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  • 1
    Digitale Medien
    Digitale Medien
    Springer
    BioMetals 11 (1998), S. 383-397 
    ISSN: 1572-8773
    Schlagwort(e): Ca 2+ -binding S100 proteins ; EF-hand ; protein structures ; Ca 2+ ; Zn 2+ ; Cu 2+
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Abstract S100 proteins (16 members) show a very divergent pattern of cell- and tissue-specific expression, of subcel-lular localizations and relocations, of post-translational modifications, and of affinities for Ca 2+ , Zn 2+ , and Cu 2+ , consistent with their pleiotropic intra- and extracellular functions. Up to 40 target proteins are reported to interact with S100 proteins and for S100A1 alone 15 target proteins are presently known. Therefore it is not surprising that many functional roles have been proposed and that several human disorders such as cancer, neurodegenerative diseases, cardiomyopathies, inflammations, diabetes, and allergies are associated with an altered expression of S100 proteins. It is not unlikely that their biological activity in some cases is regulated by Zn 2+ and Cu 2+ , rather than by Ca 2+ Despite the numerous putative functions of S100 proteins, their three-dimensional structures of, e.g., S100B, S100A6, and S100A7 are surprisingly similar. They contain a compact dimerization domain whose conformation is rather insensitive to Ca 2+ binding and two lateral a-helices III and III, which project outward of each subunit when Ca 2+ is bound. Target docking depends on the two hydrophobic patches in front of the paired EF-hand generated by the binding of Ca 2+. The selec-tivity in target binding is assured by the central linker between the two EF-hands and the C-terminal tail. It appears that the S100-binding domain in some target proteins contains a basic amphiphilic a-helix and that the mode of interaction and activation bears structural similarity to that of calmodulin.© Kluwer Academic Publishers
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    ISSN: 1432-0878
    Schlagwort(e): Auditory system ; Vocal motor system ; Parvalbumin ; Cytochrome oxidase ; 2-Deoxyglucose ; Calcium ; Plasticity ; CNS ; Song birds ; Zebra finch
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Summary The auditory and vocal motor systems of adult zebra finches were investigated 1) immunocytochemically for the distribution of the Ca2+-binding protein parvalbumin, 2) for the activity of the respiratory enzyme cytochrome oxidase, and 3) for the uptake of 2-deoxyglucose. All auditory nuclei (field L, nucleus ovoidalis, ansa lenticularis, nucleus spiriformis lateralis, nucleus mesencephalicus lateralis-pars dorsalis, nucleus tegmenti pedunculo-pontinus) and vocal motor nuclei (nucleus magnocellularis of the anterior neostriatum, area X, nucleus interfacialis, hyperstriatum ventrale-pars caudalis, nucleus robustus archistriatalis, nucleus intercollicularis) showed high levels of parvalbumin and cytochrome oxidase. Auditory nuclei in addition showed high spontaneous 2-deoxyglucose uptake, while the vocal motor nuclei either remained at background intensity (nucleus magnocellularis of the anterior neostriatum, hyperstriatum ventrale-pars caudalis, nucleus interfacialis and nucleus intercollicularis) or even below background levels (area X, nucleus robustus archistriatalis). Cytochrome oxidase activity supposedly reflects the energy demand of various aspects of metabolism, while 2-deoxyglucose uptake is primarily related to the demands of electrical activity and the Na+-K+ pump. Consequently, it is argued (i) that the congruently high cytochrome oxidase activity and 2-deoxyglucose uptake in the auditory system are due to the high spontaneous electrical activity of neurons, and (ii) that high cytochrome oxidase activity in vocal motor nuclei is related to other than electrical events since 2-deoxyglucose uptake is low. There is evidence of Ca2 + potentials in some parvalbumin-positive neuron types. Ca2+ potentials must lead to Ca2+ flooding of the cytoplasm which could be buffered by parvalbumin thus preventing interference with Ca2+ dependent metabolic reactions or shuttling the ion to sites of such reactions. The unique morphological plasticity reported from the parvalbumin-positive vocal motor nuclei may put a strain on microtubular transport which is Ca2+ dependent. This leads to the idea that parvalbumin reflects local buffering and redistribution mechanisms for Ca2+, and that cytochrome oxidase indicates the underlying energy demand.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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