Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.1.7 (acetylcholinesterase)
 28,390 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Prion diseases are neurodegenerative disorders characterized by accumulation of an aberrantly folded isoform (PrP(Sc)) of the normal prion protein (PrP(C)). Using in situ hybridization and immunohistochemistry, we have studied changes in the expression of neuropeptides, acetylcholinesterase and tyrosine hydroxylase in CD1 and FVB wild-type mouse strains, as well as in PrP(C) null mice and in mice overexpressing PrP(C) following intracerebral inoculation with RML or Me7 prions. In the immunohistochemical analysis, neuropeptide Y (NPY), enkephalin and dynorphin-like immunoreactivities increased in mossy fibers of CD1 and FVB mice inoculated with either RML- or Me7 prions, whereas cholecystokinin-like immunoreactivity was decreased. These changes in peptide levels were paralleled by an increase in the transcripts in granule cells for neuropeptide Y, enkephalin, and cholecystokinin. However, the dynorphin transcript was decreased in the granule cells. The changes occurred more rapidly in PrP(C)-overexpressing compared to wild-type mice, and could not be found at all in PrP(C)-knockout mice. These changes in peptide expression, which mostly occur before appearance of symptoms of disease, may reflect attempts to initiate protective and/or regenerative processes.
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PMID:Changes in neuropeptide expression in mice infected with prions. 1662 Nov 65

Transmissible spongiform encephalopaties are caused by an extracellular surface protein, the scrapie prion protein (PrPsc), which is an aberrant form of normal and functional cellular PrP (PrPc). The pathological hallmarks of these diseases are the accumulation and deposition of PrPsc in the form of amyloid fibrils in the central nervous system (Tateishi et al., 1988), similar to amyloid-beta (Abeta) protein in Alzheimer's disease (AD). In some patients, Abeta and prion pathology can coexist (Hainfellner et al., 1998), and a common spatial pattern of protein deposition has been described (Armstrong et al., 2001). In addition, it is well-known that acetylcholinesterase (AChE) colocalizes with Abeta deposits of brains in AD patients and accelerates assembly of Abeta peptides through the peripheral site of the enzyme (Inestrosa et al., 1996). The aim of the present study was to analyze time course and concentration dependence of the AChE proaggregating effect on synthetic peptide-spanning residues 106-126 of human PrP (PrP106-126) and the reversion of this effect by different AChE inhibitors (AChEIs).
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PMID:Effect of acetylcholinesterase inhibitors on AChE-induced PrP106-126 aggregation. 1719 41

The cellular prion protein (PrP(C)) is a neuronal-anchored glycoprotein that has been associated with various functions in the CNS such as synaptic plasticity, cognitive processes and neuroprotection. Here we investigated age-related behavioral and neurochemical alterations in wild-type (Prnp(+/+)), PrP(C) knockout (Prnp(0/0)) and the PrP(C) overexpressing Tg-20 mice. Three- or 11 month-old animals were submitted to a battery of behavioral tasks including open field, activity cages, elevated plus-maze, social recognition and inhibitory avoidance tasks. The 11 month-old Prnp(+/+) and Prnp(0/0) mice exhibited significant impairments in their locomotor activity and social recognition memory and increased anxiety-related responses. Remarkably, Tg-20 mice did not present these age-related impairments. The i.c.v. infusion of STI1 peptide 230-245, which includes the PrP(C) binding site, improved the age-related social recognition deficits in Prnp(+/+). In comparison with the two other age-matched genotypes, the 11 month-old Tg-20 mice also exhibited reduced activity of seric acetylcholinesterase, increased expression of the protein synaptophysin and decreased caspase-3 positive-cells in the hippocampus. The present findings obtained with genetic and pharmacological approaches provide convincing evidence that PrP(C) exerts a critical role in the age-related behavioral deficits in mice probably through adaptive mechanisms including apoptotic pathways and synaptic plasticity.
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PMID:Cellular prion protein modulates age-related behavioral and neurochemical alterations in mice. 1974 26