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  • Adenylate cyclase  (3)
  • Alzheimer's disease  (3)
  • Amyotrophic lateral sclerosis  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Desensitization of the epidermal adenylate cyclase system: agonists and phorbol esters desensitize by independent mechanisms
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Molecular Cell Research 1093 (1991), S. 95-101 
    Details
    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
    URL: http://dx.doi.org/10.1016/0167-4889(91)90143-L
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  • 2
    Electronic Resource
    Electronic Resource
    Hereditary dentatorubral-pallidoluysian atrophy: ubiquitinated filamentous inclusions in the cerebellar dentate nucleus neurons (1998)
    Springer
    Acta neuropathologica 95 (1998), S. 479-482 
    Details
    ISSN: 1432-0533
    Keywords: Key words Dentatorubral-pallidoluysian atrophy ; Cerebellar dentate nucleus neuron ; Skein-like inclusion ; Ubiquitin ; Amyotrophic lateral sclerosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We examined the cerebellar dentate nucleus (CDN) in 16 patients with hereditary dentatorubral-pallidoluysian atrophy (DRPLA), one of the neurodegenerative diseases caused by expansion of a CAG repeat encoding a polyglutamine tract in the disease protein. In all patients, some CDN neurons were found to contain ubiquitinated filamentous inclusions in their cytoplasm. On hematoxylin and eosin preparations, these filamentous inclusions were eosinophilic, basophilic or amphophilic, and were often found in areas of pale cytoplasm. Electron microscopy revealed that they consisted of bundles of filaments that were somewhat thicker than neurofilaments. These features of the present inclusions were indistinguishable from those of skein-like inclusions (SLI) previously described in the lower motor neurons in sporadic amyotrophic lateral sclerosis. We conclude that SLI can also occur in the CDN in DRPLA and believe that they reflect a characteristic pathological process in this disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004010050828
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Clarke's column in sporadic amyotrophic lateral sclerosis (1992)
    Springer
    Acta neuropathologica 84 (1992), S. 465-470 
    Details
    ISSN: 1432-0533
    Keywords: Amyotrophic lateral sclerosis ; Clarke's column ; Bunina body ; Spheroid ; neuronal loss
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Histological, ultrastructural and morphometrical observations on Clarke's column were carried out in 18 patients with sporadic amyotrophic lateral sclerosis (ALS) and 15 age-matched control subjects. Of the 18 ALS patients 6 had been on a respirator before death. Bunina bodies were found in the neuronal cytoplasm in 7 of the 12 non-respirator-supported ALS patients and in 3 of the 6 respirator-supported patients. The number of spheroids was significantly higher in the non-respirator-supported patients (P〈0.01) than in the control subjects; however, the number in the respirator-supported patients was about equal to that in the controls. The number of neurons in Clarke's column in the non-respirator-supported ALS patients was not reduced, but in the respirator-supported patients they tended to disappear with time after respiratory support. These findings suggest that Clarke's column neurons are also involved primarily in the disease process in sporadic ALS. However, they may begin to disappear only after the patients require respiratory support.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00304464
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  • 4
    Electronic Resource
    Electronic Resource
    The intermediolateral nucleus in sporadic amyotrophic lateral sclerosis (1993)
    Springer
    Acta neuropathologica 86 (1993), S. 190-192 
    Details
    ISSN: 1432-0533
    Keywords: Amyotrophic lateral sclerosis ; Intermediolateral nucleus ; Quantitative examination ; Bunina body ; Neuronal loss
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Histological and morphometrical observations of the intermediolateral nucleus (IML) at the levels of the upper and lower thoracic segments (T2 and T9) were carried out in 18 patients with sporadic amyotrophic lateral sclerosis (ALS) and 15 age-matched control subjects. Of the 18 ALS patients 6 had been on a respirator before death. No Bunina bodies were found in the IML neurons in either the ALS patients or the control subjects. Only a small number of spheroids were encountered rarely in the IML in both the patients and controls. The number of neurons in the IML in the non-respirator-supported ALS patients were reduced at T2, but well preserved at T9 compared with the control subjects. In the respirator-supported ALS patients, there was a marked reduction of IML neurons at both T2 and T9. Considering the absence of direct synaptic contacts with anterior horn cells, these neurons, without the formation of Bunina bodies, appeared to be involved primarily in the disease process in sporadic ALS.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00334889
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  • 5
    Electronic Resource
    Electronic Resource
    Immunohistological study on brains of Alzheimer's disease using antibodies to fetal antigens, C-series gangliosides and microtubule-associated protein 5 (1991)
    Springer
    Acta neuropathologica 81 (1991), S. 626-631 
    Details
    ISSN: 1432-0533
    Keywords: C-series gangliosides ; Microtubule-associated protein 5 ; Fetal antigen ; Alzheimer's disease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary An immunohistological study of Alzheimer's brains was performed using antibodies to C-series gangliosides and microtubule-associated protein 5 (MAP5), and their staining patterns were compared with those of antibodies to tau and β-amyloid precursor protein. Antibodies to C-series gangliosides and MAP5, both of which are known to preferentially expressed in the fetal brains, immunostained dystrophic neurites of senile plaques, neurofibrillary tangles and neuropil threads abundant in 3rd and 5th layers in the cerebral cortex, all of which are considered to be pathological hallmarks of Alzheimer's disease. The immunostaining patterns of these structures by antibodies to C-series gangliosides and MAP5 were similar to those by the antibody to tau. These three antibodies also immunostained some neurons in Alzheimer's brain, although their staining patterns were slightly different from one another; i.e., both diffuse and granular patterns were seen by the antibody to tau, but only granular pattern by the antibodies to C-series gangliosides and MAP5. These neurons immunostained by these three types of antibodies appeared to be the precursors of the classical neurofibrillary tangles, as positively stained neurons were not seen in the brains of non-demented cases. The presence of fetal antigens such as the C-series gangliosides and MAP5 in Alzheimer's brain may suggest that regeneration or sprouting of neurons is ongoing in association with the re-induction of gene expression characteristic for the brain in the early stage of development.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00296372
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  • 6
    Electronic Resource
    Electronic Resource
    Establishment of a monoclonal antibody against senile plaques and its application for immunohistological and immunoelectron microscopical studies in the brain of the elderly (1989)
    Springer
    Acta neuropathologica 79 (1989), S. 44-47 
    Details
    ISSN: 1432-0533
    Keywords: Monoclonal antibody ; Senile plaque ; Alzheimer's disease ; Senile dementia of Alzheimer type ; Congophilic angiopathy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary A monoclonal antibody (Am-3) was produced against senile plaques in the brain of a patient with Alzheimer's disease. Am-3 was reactive with senile plaques of typical, primitive and diffuse type not only in the brain used as immunogen, but also those in the brain of 15 out of 25 autopsy cases of the aged people. Moreover, Am-3 was also reactive with granular materials of various sizes scattered in the 1st, 3rd and 4th layers of the cerebral cortices of the cases with severe dementia. Am-3 was also reactive with vessel wall of the congophilic angiopathy. By immunoelectron microscopic examination, Am-3 was positive with amyloid fibril in the core and crown of senile plaques, and in the congophilic angiopathy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00308956
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  • 7
    Electronic Resource
    Electronic Resource
    Protein kinase C-dependent modulation of stimulatory guanine nucleotide binding protein of fetal rat skin keratinocytes (1995)
    Springer
    Archives of dermatological research 288 (1995), S. 24-30 
    Details
    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
    URL: http://dx.doi.org/10.1007/s004030050018
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  • 8
    Electronic Resource
    Electronic Resource
    Deficiency of kallikrein-like enzyme activities in cerebral tissue of patients with alzheimer's disease (1990)
    Springer
    Cellular and molecular life sciences 46 (1990), S. 94-97 
    Details
    ISSN: 1420-9071
    Keywords: Alzheimer's disease ; brain ; proteases ; kallikrein ; prolyl endopeptidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary We examined the changes in the intracerebral activities, at the time of postmortem autopsy, in patients with Alzheimer's disease. When compared with the control group, the activity of kallikrein-like enzyme was significantly decreased, while prolyl endopeptidase activity increased, in the patients group. Aprotinin inhibited 50% of the activity of the former enzyme at 2×10−7M. Taken together with the results of a multivariate study, the above findings may indicate that intracerebral kallikrein deficiency plays an important role in the pathogenesis of Alzheimer's disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01955428
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  • 9
    Electronic Resource
    Electronic Resource
    CRP down-regulates adenylate cyclase activity by reducing the level of phosphorylated IIAGlc, the glucose-specific phosphotransferase protein, in Escherichia coli (1998)
    Springer
    Molecular genetics and genomics 259 (1998), S. 317-326 
    Details
    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
    URL: http://dx.doi.org/10.1007/s004380050818
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