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  • 1995-1999  (4)
  • 1985-1989
  • 1900-1904
  • Arabidopsis  (2)
  • Key words Cell cycle  (2)
  • 1
    ISSN: 1432-0533
    Keywords: Key words Cell cycle ; Ki-67 ; Apoptosis ; Hippocampus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Recent studies, showing that cell cycle-related nuclear proteins p105 and Ki-67 are associated with Alzheimer’s disease (AD)-related cytoskeletal pathology, suggested that these proteins, in addition to their functions in regulating the cell cycle, may have more specialised functions in the adult nervous system. In order to test this hypothesis we studied the expression of the cell cycle-related proteins Ki-67, pCNA and p53 in the hippocampi of 33 subjects, including some with AD or other neurodegenerative disorders and some with no neurological disease. By immunohistochemistry we found nuclear expression of Ki-67 in all subregions of the hippocampus, with the highest levels in the dentate gyrus. Both neurons and glial cells expressed this protein. The proportion of cells positive for Ki-67 and the distribution pattern varied considerably depending on the pathological diagnosis. Neuronal nuclear expression of Ki-67 was increased in AD but was also elevated in young Down’s syndrome subjects and in those with Pick’s disease. Expression of this protein was therefore not AD-specific. We did not find nuclear pCNA or p53 expressed in our patient groups. Contrary to previous studies AD-type neurofibrillary tangles were not labelled with any of the cell cycle markers used. The presence of nuclear Ki-67 expression indicates that some hippocampal neurons are not in the quiescent G0 phase but have re-entered the cell cycle. The absence of nuclear pCNA or p53 suggests that the cycle is arrested in G1. The significance of our findings and their relationship to the production of neurodegenerative cell death via an apoptotic mechanism are discussed.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 94 (1997), S. 6-15 
    ISSN: 1432-0533
    Keywords: Key words Cell cycle ; Alzheimer’s disease ; Down’s syndrome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Using immunohistochemistry we have analysed the nuclear expression of cyclins A, B, D, and E in neurones in the hippocampi of control subjects and patients suffering from various neurodegenerative disorders including Alzheimer’s disease (AD). Cyclins A and D could not be detected but varying degrees of cyclin E expression were found in all patient groups including control subjects. Cyclin B expression was not detected in control subjects but it was expressed in the subiculum, dentate gyrus and CA1 region in patients with AD-type pathology and in the CA2 region and the dentate gyrus of cases of Pick’s disease. These reults suggest that some neurones may have re-entered the cell cycle. The expression of cyclin E without cyclin A expression may indicate an arrest in G1 with the possibility of re-differentiation and exit from G1 to G0. The expression pattern of cyclin E indicates that re-entry into the cell cycle is possible even in control patients, but it is accentuated in patients with AD-related pathology. However, cyclin B was only expressed in AD patients and occurred in areas that were severely affected by pathology. Neurones with cyclin B-reactive nuclei in AD were AT8 positive but did not contain fully developed tangles. In neurones, where cyclin B is expressed, it would appear that the G1/S checkpoint has been bypassed and that the cell cycle is arrested in G2. It is proposed that these neurones do not have the opportunity for subsequent re-differentiation. Since factors known to be present in G2 seem to be responsible for microtubule destabilisation and hyperphosphorylation of tau we hypothesise that cell cycle disturbances may be important in the pathogenesis of AD.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Plant growth regulation 18 (1996), S. 71-77 
    ISSN: 1573-5087
    Keywords: Arabidopsis ; ethylene ; ethylene binding protein ; signal transduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract A review of work carried out on ethylene binding in higher plants is presented. The use of radio-labelled displacement assays has identified specific 14C-ethylene binding in all tissues so far studied. virtually all higher plants studied contain at least two classes of ethylene binding site, one of which fully associates and dissociates in about 2 h and a class of sites that takes up to 20 h to become fully saturated. Although the types of site differ in their rate constants of association they have similar and high affinities for ethylene. A series of Arabidopsis thaliana mutants shown to vary in sensitivity to ethylene have been analysed for 14C-ethylene binding. One mutant, eti 5, which was shown to be unaffected by ethylene concentrations of up to 10,000 μL L−1 was also shown to exhibit reduced binding. In vivo and in vitro studies on pea have shown that ethylene binding can be detected in this tissue. In vitro studies have shown that both membrane and cytosolic fractions contain measurable amounts of ethylene binding. Interestingly, cytosolic ethylene binding consisted only of the fast associating/dissociating type. Developing cotyledons of Phaseolus vulgaris contain a higher concentration of ethylene binding sites that other tissues and only contain the slow dissociating component. These facets have allowed the purification of ethylene binding protein(s) (EBP) from this tissue. The proteins which bind ethylene can be resolved into two bands of 26 and 28 kDa on semi-denaturing PAGE and the proteins appear to be single entities on a 2-D gels. Data will be presented which indicate a possible role for heterotrimetric G-proteins in the early stages of the ethylene signal transduction pathway.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-5087
    Keywords: Arabidopsis ; EBP ; ethylene ; phosphorylation ; receptors ; signal transduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Previous work in our laboratory has demonstrated the existence of high affinity binding sites for the plant growth regulator ethylene. The ethylene binding protein (EBP), from Phaseolus cotyledons, shows many of the characteristics of a functional receptor for ethylene, has been purified on SDS-PAGE and polyclonal antibodies raised in rabbits. Current work involves the investigation of the ethylene transduction signal in a number of ethylene-responsive tissues. In peas, it has been shown that ethylene promotes the phosphorylation of specific proteins of similar molecular weight to the EBP from Phaseolus. Such ethylene-induced phosphorylation can be inhibited by the ethylene antagonist, 2,5-NBD. The antibodies raised to the EBP from Phaseolus have been shown to immunoprecipitate 32P-labelled proteins from membrane protein preparations obtained from pea tissue. Studies on ethylene binding in pea have also shown that the binding of ethylene may be regulated by phosphorylation. Thus, under conditions which promote phosphorylation, binding is inhibited, whereas the reverse is true under conditions which enhance dephosphorylation. Further work is described which examines the effect of protein kinase, protein phosphatase and calcium channel inhibitors on ethylene-induced phosphorylation in peas, together with wild-type (WT) and ethylene insensitive (eti) mutants of Arabidopsis thaliana. The effects of these treatments can be monitored in vivo using the ethylene-induced triple response as a screen. Furthermore, the protein profiles of such treated seedlings can then be compared by labelling protein extracts with 32P and subjecting the samples to SDS-PAGE followed by autoradiography.
    Type of Medium: Electronic Resource
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