Visualization of detailed acetylcholinesterase fiber and neuron staining in rat brain by a sensitive histochemical procedure.

Tago, Hisao; Kimura, Hiroshi; Maeda, Toshihiro

doi:10.1177/34.11.2430009

Cited by 421 publications

(170 citation statements)

References 24 publications

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“…All neuronal cell types, SH-SY5Y, NGF-stimulated PC-12 cells, and CGN exhibited a similar localization pattern. The localization of AChE in neuronal cells is supported in data from other laboratories that analyzed the localization of AChE catalytic activity by histochemical methods [Spencer and Baker, 1986;Tago et al, 1986;Greenfield, 1991;Anglade et al, 1999], immunocytochemical data [Rotundo and Carbonetto, 1987;Tojima et al, 2000], and flow cytometry [Pick et al, 2004]. While the neuronal localization pattern was identical, the primary CGN expressed ~20-fold more AChE catalytic activity than the SH-SY5Y cell line.…”

Section: Discussionmentioning

confidence: 70%

Differential localization of acetylcholinesterase in neuronal and non‐neuronal cells

Thullbery

Cox

Schule

et al. 2005

J of Cellular Biochemistry

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Acetylcholinesterase (AChE) expression is regulated in cell types at the transcriptional and translational levels. In this study, we characterized and compared AChE catalytic activity, mRNA, protein expression, and protein localization in a variety of neuronal (SH-SY5Y neuroblastoma and primary cerebellar granule neurons (CGN)) and non-neuronal (LLC-MK2, HeLa, THP-1, and primary astrocytes) cell types. All cell lines expressed AChE catalytic activity; however the levels of AChE-specific activity were higher in neuronal cells than in the non-neuronal cell types. CGN expressed significantly more AChE activity than SH-SY5Y cells. All cell lines analyzed expressed AChE protein at equivalent levels, as well as mRNA splice variants. Localization of AChE was characterized by immunofluorescence and confocal microscopy. SH-SY5Y, CGN, and nerve-growth factor-differentiated PC-12 cells exhibited a pattern of AChE localization characterized as diffuse in the cytoplasm and punctate staining along neurites and on the plasma membrane. The localization in HeLa, LLC-MK2, fibroblasts, and undifferentiated PC-12 cells was significantly different than in neuronal cells-AChE was intensely localized in the perinuclear region, without staining near or on the plasma membrane. Based on the evidence presented here, we hypothesize that the presence of AChE protein doesn't correlate with catalytic activity, and the diffuse cytoplasmic and plasma membrane localization of AChE is a property of neuronal cell types. Keywords acetylcholinesterase; confocal microscopy; cerebellar granule neuron; neuroblastoma; SH-SY5Y; HeLa; PC-12 Acetylcholinesterase (AChE) belongs to the serine hydrolase family that contains the α/β hydrolase fold as a common structural element [Ollis et al., 1992]. The catalytic active site of AChE is made up of a precise arrangement of active site functional groups that catalyze the hydrolytic breakdown of esters that bear quaternary ammonium groups. The biological importance of AChE-catalyzed hydrolysis is manifested in the rapid termination of the neuronal impulse that occurs when acetylcholine (ACh) is released into the synaptic cleft. AChE rapidly hydrolyzes ACh into acetic acid and choline at extremely fast turnover rates [Taylor and Radic, 1994].

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Section: Discussionmentioning

confidence: 70%

Differential localization of acetylcholinesterase in neuronal and non‐neuronal cells

Thullbery

Cox

Schule

et al. 2005

J of Cellular Biochemistry

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“…Briefly, 40-m-thick horizontal sections were incubated overnight at 4°C in antibody vehicle containing purified mouse mAb. Detection of antibody-antigen complexes was accomplished using the ABC Elite peroxidase reaction kit (Vector Laboratories, Burlingame, CA) and visualized using a nickel-enhanced diaminobenzidine procedure (Tago et al, 1986;Rhodes et al, 1995). Doublelabel immunofluorescence labeling was performed as described previously (Rhodes et al, 1997), except that isotype-specific anti-mouse antibodies conjugated to Alexa fluorophores (Molecular Probes) were used as the detecting antibodies.…”

Section: Methodsmentioning

confidence: 99%

KChIPs and Kv4 α Subunits as Integral Components of A-Type Potassium Channels in Mammalian Brain

Rhodes¹,

Carroll²,

Sung³

et al. 2004

J. Neurosci.

237

290

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“…In addition, motor endplates were visualized according to Tago's standard method (Tago et al 1986) based on their acetylcholinesterase (AChE) activity. Total fiber number was counted in normal, reinnervated, and reinnervated-regenerated muscles analyzing the whole cross section of each muscle (three muscles for each group) with the help of Olympus DP Soft software, Version 3.2.…”

Section: Morphological and Morphometric Analysis Of Musclesmentioning

confidence: 99%

Regeneration of Reinnervated Rat Soleus Muscle Is Accompanied by Fiber Transition Toward a Faster Phenotype

Mendler

Pintér

Kiricsi

et al. 2007

J Histochem Cytochem.

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S U M M A R Y The functional recovery of skeletal muscles after peripheral nerve transection and microsurgical repair is generally incomplete. Several reinnervation abnormalities have been described even after nerve reconstruction surgery. Less is known, however, about the regenerative capacity of reinnervated muscles. Previously, we detected remarkable morphological and motor endplate alterations after inducing muscle necrosis and subsequent regeneration in the reinnervated rat soleus muscle. In the present study, we comparatively analyzed the morphometric properties of different fiber populations, as well as the expression pattern of myosin heavy chain isoforms at both immunohistochemical and mRNA levels in reinnervated versus reinnervated-regenerated muscles. A dramatic slow-tofast fiber type transition was found in reinnervated soleus, and a further change toward the fast phenotype was observed in reinnervated-regenerated muscles. These findings suggest that the (fast) pattern of reinnervation plays a dominant role in the specification of fiber phenotype during regeneration, which can contribute to the long-lasting functional impairment of the reinnervated muscle. Moreover, because the fast II fibers (and selectively, a certain population of the fast IIB fibers) showed better recovery than did the slow type I fibers, the faster phenotype of the reinnervated-regenerated muscle seems to be actively maintained by selective yet undefined cues. (J Histochem Cytochem 56:111-123, 2008)

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Visualization of detailed acetylcholinesterase fiber and neuron staining in rat brain by a sensitive histochemical procedure.

Cited by 421 publications

References 24 publications

Differential localization of acetylcholinesterase in neuronal and non‐neuronal cells

Differential localization of acetylcholinesterase in neuronal and non‐neuronal cells

KChIPs and Kv4 α Subunits as Integral Components of A-Type Potassium Channels in Mammalian Brain

Regeneration of Reinnervated Rat Soleus Muscle Is Accompanied by Fiber Transition Toward a Faster Phenotype

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