A 13 kDa fragment is responsible for the hydrophobic aggregation of brain G4 acetylcholinesterase

Fuentes, María-Elena; Rosenberry, Terrone L.; Inestrosa, Nibaldo C.

doi:10.1042/bj2561047

Cited by 33 publications

(10 citation statements)

References 22 publications

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“…Presently, the mechanism by which AChE‐mediated cell‐substratum adhesion could lead to enhanced axonal outgrowth is not known. In nervous tissues, the major form of AChE consists of a tetramer of four AChE monomers (G4), which can be anchored to the cell membrane by a 20 kDa hydrophobic protein (Boschetti and Brodbeck, 1996; Fuentes et al, 1988; Navaratnam et al, 2000; Perrier et al, 2000; see Fig. 9).…”

Section: Discussionmentioning

confidence: 99%

Direct evidence for an adhesive function in the noncholinergic role of acetylcholinesterase in neurite outgrowth

et al. 2001

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Section: Discussionmentioning

confidence: 99%

Direct evidence for an adhesive function in the noncholinergic role of acetylcholinesterase in neurite outgrowth

et al. 2001

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“…In contrast, the sedimentation coefficient of the G, AChE in human cerebrospinal fluid and fetal bovine serum (Ralston et al, 1985) does not depend on the presence of detergent in the gradient. Therefore, it can be concluded that in mammalian brain three different types of G4 forms may be produced: (i) a hydrophilic secretory form, (ii) a highly hydrophobic proteinase K-sensitive form (Fuentes et al, 1988;Roberts et al, 1991;Heider and Brodbeck, 1992), and (iii) a hydrophilic molecule with the capacity to interact with the membrane and with detergents but with an overall hydrophobicity not sufficient to maintain the enzyme in a hydrophobic environment such as the detergent-rich phase in a partition with Triton X-114. These three forms might correspond to G,f, G,s, and G,i AChE molecules (G, forms with fast, slow, and intermediate electrophoretic mobility, respectively) identified in chick muscle by charge-shift electrophoresis and sedimentation analysis (Toutant, 1986).…”

Section: Discussionmentioning

confidence: 99%

Amphiphilic properties of molecular forms of acetylcholinesterase in normal and dystrophic muscle

Cabezas‐Herrera

Campoy

Vidal

1994

J of Neuroscience Research

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Acetylcholinesterase (AChE) molecular forms were studied in normal (NM) and in dystrophic (DM) 129B6F1/J mouse muscle. Successive extractions of the tissue with saline and saline-Triton X-100 buffers yielded two soluble fractions, S1 and S2. Forty percent of the AChE in NM was measured in S1 and 60% in S2, and 65% and 35%, respectively, in extracts from DM. A12, A8, G4, G2, and G1 forms of AChE were found in S1 and S2 from NM and DM. A similar content of asymmetric molecules was noticed between NM and DM. G4 AChE was a minor species in DM, and G1 and G2 AChE were more abundant in DM than in NM. The amphiphilic properties of the several molecules were assessed by Triton X-114 phase-partitioning and hydrophobic chromatography. Thirty and 70% of the enzyme in a mixture of S1 and S2 partitioned in the detergent-rich and in the detergent-poor phases, respectively, whether the extracts were obtained from NM or DM. Asymmetric and G4 AChE predominated in the aqueous phase and G1 and G2 in the detergent phase. Ten and 25% of the enzyme in S1 from NM or DM, respectively, was adsorbed to the phenyl-agarose. Elution of the retained enzyme followed by sedimentation analysis revealed that a certain amount of asymmetric and most of the G1 and G2 forms were associated with the matrix. The content of amphiphilic asymmetric and light globular forms was notably higher in DM than in NM. The results suggest that dystrophic muscle produces a specific pattern of molecular forms of AChE.

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“…These two enzyme molecules displayed amphiphilic properties. The heavy form disappeared in analysis performed in detergent-free gradients, this phenomenon being related to the characteristic aggregation of the amphiphilic AChE tetramers (Rotundo, 1984;Fuentes et al, 1988;Saez-Valero et al, 1993). In addition, the sedimentation value of the light form decreased from 433, in gradients prepared without detergent, to 4.1s and to 3.0s in gradients with Triton X-100 and Brij 96, respectively.…”

Section: Solubilization Of Cholinesterasesmentioning

confidence: 95%

Acetyl‐ and butyrylcholinesterase activities in the rat retina and retinal pigment epithelium

Sánchez‐Chávez

Vidal

Salceda

1995

J of Neuroscience Research

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The acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) activities in the neural retina and retinal pigment epithelium (RPE) of adult rats were determined. The tissues were extracted with a saline buffer to release the soluble enzymes (S1) and the pellet re-extracted with Triton X-100 to detach the membrane-bound enzymes (S2). Less than 5% of the cholinesterase activity measured in retina and almost 30% of that assayed in RPE was due to BChE. About 20% and 10% of the AChE in retina and RPE was brought into solution with a saline buffer and the rest with a detergent-containing buffer. Main AChE molecular forms of 10.5S (hydrophilic G4H), 9.5S (amphiphilic G4A) and 3.0S (amphiphilic G1A) were identified in retina by subjecting the supernatant S1 to sedimentation analysis in sucrose gradients made with Brij 96. Amphiphilic G4 and G1 AChE were found in S2. Analysis of the soluble fractions obtained from RPE in the gradients made with Brij 96 revealed 16.0S (asymmetric A12), 10.5-10.0S (globular G4H + G4A), 4.5S (G2A), and 3.0S (G1A) AChE forms in S1, whereas G4A, G2A, and G1A enzyme molecules predominated in S2. Our results show that amphiphilic tetramers and monomers of AChE are abundant in neural retina, and enzyme tetramers, dimers, and monomers in RPE. The AChE in the neural retina might be involved in cholinergic actions. The enzyme function in the retinal pigment epithelium remains to be established.

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A 13 kDa fragment is responsible for the hydrophobic aggregation of brain G4 acetylcholinesterase

Cited by 33 publications

References 22 publications

Direct evidence for an adhesive function in the noncholinergic role of acetylcholinesterase in neurite outgrowth

Direct evidence for an adhesive function in the noncholinergic role of acetylcholinesterase in neurite outgrowth

Amphiphilic properties of molecular forms of acetylcholinesterase in normal and dystrophic muscle

Acetyl‐ and butyrylcholinesterase activities in the rat retina and retinal pigment epithelium

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