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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 77 (1989), S. 449-454 
    ISSN: 1432-0533
    Keywords: Ca2+-ATPase ; Blood-brain barrier (BBB) ; Brain edema ; Capillary ; Astrocyte
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary To investigate the functional relationship between astrocytes and Ca2+-ATPase of cerebral capillary endothelial cells (capillary Ca2+-ATPase), cold lesions were produced and the cytochemical reaction (CR) for Ca2+-ATPase activity and morphological changes of astrocytes were chronologically studied. Under normal conditions, CR for capillary Ca2+-ATPase activity was mild. However, at 20 min after the operation, astrocytic end-feet embracing the capillaries were swollen, and CR was moderate. Deposits of slightly coarsened reaction product (RP) appeared and accumulated on the abluminal surface. CR became stronger as edema fluid accumulated. At 4, 7 and 15 days, detachment of the astrocytic processes from the capillary wall was observed and in the uncovered capillaries, CR was intense, especially on the abluminal surface. It could be thus possible that the enzyme was related to the blood-brain barrier (BBB). At 2 months, reactive astrocytes has recovered lesionresistant capillaries. CR was mild and its associated deposits were coarser, the number decreasing on both surfaces. The nature and localization of the deposits of RP in the scar were different from those under normal conditions, possibly due to the functional differences between normal and reactive astrocytes in the BBB. CR was mild in association with astrocytes embracing the capillary wall and was intense without astrocytes. Therefore, it might be possible that astrocytes exerted certain effects on capillary Ca2+-ATPase activity in relation to BBB function.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 78 (1989), S. 449-454 
    ISSN: 1432-0533
    Keywords: Astrocyte ; Reactive astrocyte ; Ca2+-ATPase ; Ultracytochemistry-Brain edema
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Ca2+-ATPase activity on the astrocyte plasma membrane was investigated ultracytochemically, using the lead salt technique. Normal astrocytes showed a weak cytochemical reaction for Ca2+-ATPase activity, deposits of the reaction product being small. At 7 and 15 days after cold lesioning, reactive astrocytes apparently in the process of repair of the edematous lesion were observed; these demonstrated an intense cytochemical reaction for Ca2+-ATPase activity in their plasma membranes facing the extracellular fluid, with reaction product accumulation. At 2 months, the lesion had progressed to glial scars containing sporadic microcysts. The reactive astrocytes surrounding the microcysts demonstrated a moderate cytochemical reaction for Ca2+-ATPase activity in their free plasma membranes, whereas those arranged in a cell-to-cell pattern showed little reaction product in their plasma membranes. In conclusion, a more intense cytochemical reaction was always observed in the free plasma membrane of reactive astrocytes.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 58 (1982), S. 237-242 
    ISSN: 1432-0533
    Keywords: Membrane specialization ; Globoid cell ; Astrocyte ; Globoid cell leukodystrophy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Subplasmalemmal linear densities (Yajima et al. 1977 a) were the membrane specializations observed in globoid cells in globoid cell leukodystrophy (GLD) and in the cells of the mononuclear phagocytic system (Kawanami et al. 1980). In the spinal cord of the twitcher mouse, an authentic murine model of GLD, somewhat similar membrane specializations were noted in astrocytes, and on some occasions, a spot desmosome-like cellular contact was observed between globoid cells, which were likely to be mesodermal in origin, and astrocytes, which are of ectodermal origin. Possible significance of such apparent cellular contact is discussed briefly.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Molecular Cell Research 1093 (1991), S. 95-101 
    ISSN: 0167-4889
    Keywords: (Pig epidermis) ; Adenylate cyclase ; Agonist ; Desensitization ; Phorbol ester
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1617-4623
    Keywords: Key words cAMP level ; Adenylate cyclase ; CRP ; Phosphorylation state ; IIAGlc
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The cellular cAMP level is markedly down-regulated by cAMP receptor protein (CRP) in Escherichia coli. CRP regulates adenylate cyclase both at the level of transcription of its structural gene cya and at the level of enzyme activity. We established a method to determine the phosphorylation state of IIAGlc, the glucose-specific phosphotransferase protein, in intact cells. We found that IIAGlc exists predominantly in the unphosphorylated form in wild-type cells growing in LB medium, while it is largely phosphorylated in crp or cya cells. Disruption of the ptsG gene that codes for the membrane component of the major glucose transporter (IICBGlc), and/or the fruF gene coding for FPr (fructose-specific hybrid phosphotransferase protein), did not affect the phosphorylation state of IIAGlc. When IICBGlc was overproduced in the presence of glucose, the levels of both cAMP and phosphorylated IIAGlc in crp cells were concomitantly decreased to wild-type levels. In addition, when His-90 in IIAGlc was replaced by glutamine, both phosphorylation of IIAGlc and the overproduction of cAMP in crp cells were eliminated. We also found that extracts of crp + cells markedly stimulate dephosphorylation of IIAGlc-P in vitro. We conclude that CRP-cAMP down-regulates adenylate cyclase primarily by reducing the level of phosphorylated IIAGlc. The data suggest that unspecified proteins whose expression is under the control of CRP-cAMP are responsible for this regulation.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-0533
    Keywords: Key wordsα-Synuclein ; Astrocyte ; Oligodendrocyte ; Glial inclusion ; Parkinson’s disease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The precursor of the non-Aβ component of Alzheimer’s disease amyloid (NACP), also called α-synuclein, is a major component of Lewy bodies in Parkinson’s disease (PD) as well as of neuronal and oligodendroglial cytoplasmic inclusions in multiple system atrophy. We previously reported argyrophilic, tau-negative glial inclusions in the midbrains of patients with PD and have now conducted immunocytochemical and ultrastructural examinations. The PD glial inclusions also are immunoreactive for NACP/α-synuclein, but not for β-synuclein, and ultrastructurally are composed of filamentous structures about 25–40 nm in diameter. Double immunolabeling showed that the inclusions were present in both astrocytic and oligodendroglial cells. They were located within the substantia nigra in 13 of 30 patients with PD and outside the nigra in 24. The number of inclusions was correlated with the severity of nigral neuronal loss. These findings indicate that abnormal accumulation of NACP/α-synuclein in glial cells is a pathological feature of PD related to its progression.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Archives of dermatological research 288 (1995), S. 24-30 
    ISSN: 1432-069X
    Keywords: Key words G-protein ; Adenylate cyclase ; Phorbol ; esters ; Densensitization ; Keratinocytes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Although the protein kinase C (PKC) activator, phorbol 12-myristate 13-acetate (PMA) has been known to induce heterologous desensitization of the epidermal adenylate cyclase, the precise mechanism of PMA action remains unknown. Effects of PMA on the receptor-G-protein-adenylate cyclase system of fetal rat skin keratinocytes (FRSK) were investigated. Choleratoxin catalysed the ADP ribosylation of 45 kDa and 52 kDa membrane proteins and islet activating protein (IAP) catalysed the ADP ribosylation of a 40 kDa membrane protein. Incubation of FRSK with PMA decreased the cholera toxin-catalysed ADP ribosylation of the membrane protein, but not the IAP-catalysed ADP ribosylation. The effect of PMA on the cholera toxin-catalysed ADP ribosylation was inhibited by the PKC inhibitor, H-7 (1-(5-isoquinolinesulfonyl)-2-methyl piperazine dihydrochloride). 1-Oleoyl-2-acetylglycerol (OAG), a membrane-permeable diacylglycerol analogue, also decreased the cholera toxin-catalysed ADP ribosylation, but 4- O -methyl PMA, a very weak PKC activator, had no effect. Keratinocytes are known to express the guanine nucleotide binding proteins, Gsα, Gi2α and Gi3α. Immunoblot analysis of the PMA-treated FRSK showed no detectable difference in the amount of Gsα, Gi2α, Gi3α or the β subunit of the G-protein. PMA significantly decreased the β-adrenergic adenylate cyclase response and cholera toxin-induced cyclic AMP accumulation, while it markedly increased forskolin-induced cyclic AMP accumulation. These results indicate that phorbol esters affect the stimulatory guanine nucleotide binding protein (Gs) of FRSK via a PKC-dependent pathway.
    Type of Medium: Electronic Resource
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