Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Choline acetyltransferase expression

Yasuyama K, Salvaterra PM (1999) Localization of choline acetyltransferase-expressing neurons in Drosophila nervous system. Microsc Res Tech 45 65-79... [Pg.61]

Andres, C., Beeri, R., Friedman, A., Lev-Lehman, E., Henis, S., Timherg, R., Shani, M., Soreq, H. (1997). Acetylcholinesterase-transgenic mice display embryonic modulations in spinal cord choline acetyltransferase and neurexin Iheta gene expression followed by late-onset neuromotor deterioration. Proc. Natl Acad. Sci. USA 94 8173-8. [Pg.708]

Catalpol. Zhang et al. [233] studied the neuroprotective effects of catalpol, an iridoid glycoside isolated from the fresh rehmannia roots, on the cholinergic system and inflammatory cytokines in the senescent mouse brain induced by D-galactose. Acetylcholinesterase (AChE) activity increased in senescent mouse brain and choline acetyltransferase (ChAT) decreased in the basal forebrain of senescent mouse. Muscarinic acetylcholine receptor Ml (mAChRl) expression declined and the levels of tumor necrosis factor (TNF-a), interleukin-ip (IL-ip), and advanced glycation end products... [Pg.404]

Fig. 84. Illustrations of choline-acetyltransferase (ChAT)-like immunoreactivity in the rabbit cerebellum. A. Sagittal view of the rabbit cerebellum delineating the lobules according to Larsell (Larsell, 1970). Mean measurements of ChAT activity are indicated by numbers in parentheses. B. Magnified view of the ventral vermis. The vermis contains areas of ChAT-positive mossy fiber terminals (indicated by dots). These areas in lobules 1 and 9d are illustrated in C and D, respectively. E. View of the right paraflocculus of the rabbit. ChAT-like immunoreactivity and ChAT activity was highest in the ventral paraflocculus, particularly lobule 2. The numbers in parentheses are mean measurements of ChAT activity, expressed as mmol of Ach synthe-sized/hr. g tissue at 37°C, for each cerebellar lobule in six rabbits. Barmack et al. (1992a). Fig. 84. Illustrations of choline-acetyltransferase (ChAT)-like immunoreactivity in the rabbit cerebellum. A. Sagittal view of the rabbit cerebellum delineating the lobules according to Larsell (Larsell, 1970). Mean measurements of ChAT activity are indicated by numbers in parentheses. B. Magnified view of the ventral vermis. The vermis contains areas of ChAT-positive mossy fiber terminals (indicated by dots). These areas in lobules 1 and 9d are illustrated in C and D, respectively. E. View of the right paraflocculus of the rabbit. ChAT-like immunoreactivity and ChAT activity was highest in the ventral paraflocculus, particularly lobule 2. The numbers in parentheses are mean measurements of ChAT activity, expressed as mmol of Ach synthe-sized/hr. g tissue at 37°C, for each cerebellar lobule in six rabbits. Barmack et al. (1992a).
Gould E, Butcher LL (1987) Transient expression of choline acetyltransferase-like immunoreactivity in Purkinje cells of the developing rat cerebellum. Dev. Brain Res., 34, 30,3-306. [Pg.331]

Heat shock protein 70 and c-fos mRNA expression which were escalated during cerebral ischemia were reduced by phthalide 30 [320]. Moreover, 30, 31 and 32 diminished apoptotic neuronal cell death [321], while ameliorating the activities of mitochondrial respiratory chain complexes [322] and choline acetyltransferase (which is related to learning) [323], lending further support for the cerebro-protective potential of these three phthalides against focal ischemia. [Pg.646]

Influence of the culture substratum on the expression of choline acetyltransferase activity in purified motoneurons from rat embryos. Dev. Brain Res. 47 251-262. [Pg.168]

Magal, E., Burnham, P. and Varon, S. (1991b) Effects of ciliary neuronotrophic factor on rat spinal cord neurons in vitro survival and expression of choline acetyltransferase and low-affinity nerve growth factor receptors. Dev. Brain Res. 63 141-150. [Pg.305]

Choline acetyltransferase choline acetyltransferase (CAT) is an enzyme catalyzing the syntheses of acetylcholine from choline and acetyl coenzyme A. Choline acetyltransferase is expressed in neural and neuroendocrine cells and their tumors. [Pg.219]

Pedersen, W.A., Cashman, N.R. and Mattson, M.P. 1999. The lipid peroxidation product 4-hydroxynonenal impairs glutamate and glucose transport tmd choline acetyltransferase activity in NSC-19 motor neuron cells. Exp. Neurol. 155 1-10 Pei, J.J., Sersen, E., Iqbal, K. and Grundke-Iqbal, I. 1994. Expression of protein phosphatases (PP-1, PP-2A, PP-2B and PTP-IB) and protein kinases (MAP kinase and P34cdc2) in the hippocampus of patients with Alzheimer disease and normal aged individuals. Brain Res. 655 70-76... [Pg.523]


See other pages where Choline acetyltransferase expression is mentioned: [Pg.174]    [Pg.273]    [Pg.735]    [Pg.183]    [Pg.434]    [Pg.77]    [Pg.665]    [Pg.238]    [Pg.300]    [Pg.300]    [Pg.175]    [Pg.23]    [Pg.288]    [Pg.228]    [Pg.237]    [Pg.278]    [Pg.378]    [Pg.218]    [Pg.268]    [Pg.73]    [Pg.212]    [Pg.110]    [Pg.637]   
See also in sourсe #XX -- [ Pg.23 ]




SEARCH



Acetyltransferase

Choline acetyltransferase

© 2024 chempedia.info