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  • Electronic Resource  (4)
  • 1975-1979  (4)
  • 1977  (4)
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  • Electronic Resource  (4)
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  • 1975-1979  (4)
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  • 1
    Electronic Resource
    Electronic Resource
    Ultrastructural pattern of acetylcholinesterase distribution in the cerebellar cortex of the quail (1977)
    Springer
    Anatomy and embryology 152 (1977), S. 29-41 
    Details
    ISSN: 1432-0568
    Keywords: Cerebellum ; Acetylcholinesterase ; Ultrastructural cytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The ultrastructural localization of acetylcholinesterase (AChE) was studied in the cerebellar cortex of the quail by means of histochemical methods. The greater amount of AChE was detected at level of the molecular layer in the intercellular spaces between parallel fibers and between parallel fibers and dendritic terminals. Many neurons showed intracellular localization of enzyme activity: the AChE positive neurons were all Golgi cells, most stellate and basket cells and different aliquots of Purkinje and granule cells. The enzymatic activity was usually localized in the cisternae of endoplasmic reticulum, in the nuclear envelope (but this last localization was not present in Purkinje cells) and sometimes in the Golgi apparatus; reaction granules were usually scarce in the different dendritic branches ramifying in the molecular layer. On the basis of the ultrastructural pattern of AChE distribution, some considerations are developed on the methodological aspects concerning the reliability of histochemical methods, the differences recorded at light and electron microscope level, the problems related to extracellular localization of enzyme, the difficulty of establishing a precise correlation between AChE localization in a cerebellar neuron and its possible cholinergic and/or cholonoceptive nature.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00341433
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Ultrastructural analysis on acetylcholinesterase localization in the cerebellar cortex of teleosts (1977)
    Springer
    Anatomy and embryology 152 (1977), S. 15-27 
    Details
    ISSN: 1432-0568
    Keywords: Fish cerebellum ; Acetylcholinesterase ; Ultrastructural cytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The histochemical localization of acetylcholinesterase (AChE) was studied by electron microscopy in the cerebellar cortex of the goldfish and the catfish. The patterns of enzyme distribution show noticeable differences in the two teleost species at the level of the corresponding cerebellar structures. Among the most distinctive features in the prevailing intracellular localization of enzyme activity in the goldfish and the prevailing extracellular localization in the catfish in the molecular layer and, to a lesser extent, the granular layer. Only quantitative differences in the ability to synthesize AChE can be recorded among the different cerebellar neurons in the two species, since all these neurons exhibit different amounts of enzyme activity linked to their cytoplasmic structures. Comparing the results obtained with those of previous histochemical, experimental and developmental researches, the hypothesis seems well founded that the embryonic pool of cerebellar neurons is made up to AChE-synthesizing neuroblasts which, during development, lose or maintain to a different degree the mechanisms for AChE synthesis. In addition the light and electron microscope histochemistry reveals at different levels of resolution that the final pattern of AChE distribution in the cerebellar cortex is the sum of different degrees of AChE synthesis by cerebellar neurons and different degrees of enzyme release in extracellular spaces.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00341432
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Cholinesterase patterns in the cerebellum of reptiles (1977)
    Springer
    Histochemistry and cell biology 51 (1977), S. 195-200 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary In the cerebellum of four species belonging to the three main reptilian orders the histochemical localization of cholinesterases has been studied. The use of different substrate-inhibitor combinations permits to record the distribution patterns of acetylcholinesterase and pseudocholinesterase, mainly revealed as butyrylcholinesterase activity. From the neurological point of view it is interesting to note that acetylcholinesterase activity shows three different distribution patterns in reptilian cerebellum, thus confirming the characteristic variability previously noticed in the cerebellar cortex of other vertebrates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00567223
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    The pyridine nucleotide and non-pyridine nucleotide dependence of L-glutamate dehydrogenase in the histochemical system (1977)
    Springer
    Histochemistry and cell biology 53 (1977), S. 117-133 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Under histochemical conditions (fresh frozen sections from liver, kidney and cerebellum of the rat) it was shown that the oxidation of L-glutamic acid was carried out by the NAD-dependent L-glutamate dehydrogenase (E.C. 1.4.1.2) and/or the NAD- or NADP-dependent L-glutamate dehydrogenase (E.C. 1.4.1.3) as well as by an enzyme system which is not dependent on externally added NAD, NADP, FAD, FMN or CoQ10 for activity. This non-pyridine dependent activity was related to the L-glutamate dehydrogenases proper, owing to the following: a) the localization of activity noticed corresponds to that obtained with the NAD- or NADP-containing media, b) the incubation time needed for initial formation of red and blue formazans is similar to that with coenzyme-containing media, c) pre-extraction experiments reveal similarity in enzyme diffusion rates, d) the named activity is influenced by the same agents and to the same extent as the activity obtained by the inclusion of NAD or NADP (e.g. dissociation of the dehydrogenase molecule into subunits due to urea, inhibition of activity due to N-ethyl maleimide and 1.10-phenanthroline, activation due to the allosteric effect of ADP and to high substrate concentration, allosteric inhibition caused by GTP and inhibition caused by α-ketoglutaric acid, no inhibitory effect of KCN), and e) the named activity was not affected by added PMS (excluding activity due to L-aminoacid oxidase). In the in situ localization of enzyme activity it was found that L-glutamate dehydrogenases E.C. 1.4.1.2 and E.C. 1.4.1.3 co-exist in the cells of kidney and cerebellum, while the L-glutamate dehydrogenase E.C. 1.4.1.3 only was present in liver cells. Finally, it was stated that incubation time should be kept as short as possible in order to avoid “Nothing dehydrogenase” reaction as well as inhibition due to accumulation of α-ketoglutaric acid. Only “gel” incubation media should be applied.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00498487
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    Paper (German National Licenses)
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