acid Sequence Gene Phylogeny Caenorhabditis elegans DNA Primers chemistry.chemical_classification biology Gene Expression Profiling Tryptophan Helminth Proteins DNA Helminth biology.organism_classification Acetylcholinesterase Dictyocaulus Infectious Diseases Nematode Enzyme chemistry Biochemistry Larva Cattle Animal Science and Zoology Parasitology Sequence Alignment Acetylcholine medicine.drug |
| Zdroj: | Parasitology. 133:381-387 |
| ISSN: | 1469-8161 0031-1820 |
| DOI: | 10.1017/s0031182006000345 |
| Popis: | Acetylcholine (ACh) is one of an array of neurotransmitters used by invertebrates and, analogous to vertebrate nervous systems, acetylcholinesterase (AChE) regulates synaptic levels of this transmitter. Similar to other invertebrates, nematodes possess several AChE genes. This is in contrast to vertebrates, which have a single AChE gene, transcripts of which are alternatively spliced to produce different types of the enzyme which vary at their C-termini. Parasitic nematodes have a repertoire of AChE genes which include those encoding neuromuscular AChEs and those genes which code for secreted AChEs. The latter proteins exist as soluble monomers released by the parasite during infection and these AChE are distinct from those enzymes which the nematodes use for synaptic transmission in their neuromuscular system. Thus far,Dictyocaulus viviparusis the only animal-parasitic nematode for which distinct genes that encode both neuromuscular and secreted AChEs have been defined. Here, we describe the isolation and characterization of a cDNA encoding a putative neuromuscular AChE fromD. viviparuswhich contains a tryptophan amphiphilic tetramerization (WAT) domain at its C-terminus analogous to the common ‘tailed’ AChE form found in the neuromuscular systems of vertebrates and in the ACE-1 AChE fromCaenorhabditis elegans. This enzyme differs from the previously isolated,D. viviparusneuromuscular AChE (Dv-ACE-2), which is a glycosylphosphatidylinositol-anchored variant analogous to vertebrate ‘hydrophobic’ AChE. |
| Databáze: | OpenAIRE |
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