Kasa P

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Full name : Kasa Peter

First name : Peter

Mail : Department of Cell Biology and Molecular Medicine, University of Szeged, Szeged

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Country : Hungary

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References (40)

Title : Long-term effects of selective immunolesions of cholinergic neurons of the nucleus basalis magnocellularis on the ascending cholinergic pathways in the rat: a model for Alzheimer's disease - Szigeti_2013_Brain.Res.Bull_94_9
Author(s) : Szigeti C , Bencsik N , Simonka AJ , Legradi A , Kasa P , Gulya K
Ref : Brain Research Bulletin , 94 :9 , 2013
Abstract : Alzheimer's disease is associated with a significant decrease in the cholinergic input to the neocortex. In a rat model of this depletion, we analyzed the subsequent long-term changes in cholinergic fiber density in two well-defined areas of the frontal and parietal cortices: Fr1, the primary motor cortex, and HL, the hindlimb area of the somatosensory (parietal) cortex, two cortical cholinergic fields that receive inputs from the nucleus basalis magnocellularis (nBM). A specific cholinergic lesion was induced by the intraparenchymal injection of 192 IgG-saporin into the nBM. Choline acetyltransferase (ChAT) immunohistochemistry was applied to identify the loss of cholinergic neurons in the nBM, while acetylcholinesterase (AChE) enzyme histochemistry was used to analyze the decreases in the number of cholinoceptive neurons in the nBM and the cholinergic fiber density in the Fr1 and HL cortical areas in response to the nBM lesion. The immunotoxin differentially affected the number of ChAT- and AChE-positive neurons in the nBM. 192 IgG-saporin induced a massive, irreversible depletion of the ChAT-positive (cholinergic) neurons (to 11.7% of the control level), accompanied by a less dramatic, but similarly persistent loss of the AChE-positive (cholinoceptive) neurons (to 59.2% of the control value) in the nBM within 2 weeks after the lesion. The difference seen in the depletion of ChAT- and AChE-positive neurons is due to the specificity of the immunotoxin to cholinergic neurons. The cholinergic fiber densities in cortical areas Fr1 and HL remained similarly decreased (to 62% and 68% of the control values, respectively) up to 20 weeks. No significant rebound in AChE activity occurred either in the nBM or in the cortices during the period investigated. This study therefore demonstrated that, similarly to the very extensive reduction in the number of ChAT-positive neurons in the nBM, cortical areas Fr1 and HL underwent long-lasting reductions in the number of AChE-positive fibers in response to specific cholinergic lesioning of the nBM.
ESTHER : Szigeti_2013_Brain.Res.Bull_94_9
PubMedSearch : Szigeti_2013_Brain.Res.Bull_94_9
PubMedID: 23357177

Title : Poster (41) Cholinesterase inhibitors are not all alike. -
Author(s) : Rakonczay Z , Papp H , Kasa P
Ref : In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects , (Inestrosa NC, Campos EO) P. Universidad Catolica de Chile-FONDAP Biomedicina :342 , 2004
PubMedID:

Title : Cholinesterase inhibitors are not all alike -
Author(s) : Rakonczay Z , Papp H , Kasa P
Ref : In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects , (Inestrosa NC, Campos EO) P. Universidad Catolica de Chile-FONDAP Biomedicina :89 , 2004
PubMedID:

Title : C-terminal fragments of amyloid-beta peptide cause cholinergic axonal degeneration by a toxic effect rather than by physical injury in the nondemented human brain - Kasa_2003_Neurochem.Res_28_493
Author(s) : Kasa P , Papp H , Zombori J , Mayer P , Checler F
Ref : Neurochem Res , 28 :493 , 2003
Abstract : Previous experimental studies have indicated that amyloid-beta peptide (Abeta) may cause axonal degeneration in the brain of individuals with Alzheimer's disease (AD) by physical injury, mass lesion, or membrane perturbation. In this study, acetylcholinesterase histochemical, and Abeta and tau immunohistochemical double-staining were performed in nondemented elderly human hippocampal and entorhinal brain samples, to demonstrate the presence of dystrophic neurites caused by the C-terminal or N-terminal fragments of Abeta. The early interactions between the Abeta-stained senile plaques (SPs) and the enzyme-positive axons were investigated. The double-stained samples revealed that Abeta deposition occurs first, followed by the development of cholinergic axonal damage. Most of the dystrophic axonal processes are incorporated in the peripheral area of the SPs and are positive for phosphorylated tau [pS202] and tau-5. The result suggests that C-terminal fragments are more harmful than N-terminal fragments of Abeta and may induce the development of dystrophic neurites by a toxic effect rather than by physical injury.
ESTHER : Kasa_2003_Neurochem.Res_28_493
PubMedSearch : Kasa_2003_Neurochem.Res_28_493
PubMedID: 12675137

Title : Role of acetylcholinesterase inhibitors in the metabolism of amyloid precursor protein - Pakaski_2003_Curr.Drug.Targets.CNS.Neurol.Disord_2_163
Author(s) : Pakaski M , Kasa P
Ref : Curr Drug Targets CNS Neurol Disord , 2 :163 , 2003
Abstract : Potentiation of central cholinergic activity has been proposed as a therapeutic approach for improving the cognitive function in patients with Alzheimer's disease (AD). Increasing the acetylcholine concentration in the brain by modulating acetylcholine-sterase (AChE) activity is among the most promising therapeutic strategies. Efforts to treat the underlying pathology based on the modulation of amyloid precursor protein (APP) processing in order to decrease the accumulation of beta-amyloid are also very important. Alterations in APP metabolism have recently been proposed to play a key role in the long-lasting effects of AChE inhibitors. This review surveys recent data from in vivo and in vitro studies that have contributed to our understanding of the role of AChE inhibitors in APP processing. The regulatory mechanisms relating to the muscarinic agonist effect, protein kinase C activation and mitogen-activated protein kinase phosphorylation, involving the alpha-secretase or the 5 -UTR region of the APP gene, are also discussed. Further work is warranted to elucidate the exact roles in APP metabolism of the AChE inhibitors used in AD therapy at present.
ESTHER : Pakaski_2003_Curr.Drug.Targets.CNS.Neurol.Disord_2_163
PubMedSearch : Pakaski_2003_Curr.Drug.Targets.CNS.Neurol.Disord_2_163
PubMedID: 12769797

Title : Effects of acetylcholinesterase inhibitors on the metabolism of amyloid precursor protein in vitro -
Author(s) : Pakaski M , Papp H , Rakonczay Z , Fakla I , Kasa P
Ref : Neurobiology , 9 :55 , 2001
PubMedID: 11558939

Title : Donepezil dose-dependently inhibits acetylcholinesterase activity in various areas and in the presynaptic cholinergic and the postsynaptic cholinoceptive enzyme-positive structures in the human and rat brain - Kasa_2000_Neurosci_101_89
Author(s) : Kasa P , Papp H , Kasa P, Jr. , Torok I
Ref : Neuroscience , 101 :89 , 2000
Abstract : In the symptomatic treatment of mild to moderately severe dementia associated with Alzheimer's disease, donepezil (E2020) has been introduced for the inhibition of acetylcholinesterase activity in the human brain. However, there is no morphological evidence as to how this chemical agent affects the acetylcholinesterase-positive structures in the various areas of the human and the rat CNS. This study demonstrates by histochemical means that donepezil exerts a dose-dependent inhibitory effect in vitro on acetylcholinesterase activity. The most sensitive areas were the cortex and the hippocampal formation. Within the different layers of the cortex, the cholinoceptive acetylcholinesterase-positive postsynaptic pyramidal cell bodies were more sensitive than the presynaptic cholinergic axonal processes. In the cortex, the cell body staining was already abolished by even 2 x 10(-8)M donepezil, whereas the axonal staining could be eliminated only by at least 5 x 10(-8)M donepezil. In the hippocampus, the axonal acetylcholinesterase reaction end-product was eliminated by 5 x 10(-7)M donepezil. The most resistant region was the putamen, where the staining intensity was moderately reduced by 1 x 10(-6)M donepezil. In the rat brain, the postsynaptic cholinoceptive and presynaptic cholinergic structures were inhibited by nearly the same dose of donepezil as in the human brain. These histochemical results provide the first morphological evidence that, under in vitro circumstances, donepezil is not a general acetylcholinesterase inhibitor in the CNS, but rather selectively affects the different brain areas and, within these, the cholinoceptive and cholinergic structures. The acetylcholinesterase staining in the nerve fibers (innervating the intracerebral blood vessels of the human brain and the extracerebral blood vessels of the rat brain) and at the neuromuscular junction in the diaphragm and gastrocnemius muscle of rat, was also inhibited dose dependently by donepezil. It is concluded that donepezil may be a valuable tool with which to influence both the pre- and the postsynaptic acetylcholinesterase-positive structures in the human and rat central and peripheral nervous systems.
ESTHER : Kasa_2000_Neurosci_101_89
PubMedSearch : Kasa_2000_Neurosci_101_89
PubMedID: 11068139

Title : In vitro effects of metrifonate on neuronal amyloid precursor protein processing and protein kinase C level - Pakaski_2000_Brain.Res_863_266
Author(s) : Pakaski M , Rakonczay Z , Fakla I , Papp H , Kasa P
Ref : Brain Research , 863 :266 , 2000
Abstract : Alteration in the processing of the amyloid precursor protein (APP) is a central event in the formation of amyloid deposits in the brains of individuals with Alzheimer's disease (AD). It has been suggested that acetylcholinesterase (AChE) inhibitors, which promote the cholinergic function and consequently improve the cognitive deficits, may also exert a neuroprotective effect by activating normal APP processing. We now report that an irreversible AChE inhibitor (metrifonate) increase the cell-associated APP level in a basal forebrain neuronal culture and also elevate the amount of APP secreted into the medium. The alterations in APP processing were accompanied by increased protein kinase C (PKC) levels. The results suggest that AChE inhibitors modulate the metabolism of APP, possibly via their stimulatory effects on PKC. Since changes in the activity and level of PKC may be involved in the pathogenesis of AD, it is concluded that the beneficial effect of metrifonate in AD therapy may be due not only to the stimulatory cholinergic function, but also to its activating effect on PKC.
ESTHER : Pakaski_2000_Brain.Res_863_266
PubMedSearch : Pakaski_2000_Brain.Res_863_266
PubMedID: 10773217

Title : Expressions of amyloid precursor protein, synaptophysin and presenilin-1 in the different areas of the developing cerebellum of rat - Fakla_2000_Neurochem.Int_36_143
Author(s) : Fakla I , Kovacs I , Yamaguchi H , Geula C , Kasa P
Ref : Neurochem Int , 36 :143 , 2000
Abstract : This study reveals the expressions of Alzheimer's disease-related amyloid precursor protein, presenilin-1, and a presynaptic marker protein, synaptophysin, in the archi-, paleo- and neocerebellum during the postnatal development of the rat. The Western blot results demonstrate a gradual increase in the soluble amyloid precursor protein level in the archicerebellum during the first 3 weeks, while in the neo- and paleocerebellum the levels reach a plateau as early as the 1st week. Immunohistochemically, the protein is present in the deep part of the external granule cell layer and the internal granule cell layer in the newborn animal, while in 3-week-old animals the staining appears mainly in the perikarya and dendrites of the Purkinje cells. The level of synaptophysin increases progressively from postnatal day 7 up to 3 weeks in the archi- and paleocerebellum, and up to 6 weeks in the neocerebellum. Immunohistochemically, the amyloid precursor protein staining appears first in the inner part of the molecular layer and in the internal granule cell layer. In a 3-week-old animal, synaptophysin staining is present in all areas of the cerebellar molecular layer and in the internal granule cell layer. The presenilin-1 immunohistochemical reaction appeared equally in the archi-, paleo- and neocerebellum. Much of the staining is present in the glial cells and Purkinje cells. Less immunoreactivity is observed in the Golgi cells and granule cells. It is concluded that the postnatal expressions of soluble and membrane-bound amyloid precursor protein, synaptophysin and presenilin-1 are regulated differently during the ontogenetical development of the archi-, paleo- and neocerebellum of rat. Further, the amyloid precursor protein and presenilin-1 may be present in cells which do not degenerate in Alzheimer's disease.
ESTHER : Fakla_2000_Neurochem.Int_36_143
PubMedSearch : Fakla_2000_Neurochem.Int_36_143
PubMedID: 10676878

Title : Human amyloid-beta1-42 applied in vivo inhibits the fast axonal transport of proteins in the sciatic nerve of rat - Kasa_2000_Neurosci.Lett_278_117
Author(s) : Kasa P , Papp H , Kovacs I , Forgon M , Penke B , Yamaguchi H
Ref : Neuroscience Letters , 278 :117 , 2000
Abstract : Human amyloid-beta1-42 has been suggested to be a pathogenetic factor in Alzheimer's disease. The precise mechanism by which this peptide causes the degeneration of neurons in the affected brain is not yet fully understood. By using immunohistochemistry we explored the inhibitory effects of human amyloid-beta1-42 applied in vivo on the fast axonal transport of acetylcholinesterase, the amyloid precursor protein, the vesicular acetylcholine transporter and synaptophysin in the sciatic nerve of rat. Our findings provide evidence for the in vivo neurotoxic effect of human amyloid-beta peptide.
ESTHER : Kasa_2000_Neurosci.Lett_278_117
PubMedSearch : Kasa_2000_Neurosci.Lett_278_117
PubMedID: 10643815

Title : Preferential inhibition of acetylcholinesterase molecular forms in normal human brain -
Author(s) : Rakonczay Z , Torok L , Kasa P
Ref : Neurobiology (Bp) , 7 :75 , 1999
PubMedID: 10746253

Title : Amyloid beta-peptide treatment induces a redistribution of acetylcholinesterase within the enzyme-containing neurons in in vitro tissue cultures -
Author(s) : Kasa P , Penke B , Pakaski M
Ref : Neurobiology , 6 :369 , 1998
PubMedID: 9778655

Title : Cholinergic structures and neuropathologic alterations in the olfactory bulb of Alzheimer's disease brain samples - Kovacs_1998_Brain.Res_789_167
Author(s) : Kovacs I , Torok I , Zombori J , Kasa P
Ref : Brain Research , 789 :167 , 1998
Abstract : This report describes the laminar distribution of acetylcholinesterase-positive structures and the neuropathologic alterations in the human olfactory bulb of control and Alzheimer's disease brain samples. The results suggests that no correlation exists between the distribution of cholinergic axons and the neuropathological alterations in the different layers in Alzheimer's disease.
ESTHER : Kovacs_1998_Brain.Res_789_167
PubMedSearch : Kovacs_1998_Brain.Res_789_167
PubMedID: 9602111

Title : Cholinoceptive neurons without acetylcholinesterase activity and enzyme-positive neurons without cholinergic synaptic innervation are present in the main olfactory bulb of adult rat - Kasa_1996_Neurosci_73_831
Author(s) : Kasa P , Karcsu S , Kovacs I , Wolff JR
Ref : Neuroscience , 73 :831 , 1996
Abstract : Light and electron microscopic histochemistry revealed acetylcholinesterase-positive and acetylcholinesterase-negative neurons in the main olfactory bulb of adult rat. Their distribution patterns on various neuron types have been analysed in detail. (1) No acetylcholinesterase staining could be demonstrated in the granule cells which receive a large number of the cholinergic synapses. (2) In contrast, enzyme activity was present in the soma and dendrites in most of the non-cholinergic and non-cholinoceptive relay cells (mitral cells and tufted cells) and in a subset of short-axon interneurons, where cholinergic synapses could not be detected. (3) Within the neuropil of glomeruli, two compartments were present, one of which was free of acetylcholinesterase-positive structures, while many enzyme-positive neuronal elements were seen in the other. (4) Characteristically, cholinergic and non-cholinergic neuronal structures showed triadic arrangements. (5) The axonal release of acetylcholinesterase from cholinergic axons is probable. It is suggested that, in the olfactory bulb, acetylcholinesterase is release by cholinergic afferent axons, and it is the cholinergic synapses that determine which postsynaptic neurons are cholinoceptive rather than the intraneuronal presence of acetylcholinesterase. In the main olfactory bulb, the acetylcholinesterase present in the relay cells therefore appears to have functions other than the hydrolysis of acetylcholine.
ESTHER : Kasa_1996_Neurosci_73_831
PubMedSearch : Kasa_1996_Neurosci_73_831
PubMedID: 8809802

Title : Effect of hypocholinergic activity on the immunoreactivity of beta-amyloid precursor protein in the central nervous system -
Author(s) : Kasa P , Kovacs I , Farkas Z , Geula C
Ref : Neurobiology (Bp) , 4 :119 , 1996
PubMedID: 9116689

Title : Neuropathologic changes in the olfactory bulb in Alzheimer's disease -
Author(s) : Kovacs I , Torok I , Zombori J , Kasa P
Ref : Neurobiology (Bp) , 4 :123 , 1996
PubMedID: 9116690

Title : The effect of pesticides on carp (Cyprinus carpio L). Acetylcholinesterase and its biochemical characterization - Szabo_1992_Ecotoxicol.Environ.Saf_23_39
Author(s) : Szabo A , Nemcsok J , Asztalos B , Rakonczay Z , Kasa P , Hieu LH
Ref : Ecotoxicology & Environmental Safety , 23 :39 , 1992
Abstract : The activity and molecular forms of acetylcholinesterase (AChE) were characterized in tissues of the carp (Cyprinus carpio). Tissue AChE activity was determined in response to specific inhibitors (ethopropazine, BW 284 C51) or pesticides (CuSO4, paraquat (PQ), methidathion (MD)). The highest AChE activity was found in the serum (878 +/- 100 U/liter), followed by the brain (113 +/- 12 U/liter), heart (89 +/- 6 U/liter), and trunk muscle (35 +/- 5 U/liter). Experiments with specific choline esterase inhibitors revealed a very low amount of pseudocholinesterase in all tissues studied. The ratio of the membrane-bound to the cytoplasmic-free AChE molecular forms was increased in the order of brain, trunk muscle, and heart. In sera of fish treated with MD (2 ppm) there was an 80% inhibition of AChE lasting for 2 weeks. Treatment with CuSO4 or PQ (both 5 ppm) led to a 50% decrease in the serum AChE activity followed by a transient increase over the control level. After 2 weeks of chronic treatment, AChE activity in fish exposed to CuSO4 returned to the control level, whereas in fish treated with PQ an elevated level (130% when compared to the control level) of enzyme activity was found. Our present experimental data indicate that pesticides occurring in natural waters not only inhibit AChE activity in fish but may influence the resynthesis of the enzyme as well.
ESTHER : Szabo_1992_Ecotoxicol.Environ.Saf_23_39
PubMedSearch : Szabo_1992_Ecotoxicol.Environ.Saf_23_39
PubMedID: 1375147

Title : Glial cells in coculture can increase the acetylcholinesterase activity in human brain endothelial cells - Pakaski_1992_Neurochem.Int_21_129
Author(s) : Pakaski M , Kasa P
Ref : Neurochem Int , 21 :129 , 1992
Abstract : The elements of the cholinergic system (acetylcholinesterase and choline acetyltransferase) and butyrylcholinesterase were studied in human cortical capillary samples, brain-derived endothelial cell cultures and glial cell cultures. It was shown that the elements of the cholinergic system are present in the microvessels, but the choline acetyltransferase activity may be due to contamination with cholinergic nerve terminals since no choline acetyltransferase could be demonstrated in endothelial cell cultures. The present results revealed that the activity of acetylcholinesterase is reduced in the cortical endothelial cell cultures after longer culture times, while butyrylcholinesterase activity is not altered. In a system where endothelial cells were cocultured with embryonic human brain astroglial cells for 12 days in vitro, the acetylcholinesterase activity was increased 2-fold. These results support a glial influence on the enzyme activity of the cerebral endothelium
ESTHER : Pakaski_1992_Neurochem.Int_21_129
PubMedSearch : Pakaski_1992_Neurochem.Int_21_129
PubMedID: 1303138

Title : Endothelial cells from human fetal brain microvessels may be cholinoceptive, but do not synthesize acetylcholine - Kasa_1991_J.Neurochem_56_2143
Author(s) : Kasa P , Pakaski M , Joo F , Lajtha A
Ref : Journal of Neurochemistry , 56 :2143 , 1991
Abstract : Brain homogenate, cerebral microvessels, and endothelial cells (ECs) were prepared from 15-18-week-old human fetuses and analyzed biochemically for the presence of elements of the cholinergic system [acetylcholinesterase (AChE), choline acetyltransferase (ChAT), and butyrylcholinesterase]. The ECs were cultured, and their purity was checked by light microscopic immunohistochemistry with the application of anti-human factor VIII and glial fibrillary acidic protein. The highest activity of ChAT was found in the brain homogenate and the lowest in the microvessel fraction. No ChAT activity could be detected in the cultured ECs, despite the presence of high AChE activity. It is suggested that human brain ECs may be under the control of acetylcholine released from cholinergic nerve terminals but that the cells do not produce the transmitter itself. In coculture experiments, when ECs were plated on the upper surface of a polycarbonate filter and glial cells were seeded on the lower surface, the electric resistance was measured. During the culture period, the resistance first increased up to 5 days in vitro (297 +/- 17 ohm.cm2) but later gradually declined. These results demonstrate that human ECs cocultured with glial cells provide a useful model for study of the function of the blood-brain barrier in vitro.
ESTHER : Kasa_1991_J.Neurochem_56_2143
PubMedSearch : Kasa_1991_J.Neurochem_56_2143
PubMedID: 2027020

Title : Effects of ischemia on cholinergic neurotransmission and electrolyte content in newborn pig lumbar spinal cord - Tekulics_1990_Life.Sci_46_811
Author(s) : Tekulics P , Rakonczay Z , Szerdahelyi P , Kasa P , Gulya K
Ref : Life Sciences , 46 :811 , 1990
Abstract : The biochemical changes of the elements of cholinergic neurotransmission (choline acetyltransferase, ChAT; acetylcholinesterase, AChE; butyrylcholinesterase, BCHE; and muscarinic cholinergic receptors, mAChR) as well as the electrolyte content were studied in ischemic lumbar spinal cord segments of newborn pigs. Ischemia was elicited by ligating the aorta for 30 min. Although no significant changes were observed in the sodium, potassium and calcium content of ischemic spinal cords, the calcium content was slightly elevated, to 119.3% of the control value. Whereas significant depletions were observed in both AChE and ChAT activities (to 69.1 and 87.7% of the control value, respectively), there was no significant change in BCHE activity as compared to the control value. The mAChR were also decreased, from 33.25 +/- 2.2 to 27.18 +/- 1.9 fmol/mg protein, while the Kd value was not significantly altered. It is concluded that even a relatively brief interruption of the oxygen supply can cause severe damage in the lumbar spinal cord of the newborn pig, affecting the cholinergic neurotransmission elements. This animal model might be suitable for studying the effects of hypoxia in newborns and children during chest operations involving the descending aorta.
ESTHER : Tekulics_1990_Life.Sci_46_811
PubMedSearch : Tekulics_1990_Life.Sci_46_811
PubMedID: 2157120

Title : Effects of methidathion on distribution of molecular forms of acetylcholinesterase in carp, as revealed by density gradient centrifugation - Nemcsok_1990_Pestic.Biochem.Physiol_37_140
Author(s) : Nemcsok J , Rakonczay Z , Kasa P , Asztalos B , Szabo A
Ref : Pesticide Biochemistry and Physiology , 37 :140 , 1990
Abstract : The effects of the insecticide methidathion (MD) (S-2,3-dihydro-5-methoxy-2-oxo-1,3,4-thiodiazol-3-yl-methyl-O,O-dimethyl-phosphodithioate) were studied on the molecular forms of acetylcholinesterase (AChE, EC 3.1.1.7) in the brain and liver in carp. Both organs contain three different molecular forms: G1, G4, and A12. During exposure of fish to 2 ppm MD in vivo, the enzyme activity decreased significantly in the tissues investigated. Moreover, the relative distribution of the AChE molecular forms changed compared to that in the control animals. There was a significant decrease in the G1 form and an increase in the G4 form in the brain, while in the liver there was a decrease in the G4 form and an increase of about 50% in the G1 form. The results suggest that the investigation of fish AChE molecular forms could contribute to an understanding of fish AChE at a molecular level and emphasize the importance of in vivo and in vitro approaches in assessing chemical effects and their potential hazards in the aquatic environment.
ESTHER : Nemcsok_1990_Pestic.Biochem.Physiol_37_140
PubMedSearch : Nemcsok_1990_Pestic.Biochem.Physiol_37_140
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Title : The Role of Glial Cells in Neuronal Acetylcholine Synthesis -
Author(s) : Kasa P
Ref : Advances in Behavioral Biology , 30 :907 , 1986
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Title : Ethylcholine mustard aziridinium blocks the axoplasmic transport of acetylcholinesterase in cholinergic nerve fibres of the rat - Kasa_1985_Histochem_83_343
Author(s) : Kasa P , Hanin I
Ref : Histochemistry , 83 :343 , 1985
Abstract : A cholinotoxin, ethylcholine mustard aziridinium ion, (AF64A) specifically and irreversibly blocks the intraaxonal transport of acetylcholinesterase in the rat. Impairment of the transport of this enzyme in the septo-hippocampal cholinergic fibres and in the sciatic nerve has been studied, using different doses of AF64A. It is demonstrated that the effect on the axonal transport is dose-dependent, but is not related to the mode of drug application. AF64A thus may exert its neurotoxic effects on cholinergic neurons at several target sites of action. In addition to the localized presynaptic mechanisms, it may also be compromising cholinergic function by inhibiting axonal transport in vivo.
ESTHER : Kasa_1985_Histochem_83_343
PubMedSearch : Kasa_1985_Histochem_83_343
PubMedID: 2415497

Title : Effects of the cholinotoxin, AF64A, on neuronal trace-metal distribution in the rat hippocampus and neocortex - Szerdahelyi_1984_Histochem_81_497
Author(s) : Szerdahelyi P , Kasa P , Fisher A , Hanin I
Ref : Histochemistry , 81 :497 , 1984
Abstract : Ethylcholine mustard aziridinium ion (AF64A) is a neurotoxin which is specific for cholinergic nerve terminals. Besides its effects on elements of the acetylcholine system, we observed that, after 2 and 8 days, a single 20-nmol intracerebroventricular dose altered the Timm's staining of certain regions of the central nervous system and reduced the tissue levels of trace metals. In the hippocampal formation, there was a considerable decrease in the staining of the neuropil of the stratum radiatum and stratum oriens, which contain cholinergic nerve terminals. A reduction in staining was also demonstrated in the perikarya of cortical pyramidal cells. The diminished trace-metal level in both regions was confirmed by quantitative measurements of zinc and copper levels. A similar reduction was not observed at a lower dose (8 nmol) of the cholinotoxin. The results led to the conclusion that AF64A may cause the decrease of the trace-metal content of the postsynaptic neurons through an indirect mechanism.
ESTHER : Szerdahelyi_1984_Histochem_81_497
PubMedSearch : Szerdahelyi_1984_Histochem_81_497
PubMedID: 6549180

Title : Poster 51. Change in the distribution of acetylcholinesterase molecular forms in the peripheral nerves of rabbits with experimental allergic neuritis -
Author(s) : Rakonczay Z , Molnar GK , Kasa P
Ref : In: Cholinesterases, fundamental and applied aspects : proceedings of the Second International Meeting on Cholinesterases , (Brzin M, Barnard EA, Sket D, Eds) De Gruyter , 1984
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Title : Histochemistry of choline acetyltransferase -
Author(s) : Kasa P
Ref : Cholinergic.Mechanisms, Raven Press :271 , 1975
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Title : Transport of choline acetyltransferase and acetylcholinesterase in the rat sciatic nerve, a biochemical and electron histochemical study -
Author(s) : Kasa P , Mann SP , Karcsu S , Toth L , Jordan S
Ref : Journal of Neurochemistry , 21 :431 , 1973
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Title : Localization of choline acetyltransferase -
Author(s) : Kasa P , Mann SP , Hebb CO
Ref : Nature , 226 :812 , 1970
PubMedID: 4192205

Title : Localization of choline acetyltransferase. Ultrastructural localization in spinal neurones -
Author(s) : Kasa P , Mann SP , Hebb CO
Ref : Nature , 226 :814 , 1970
PubMedID: 4192206

Title : A possible histochemical method for the localization of choline acetyltransferase -
Author(s) : Hebb CO , Kasa P , Mann SP
Ref : Journal of Physiology , 208 :1P , 1970
PubMedID: 5499759

Title : The correlation between choline acetyltransferase and acetylcholinesterase activity in different areas of the cerebellum of rat and guinea pig -
Author(s) : Kasa P , Silver A
Ref : Journal of Neurochemistry , 16 :386 , 1969
PubMedID: 5795591

Title : Electron histochemical evidence of different types of mossy fibre endinus in the cerebellar cortex -
Author(s) : Kasa P
Ref : Experientia , 25 :740 , 1969
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Title : Ultrastructural localization of acetylcholinesterase in the cerebellar cortex with special reference to the intersynaptic organelles -
Author(s) : Kasa P
Ref : Histochemie , 14 :161 , 1968
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Title : Acetylcholinesterase transport in the central and peripheral nervous tissue, the role of tubules in the enzyme transport -
Author(s) : Kasa P
Ref : Nature , 218 :1265 , 1968
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Title : ACHE synthesis in cholinergic neurons, electron histochemistry of enzyme translocation -
Author(s) : Kasa P , Csillik B
Ref : Histochemie , 12 :175 , 1968
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Title : Electron microscopie localisation of acetylcholinesterase in the superior cervical ganglion of the rat -
Author(s) : Kasa P , Csernovszky E
Ref : Acta Histochemica , 28 :274 , 1967
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Title : Electron microscopie localization of cholinesterase by a copper-lead-thiocholine technique -
Author(s) : Kasa P , Csillik B
Ref : Journal of Neurochemistry , 13 :1345 , 1966
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Title : Histochemical and ultrastructural alterations in the isolated archicerebellum of the rat -
Author(s) : Kasa P , Csillik B , Joo F , Knyihar E
Ref : Journal of Neurochemistry , 13 :173 , 1966
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Title : Cholinergic excitation and inhibition in the cerebellar cortex -
Author(s) : Kasa P , Csillik B
Ref : Nature , 208 :695 , 1965
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Title : Histochemical localization of acetylcholinesterase in the cat cerebellar cortex -
Author(s) : Kasa P , Joo F , Csillik B
Ref : Journal of Neurochemistry , 12 :31 , 1965
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