Nematode Acetylcholinesterases: Several Genes and Molecular Forms of Their Products

Arpagaus, Martine; Richier, Patricia; L'Hermite, Yann; Roy, Florence Le; Bergé, Jean-Baptiste; Thierry-Mieg, Danielle; Toutant, Jean‐Pierre

doi:10.1007/978-1-4615-3046-6_9

Multidisciplinary Approaches to Cholinesterase Functions 1992

DOI: 10.1007/978-1-4615-3046-6_9

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Nematode Acetylcholinesterases: Several Genes and Molecular Forms of Their Products

Martine Arpagaus

Patricia Richier

Yann L'Hermite

et al.

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1996

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Cited by 2 publications

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“…We report that two major amphiphilic forms exist in Steinernema AChE : a glycolipid-anchored dimer of catalytic subunits and a higher oligomer of hydrophilic subunits linked by disulfide bonds to a structural hydrophobic component. Some of the results have been presented as abstracts [16,171.…”

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confidence: 99%

Acetylcholinesterases of the nematode Steinernema carpocapsae

Arpagaus¹,

Richier²,

Bergé³

et al. 1992

European Journal of Biochemistry

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We analyzed the molecular forms of acetylcholinesterase (AChE) in the nematode Steinernema carpocapsae. Two major AChEs are involved in acetylcholine hydrolysis. The first class of AChE is highly sensitive to eserine = 0.05 pM). The corresponding molecular forms are: an amphiphilic 14s form converted into a hydrophilic 14.5s form by mild proteolysis and two hydrophilic 12s and 7s forms. Reduction of the amphiphilic 14s form with 10 mM dithiothreitol produces hydrophilic 7s and 4s forms, indicating that it is an oligomer of hydrophilic catalytic subunits linked by disulfide bond(s) to a hydrophobic structural element that confers the amphiphilicity to the complex. Sedimentation coefficients suggest that 4S, 7S, 12s forms correspond to hydrophilic monomer, dimer, tetramer and that the 14s form is also a tetramer linked to one structural element. The second class of AChE is less sensitive to eserine (IC50 =0.1 mM). Corresponding molecular forms are hydrophilic and amphiphilic 4s forms (monomers) and a major amphiphilic 7s form converted into a hydrophilic dimer by Bacillus thuringiensis phosphatidylinositol-specific phospholipase C. This amphiphilic 7s form thus possesses a glycolipid anchor. It appears that Steinernemu (a very primitive invertebrate) presents AChEs with two types of membrane association that closely resemble those described for amphiphilic G2 and G4 forms of AChE in more evolved animals.Acetylcholinesterase (AChE) and butyrylcholinesterase are highly polymorphic enzymes in vertebrates. Six different molecular forms can be expressed in a tissue-specific and agedependent manner. Three globular forms (Gl, G2 and G4 forms) correspond to monomers, dimers and tetramers of catalytic subunits, and three asymmetric forms (A forms) are associations of one, two or three tetramers to a collagen 'tail' [I].In invertebrates, only AChE has been described so far and its molecular diversity is more restricted : for example, there is no convincing evidence for the existence of collagen-tailed, asymmetric forms in these organisms. In insects, only G1 and G 2 forms have been characterized. The major molecular form is an amphiphilic dimer (2, 31 linked to the plasma membrane by a glycolipid anchor [4 -61. A glycolipid-anchored AChE has also been characterized in the trematode Schistosoma mansoni [7].

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confidence: 99%

Acetylcholinesterases of the nematode Steinernema carpocapsae

Arpagaus¹,

Richier²,

Bergé³

et al. 1992

European Journal of Biochemistry

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Molecular forms of tegumental and muscle acetylcholinesterases of Schistosoma

1996

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Acetylcholinesterase (AChE) is present in the muscle and on the tegument of schistosomes. Molecular forms of schistosome AChE were examined because particular AChEs are found in tissues of distinct function elsewhere. The dimeric globular form (G2) is the only form evident in adult Schistosoma haematobium: 32% of the muscle AChE is hydrophilic and 61% is membrane associated. A substantial amount of this enzyme is phosphatidylinositol (PI) anchored since it could be released by PI-specific phospholipase C from both muscle and tegumental membranes.

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Nematode Acetylcholinesterases: Several Genes and Molecular Forms of Their Products

Cited by 2 publications

References 24 publications

Acetylcholinesterases of the nematode Steinernema carpocapsae

Acetylcholinesterases of the nematode Steinernema carpocapsae

Molecular forms of tegumental and muscle acetylcholinesterases of Schistosoma

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