Murine and human mast cell express acetylcholinesterase

Nechushtan, Hovav; Soreq, Hermona; Kuperstein, Valentina; Tshori, Sagi; Razin, Ehud

doi:10.1016/0014-5793(95)01466-7

Cited by 18 publications

(17 citation statements)

References 23 publications

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“…13 MC mediators can sensitize sensory neurons, which further activate or inhibit the MC by releasing neurotransmitters or neuropeptides (eg, neurotensin, somatostatin, substance P, and acetylcholine), revealing another probable mode of molecular communication between MCs and neurons. 19,20 In addition, the MCs seem to play a crucial role in local mechanisms of pain control. The number of MCs within the endometrium is low, and those that are present are predominantly localized to the basal layer.…”

Section: Discussionmentioning

confidence: 99%

Effectiveness of the Association N-Palmitoylethanolamine and Transpolydatin in the Treatment of Primary Dysmenorrhea

Tartaglia

Armentano

Giugliano³

et al. 2015

Journal of Pediatric and Adolescent Gynecology

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Section: Discussionmentioning

confidence: 99%

Effectiveness of the Association N-Palmitoylethanolamine and Transpolydatin in the Treatment of Primary Dysmenorrhea

Tartaglia

Armentano

Giugliano³

et al. 2015

Journal of Pediatric and Adolescent Gynecology

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“…Most isoforms are found in the central and peripheral nervous systems [Taylor and Radic, 1994;Soreq and Seidman, 2001]. Isoforms have also been characterized in hematopoietic cells, as well as in tumor cells [Karpel et al, 1994;Nechushtan et al, 1996;Perry et al, 2002]. The different isoforms have been shown by reverse-transcriptase polymerase chain reaction (RT-PCR) to result from alternative splicing of AChE mRNA leading to isoforms of AChE protein differing in their 3′ exon composition [Karpel et al, 1994;Perry et al, 2002].…”

mentioning

confidence: 99%

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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“…The importance of this to CNS disease has been reviewed by Theoharides et al 46 who observed that mast cells are primarily perivascular in the CNS. In other areas, mast cells show cholinesterase activity, which suggests that mast cell enzymatic reactions could depress cholinergic activity in localized areas of the brain 47 …”

Section: Mast Cellsmentioning

confidence: 99%