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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 60 (1993), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The distribution of a novel calcium-binding protein with a molecular mass of 18 kDa (CBP-18) in the rat brain was studied by means of biochemical methods and immunohistochemistry on cryostat-sectioned tissue and compared with staining patterns of parvalbumin on adjacent sections. The biochemical analysis revealed high levels of CPB-18 in cortex and cerebellum, low levels in the lungs, and undetectable levels in all other tissues tested. Immunohistochemically, the polyclonal rabbit-derived antibody for CPB-18 showed selective affinity with periglomerular cells and dendrites in the olfactory bulb. Distinct immunostaining of scattered cells and their proximal dendrites was found in the anterior olfactory nuclei and in the perirhinal and entorhinal cortex. Strong staining of neuropil with recognizable but diffusely outlined cells was observed in the retrosplenial cortex, central amygdala, hippocampal rudiment, septum, area preoptica, hypothalamus, colliculus superior, and parabrachial nuclei. The cerebellum showed strong neuropil staining of both the molecular and the granule cell layer. Less intense neuropil staining and a few scattered cells were found in the neocortex, the remaining basal forebrain, and in the entire brainstem. Immunoreactivity was barely detectable or missing in the striatum, the hippocampus, the thalamus, and in the colliculus inferior. Thus, CPB-18 shows a unique staining pattern in the CNS, different from all other Ca2+-binding proteins studied so far.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1468-2494
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Hair treatment chemicals induce sudden and severe hair damage. In this study, we examined cuticles from untreated, permed, and bleached hair that were mechanically discriminated by shaking in water. Both perming and bleaching treatments are prone to easily delaminate cuticles. Confocal microscopy revealed that the cuticles of permed hair were delaminated with larger pieces than untreated ones. On the other hand, the cuticles of bleached hair tend to fragment into small peptides. At the minimum concentration of thioglycolate required to elute S100A3 protein from the endocuticle into the reductive permanent waving lotion, enlarged delaminated cuticle fragments were observed. Although S100A3 is retained in bleached hair, S100A3 is irreversibly oxidized upon bleaching treatment. It is likely that the oxidative cleavage of disulfide bonds between cuticle-constituting proteins, including S100A3, results in the fragile property of cuticles. Here we present a more comprehensive model of hair damage based on a diverse mechanism of cuticle delamination.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    European journal of neuroscience 5 (1993), S. 0 
    ISSN: 1460-9568
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Muscle (body wall, buccal mass, heart) and neural tissue of the marine mollusc Aplysia californica was analysed for calcium-binding proteins using transblot45Ca overlay, Western blotting and two-dimensional polyacrylamide gel electrophoresis, and several low molecular weight calcium-binding proteins were identified. Our results show that Aplysia muscle contains an abundant protein with a Mr of ∼20 000 with strong 45Ca2+-binding ability and cross-reactivity to antibodies against the sarcoplasmic calcium-binding protein isoform II (SCP II) from Amphioxus. Immunocytochemical studies revealed that isoforms of SCP are distributed in a tissue-specific manner, SCP II-like protein is exclusively present in muscle fibres closely associated with the contractile machinery, whereas the isoform I (SCP I-like protein) is exclusively present in a subset of neurons, suggesting a function in their calcium regulation. In addition, a novel 45Ca2+-binding protein of Mr 43 000, pl 4.7, was found in muscle and in neurons. A third protein of Mr 40 000, pl 4.8, cross-reacts with anti-parvalbumin and anti-calbindin D-28K antibodies.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1365-2559
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Aims:  To investigate whether epidermoid cysts, branchial cysts, craniopharyngiomas and cholesteatomas express S100 proteins differentially by immunohistochemical assaying the presence of S100A1, S100A2, S100A3, S100A4, S100A5, S100A6 and S100B.Methods and results:  Immunopositivity/negativity was recorded for each S100 protein in a series of 52 cases consisting of 12 epidermoid cysts, 12 branchial cysts, 15 adamantinomatous craniopharyngiomas and 13 acquired cholesteatomas. Except in the case of the craniopharyngiomas, immunoreactivity was assessed independently in the basal membrane and the basal, the internal and the keratin layers. Our data show that in contrast to S100B, which was rarely expressed, S100A1, S100A2, S100A4 and S100A5 were often present in these four types of epithelial lesions. S100A3 and S100A6 and, to a lesser extent, S100A5 were the most differentially expressed proteins across the different histopathological groups analysed. These three proteins are expressed more often in craniopharyngiomas and cholesteatomas, the two more aggressive types of lesions.Conclusions:  This is the first study to report data on the expression of seven S100 proteins in different histopathological groups of epithelial head and neck lesions, whose precise embryological origins are still a matter of debate. S100 proteins could possibly be used as markers to target this embryonic origin, since our results show that S100A3 and S100A6 (and, to a lesser extent, S100A5) are expressed differentially across these different groups of epithelial lesions.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 297 (1982), S. 504-506 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Newborn and adult Wistar rats of both sexes were killed and various skeletal muscles quickly dissected out, stretched and frozen in isopentane cooled by liquid nitrogen. The muscles were then divided and the respective halves separately processed for histochemical and immunohistochemical ...
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 40 (1984), S. 910-921 
    ISSN: 1420-9071
    Keywords: Parvalbumin ; calcium-binding protein ; muscle ; mammalian
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 34 (1978), S. 38-40 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The localization of several muscle proteins in relaxed and contracted myofibrils is compared. The morphology of the myofibrils and the behavior of these proteins was also investigated under extraction conditions.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Archives of gynecology and obstetrics 216 (1973), S. 51-60 
    ISSN: 1432-0711
    Keywords: Kalbsuterus ; Estradiol-Receptoren ; DMBA ; Kerntransport ; in vitro-Versuche
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung In vitro Experimente mit isolierten Kalbsuteruskernen in Tris-EDTA-Puffer Lösungen oder Uterus Cytosol zeigten, daß sowohl Oestradiol-17β (E 2) wie 7,12-Dimethylbenz(a)antracen (DMBA) in den Kern transportiert wird. Eine spezifische Bindung an Kernreceptoren konnte dabei nicht festgestellt werden. Weiterhin untersuchten wir den gegenseitigen Einfluß von DMBA auf den Transport vonE 2 in den Kern. Dabei fand sich kein Einfluß auf den Transport oder auf die Menge der transportierten Substanzen.
    Notes: Summary In vitro incubation experiments with isolated nuclei from calf uteri in Tris-EDTA buffer or in uterine cytosol have shown, that 7,12-dimethylbenz(a)-anthracene (DMBA) was transported into the nuclei. However, a specific binding to nuclear receptors could not be found. Furthermore the influence of DMBA on the estradiol-17β (E 2) transport into the nuclei and vice versa was studied. In both cases no influence on the transport rate or on the amount of transportedE 2 or DMBA into the nuclei could be demonstrated.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1432-2307
    Keywords: Ca2+-binding proteins ; Parvalbumin ; Calbindin D-28K ; S-100 ; Tumour-associated protein ; Human carcinoma cell lines ; Mouse neuroblastoma ; Rat glioma
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Antisera against the Ca2+-binding proteins parvalbumin, calbindin D-28K, and the S-100 proteins were used to study the distribution of their target proteins in selected human carcinoma (LICR-HN6;Caco-2), mouse neuroblastoma (clone NB-2a), and rat glioma cell lines (clone C-6). Pronounced staining with anti-parvalbumin was observed in the cytosol of all cells as well as in some nuclei, in particular, mitotic nuclei were highly immuno-reactive. Applying light and immune-electron microscopy (colloidal gold labelling) the parvalbumin-fluorescence was associated with filaments in the LICR-HN6 cells. However, this immunoreactivity was not a result of the presence of parvalbumin itself - as shown by biochemical analyses (HPLC, 2D-PAGE) - but was due to the presence of a Ca2+-binding and tumour-associated protein with similar biochemical and immunological properties. S-100 proteins were present in all tumour cell lines but their intracellular distribution was different from calbindin D-28K. Calbindin-immunoreactivity was found on the membranes of the carcinoma cell lines whereas neuroblastoma and glioma cells remained unlabelled. It is suggested that these proteins might be involved in the modulation of the enhanced stimulation of Ca2+-dependent processes occurring in tumour cells.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 293 (1981), S. 300-302 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig. 1 Antibodies against homogeneous rat muscle parvalbumin were raised in rabbits as described elsewhere6'19; the specificity was examined by four methods: a, double immunodiffusion of antiserum (centre well) against (1) total rat muscle extract, (2) muscle parvalbumin and (3) total brain ...
    Type of Medium: Electronic Resource
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