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  • Calbindin Calcium-binding protein Calcium signalling Nuclear-cytoplasmic partitioning Rat (Sprague Dawley; Wistar) Mouse (CB28-nullmutant; C57BL6)  (1)
  • tooth germ  (1)
  • Springer  (2)
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Schlagwörter
  • Calbindin Calcium-binding protein Calcium signalling Nuclear-cytoplasmic partitioning Rat (Sprague Dawley; Wistar) Mouse (CB28-nullmutant; C57BL6)  (1)
  • tooth germ  (1)
  • calcium  (1)
  • calmodulin  (1)
  • mineralisation  (1)
Verlag/Herausgeber
  • Springer  (2)
Erscheinungszeitraum
  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Calcified tissue international 33 (1981), S. 545-548 
    ISSN: 1432-0827
    Schlagwort(e): calmodulin ; calcium ; mineralisation ; tooth germ
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin , Physik
    Notizen: Summary Calmodulin, a calcium binding protein, has been implicated in the regulation of many calcium-dependent biological processes. Since calcium has an important role in hard tissue genesis, both at intra- and extracellular levels, we anticipate that calcium binding proteins may modulate this process. The present study investigated a mineralising tissue, the rat molar tooth germ, to determine the presence of calmodulin-like activity. A heat-treated cell-free extract of tooth germs provided enhancement of Ca2+-dependent Mg2+-ATPase and 3′:5′-nucleotide phosphodiesterase activity. No enhancement occurred in the absence of calcium or in the presence of trifluoperazine. SDS-polyacrylamide gel electrophoresis of this extract revealed a protein band of approximately 18,000 mol. wt. These findings indicate the presence of calmodulin-like activity in rat molar tooth germs and support the proposal that calcium and calcium binding proteins, in particular calmodulin, have a major regulatory role in the biology of mineralising tissues.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Cell & tissue research 302 (2000), S. 171-180 
    ISSN: 1432-0878
    Schlagwort(e): Calbindin Calcium-binding protein Calcium signalling Nuclear-cytoplasmic partitioning Rat (Sprague Dawley; Wistar) Mouse (CB28-nullmutant; C57BL6)
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Abstract. Recent attempts to understand the function of calbindin28kDa, a widely expressed calcium-binding protein, are confounded by uncertainties over its subcellular location. Using immunoblot analysis of rat brain subregions, we found that the proportion of particulate calbindin28kDa (24–43% of total) was independent of expression level and location. The association of calbindin28kDa with particulate structures appeared to be specific, since it persisted when soluble calbindin28kDa was sequestered by antibodies added before tissue disruption. Moreover, when exogenous calbindin28kDa was added during homogenisation of brain from calbindin28kDa-nullmutant mice, only 10% partitioned to the particulate fraction compared with 33% of endogenous calbindin28kDa in wild-type controls. Confocal microscopy showed that calbindin28kDa was predominantly extranuclear in all tissues analysed (i.e. various brain regions, isolated neurons, and dental enamel epithelium). Dual-label microscopy of neural dense particulate fractions confirmed the extranuclear location of calbindin28kDa and also showed that it partly colocalised with synaptosome and microtubule markers. Using sucrose step gradients, calbindin28kDa was separated from nuclei in parallel with synaptosome and endoplasmic reticulum markers. However, no association with the marker proteins (synaptophysin, ERp29, α/β-tubulin) was detected by calbindin28kDa-immunoprecipitation analysis. Together these findings provide the first consistent picture that calbindin28kDa is located predominantly outside of the nucleus, irrespective of tissue type (neuronal vs non-neuronal) and experimental approach (biochemical vs morphological). The evidence of a substantial, strong and specific association with insoluble cellular structures challenges the widely held view of calbindin28kDa as a mobile calcium buffer, and supports the existence of important alternative roles that involve target proteins.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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