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  • Immunocytochemistry  (2)
  • Springer  (2)
  • American Geophysical Union (AGU)
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  • Springer  (2)
  • American Geophysical Union (AGU)
  • Elsevier  (1)
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 233 (1983), S. 99-111 
    ISSN: 1432-0878
    Keywords: Neurosecretion ; Vasopression ; Osmotic stress ; RIA ; Immunocytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A correlative radioimmunoassay (RIA) and immunocytochemical (ICC) study was carried out on vasopressin (VP) distribution and content in brains of normal and 3-day water-deprived rats. By RIA there were statistically significant differences in brain VP per pg/mg between normal and osmotically stressed specimens in hypothalamus (338.4 versus 134.4), thalamus (4.8 versus 0.9), septum (18.0 versus 3.4), striatum (1.6 versus 0.7) and amygdala (17.3 versus 1.3), but not in other brain regions measured. Pituitary VP decreased from 71.1 to 8.7 ng/mg, and plasma VP rose from 3.6 to 19.3 pg/ml during water deprivation. Application of the peroxidase-anti-peroxidase ICC method of Sternberger to vibratome sections showed that VP-immunoreactivity in dehydrated specimens decreased in perikarya of paraventricular nucleus and suprachiasmatic nucleus, while intrahypothalamic immunoreactive magnocellular fibers appeared more conspicuous due to proliferation of large Herring bodies. In extrahypothalamic sites VP-immunoreactivity in water-deprived rats was visibly reduced in periventricular thalamus and septum. Thus it is apparent that both intra- and extrahypothalamic VP are affected by osmotic stress, and these results are discussed within the context of current ideas relating to co-activation of neurosecretory cells that project to different sites.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0878
    Keywords: Newborn rat epidermis ; Soluble epidermal protein ; Thiolproteinase inhibitor ; Immunocytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Subcellular distribution of a thiol-proteinase inhibitor protein was determined in the epidermis of the newborn rat by light and electron microscopy. This protein was highly soluble in basal cells and concentrated on ribosomes in the perinuclear region. Solubility in Tris buffer decreased in granular and cornified cells in which the protein appeared on polysomes which were attached on other cellular structures such as dense homogenous deposits and tonofilaments. The protein also appeared to be deposited on the plasma membrane and became insoluble in Tris buffer at 37° C, but solubilized in 1 M phosphate buffer. Location of the protein around keratohyalin granules or by the plasma membrane suggested that the inhibitor protein bound to cysteinerich protein of the epidermis with or without forming a thiol-proteinase inhibitor complex. The thiol-proteinase inhibitor protein seems to contribute to epidermal cell differentiation at multiple points through changes in its solubility and subcellular localization from basal cells to cornified cells.
    Type of Medium: Electronic Resource
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