Monomeric amphiphilic forms of acetylcholinesterase appear early during brain development and may correspond to biosynthetic precursors of the amphiphilic G4 forms

Inestrosa, Nibaldo C.; Moreno, Ricardo D.; Fuentes, María-Elena

doi:10.1016/0304-3940(94)90172-4

Cited by 17 publications

(11 citation statements)

References 19 publications

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“…In tetrathyridium, as well as in segmented (not shown) and adult stages of M. corti, the monomeric molecular form of the enzyme (G1, sedimentation coefficient 4-6 S) is present. Interestingly, in the adult worm the G1 form of AChE co-exists with a more complex molecular form, showing a sedimentation velocity (10.5 S), similar to the tetrameric (G4) AChE that was described in mouse brain (Inestrosa et al, 1994). Consequently, a rise in the AChE activity and the presence of a more complex molecular form of this enzyme is coincident with the initiation of the cellular processes leading to the adult stage of the parasite.…”

Section: Discussionmentioning

confidence: 91%

Localization, specific activity, and molecular forms of acetylcholinesterase in developmental stages of the cestode Mesocestoides corti

Kemmerling

Cabrera

Campos

et al. 2005

Journal Cellular Physiology

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The nervous system of flatworms is quite simple although there is increasing evidence indicating that it is chemically complex. Studies of the nervous system in these animals have only been performed in the larval stage or in the adult worms, which are easy to obtain in nature, while the description of the nervous system in developing stages of these organisms is missing. Mesocestoides corti is a parasitic platyhelminth whose larvae can be induced in vitro to develop to adult, sexually mature worms, opening the possibility of studying the nervous system of a flatworm in different stages of development. Here, we describe the presence, activity, location, and molecular forms of acetylcholinesterase (AChE) in different stages of development of M. corti, from the larvae to adult forms of this endoparasite, obtained in in vitro cultures after induction of the larval stage with trypsin. Our results point to AChE as a molecular marker of the nervous system in platyhelminthes. The change in molecular forms of this enzyme and the increase in its activity during development from larvae to adult worm may reflect the presence of a more complex nervous system, necessary to adjust and coordinate the movement of a much bigger structure. A relationship between the development of the reproductive apparatus in segmented and adult worms with a more complex nervous system in these stages is also apparent. Finally, our study opens the possibility of applying anti-AChE as more effective therapeutic strategies against cestode parasites.

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Section: Discussionmentioning

confidence: 91%

Localization, specific activity, and molecular forms of acetylcholinesterase in developmental stages of the cestode Mesocestoides corti

Kemmerling

Cabrera

Campos

et al. 2005

Journal Cellular Physiology

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“…During rat and mouse brain development, an overall change in the expression of AChE molecular forms is observed in which the proportion of G1 decreases as the relative amounts of cell-associated G4 increase (Rieger and Vigny, 1976;Wade and Timiras, 1980;Inestrosa et al, 1994). Indeed, Layer and Willbold (1995) consider cholinesterase expression to occur in two discrete developmental phases; a morphogenetic period where low molecular weight forms predominate and a synaptogenetic phase during which expression of tetrameric AChE prevails.…”

Section: Discussionmentioning

confidence: 99%

“…6A). These forms likely function as precursors to the more complex oligomeric forms of the enzyme (Brimijoin, 1983;Massoulie et al, 1993;Inestrosa et al, 1994). To further assess the amphiphilic character of the AChE molecules, EB cell extracts were also run on sucrose gradients containing Brij-96.…”

Section: Differences In Expression Of Ache Molecular Species During Dmentioning

confidence: 99%

“…Tetramers, linked to a noncatalytic hydrophobic subunit, are most common in mammalian nervous tissue. Indeed, G4 AChE represents 80 -90% of the enzyme in mammalian brain (Inestrosa et al, 1994). The appearance of cholinesterase activity on nerve cells often precedes synaptogenesis, and it has been hypothesized that cholinesterase is important in development of the mammalian nervous system (Robertson and Yu, 1993;Layer and Willbold, 1995).…”

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confidence: 99%

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Regulation of Acetylcholinesterase Expression during Neuronal Differentiation

Coleman

Taylor

1996

Journal of Biological Chemistry

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We have examined the developmental expression of acetylcholinesterase (AChE) during the process of neuronal differentiation from a pluripotent stem cell. P19 embryonic carcinoma cells form embryoid bodies, which, when cultured with retinoic acid, are induced to differentiate into neurons and glia. No AChE activity is present in the undifferentiated stem cells, and mRNA protection analyses do not detect AChE mRNA. Commitment to a neuronal differentiation pathway results in increased levels of AChE mRNA, production of a tetrameric form of the enzyme, and secretion of AChE into the culture medium. Concomitant with subsequent morphological differentiation into neurons, enzyme secretion diminishes and AChE becomes largely tethered to the neuronal cell membranes. The enzyme is attached to the cell surface as a globular tetramer. Its hydrodynamic properties are consistent with association through a noncatalytic hydrophobic subunit rather than anchorage by a glycophospholipid tail. No change in the rate of transcription of the Ache gene was detected during the course of differentiation, suggesting that the gene is actively transcribed at very early stages of development. Results suggest that stabilization of a labile mRNA governs the increase in AChE mRNA and gene product. The studies presented indicate that an early event in neuronal differentiation is the stabilization of the mRNA leading to expression of a secreted form of AChE. A subsequent step associated with neurite outgrowth results in a transition from secretion of the tetrameric enzyme to its localization on the cell membrane.

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“…1) and in whole dystrophic muscle (Cabezas-Herrera et al, 1994a). As the content of AChE monomers is developmentally regulated (Arendt et al, 1992;Inestrosa et al, 1994), it may be thought that the increased level of light AChE species in dystrophic muscle is related to a maturational defect (Skau, 1990), the synthesis of the light AChE forms being boosted and/or their assembly for building tetramers being restricted by dystrophy. In contrast, the G2/G1 ratio consistently increased in DMV, because G1 predominated in NMV and G2 in dystrophic muscle membranes (Fig.…”

Section: Solubilization and Distribution Of Ache Forms In Muscle Micrmentioning

confidence: 99%

Glycosylation of Acetylcholinesterase Forms in Microsomal Membranes from Normal and Dystrophic Lama2^dy Mouse Muscle

Cabezas-Herrera

Moral‐Naranjo

Campoy

et al. 1997

Journal of Neurochemistry

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Abstract:The distribution and glycosylation of acetyicholinesterase (AChE) forms in vesicles derived from sarcoplasmic reticulum of normal muscle (NMV) were investigated and compared with those from dystrophic muscle vesicles (DMV). AChE activity was similar in NMV and DMV. Most of the AChE in NMV and half in DMV were released with Triton X-1 00. Asymmetric (A 12) and globular hydrophilic and amphiphilic (G~, G~, G~, and G~) AChE species occurred in NMV and DMV, the lighter forms being predominant. The percentage of G~and G~de-creased in DMV. A fraction of the AChE that could not be extracted with detergent was detached with collagenase. Most of the detergent-released A12 AChE from NMV and nearly half in DMV failed to bind to Ricinus communis agglutinin (RCA-I). Conversely, the collagenase-detached isoforms bound to RCA, revealing that asymmetric AChE associated with internal membranes or basal lamina differed in glycosylation. Moreover, nearly half of GÃChE in DMV and a few in NMV bound to RCA. Most of the RCA-unreactive Gforms in NMV come from sarcolemma. The results indicate that dystrophy induces minor changes in the distribution and glycosylation of AChE forms in internal membranes of muscle.

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Monomeric amphiphilic forms of acetylcholinesterase appear early during brain development and may correspond to biosynthetic precursors of the amphiphilic G4 forms

Cited by 17 publications

References 19 publications

Localization, specific activity, and molecular forms of acetylcholinesterase in developmental stages of the cestode Mesocestoides corti

Localization, specific activity, and molecular forms of acetylcholinesterase in developmental stages of the cestode Mesocestoides corti

Regulation of Acetylcholinesterase Expression during Neuronal Differentiation

Glycosylation of Acetylcholinesterase Forms in Microsomal Membranes from Normal and Dystrophic Lama2^dy Mouse Muscle

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Monomeric amphiphilic forms of acetylcholinesterase appear early during brain development and may correspond to biosynthetic precursors of the amphiphilic G4 forms

Cited by 17 publications

References 19 publications

Localization, specific activity, and molecular forms of acetylcholinesterase in developmental stages of the cestode Mesocestoides corti

Localization, specific activity, and molecular forms of acetylcholinesterase in developmental stages of the cestode Mesocestoides corti

Regulation of Acetylcholinesterase Expression during Neuronal Differentiation

Glycosylation of Acetylcholinesterase Forms in Microsomal Membranes from Normal and Dystrophic Lama2dy Mouse Muscle

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Glycosylation of Acetylcholinesterase Forms in Microsomal Membranes from Normal and Dystrophic Lama2^dy Mouse Muscle