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  • Immunocytochemistry  (2)
  • Osteoporosis  (2)
  • Springer  (4)
  • Public Library of Science (PLoS)
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  • Springer  (4)
  • Public Library of Science (PLoS)
  • Elsevier  (1)
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  • 1
    Electronic Resource
    Electronic Resource
    Amylin increases bone volume but cannot ameliorate diabetic osteopenia (1995)
    Springer
    Calcified tissue international 56 (1995), S. 54-61 
    Details
    ISSN: 1432-0827
    Keywords: Diabetes mellitus ; Amylin ; Osteoporosis ; Bone mineral metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract Amylin is normally secreted in a regulated fashion by the pancreatic β-cells in parallel with insulin and has been reported to have bone-conserving properties. Type I diabetes mellitus results in a low-turnover osteopenia in the presence of decreased amylin, which is in contrast to type II diabetes where less bone loss, in the presence of high amylin levels, occurs. We investigated the effects of amylin on bone mineral metabolism in normal and dibetic (streptozotocin-induced) rats, in order to ascertain whether amylin would modify the streptozotocin-induced diabetic osteopenia. Tenweek-old male Sprague-Dawley rats were randomized as follows: group A (n=18) received normal saline; group B (n=18) received amylin; group C, diabetic rats (n=23), received normal saline; and group D, diabetic rats (n=23), received amylin. Amylin (100 pmol/100 g b. w.) was administered by a daily subcutaneus injection. Double calceinlabeled tibiae were removed for histomorphometric analysis followed sacrifice on day 19. Results showed no difference in blood ionized calcium between groups. Blood glucose remained above 600 mg/dl in the diabetic animals and was not affected by the administration of amylin. Serum osteocalcin, insulin-like growth factor-1 (IGF-1), parathyroid hormone (PTH), and 1,25 dihydroxyvitamin D [1,25(OH)2D] were significantly lower in the diabetic rats compared with control group A by day 19. Amylin produced higher levels of serum osteocalcin in group B on day 9 (P〈0.05) compared with controls but returned to control values (group A) by day 19; no such change occurred in the diabetic group. Amylin administration did not influence IGF-1, 1,25(OH)2D or PTH levels compared with the untreated animals. Analysis of the bone histomorphometry showed a low-turnover osteopenia in the diabetic animals. Amylin administration resulted in a significant increase in bone volume in the normal rats, group B (P〈0.05), but was unable to significantly alter this parameter in the diabetic animals. In conclusion, amylin has a beneficial effect on the bone metabolism of the rat in vivo by increasing bone volume. It is, however, unable to overcome the osteopenia caused by streptozotocin-induced diabetes mellitus at the doses used in this study.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00298745
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  • 2
    Electronic Resource
    Electronic Resource
    When should bone density measurements be repeated? (1994)
    Springer
    Calcified tissue international 55 (1994), S. 243-248 
    Details
    ISSN: 1432-0827
    Keywords: Osteoporosis ; Bone density ; Longitudinal studies ; Statistical models ; Decision models
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract We calculated how long to wait before repeating bone mineral density (BMD) measurements to reassess fracture risk. Correlation results from serial measurements of 495 postmenopausal Japanese-American women were used to estimate 95% confidence intervals (CI) for future BMD. After 7 years of follow-up, BMD correlations with the initial measurement ranged between 0.81 and 0.94, depending on age group and measurement site. In this analysis, the period between measurements was defined as the time required for the lower 95% CI to fall below the BMD value corresponding to doubling of fracture risk. Progressive bone loss causes fracture risk to double after 10 years, on average. However, the 95% CIs indicate that a second BMD measurement will detect risk doubling after only 2 or 3 years for some women. For untreated, early postmenopausal women, the period between measurements was approximately 2–5 years for the radius and 4–6 years for the calcaneus, depending on the initial BMD level. The period was approximately 1 year longer for women age 60 and older. Treatments that halve the bone loss rate would increase the period by 1–3 years. In the absence of a second measurement of BMD, the CI will continue to expand with time, corresponding to a wider range in risk between individuals, and a greater proportion of women will be at increased fracture risk. Obtaining a second BMD measurement pinpoints the patient's status within the precision of the measurement. We conclude that repeated BMD measurements will provide a more accurate estimate of fracture risk than a single, baseline measurement.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00310399
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  • 3
    Electronic Resource
    Electronic Resource
    Changes in hypothalamic and extra-hypothalamic vasopressin content of water-deprived rats (1983)
    Springer
    Cell & tissue research 233 (1983), S. 99-111 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00222235
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  • 4
    Electronic Resource
    Electronic Resource
    Cellular localization of thiol-proteinase inhibitor in the epidermis of the newborn rat (1982)
    Springer
    Cell & tissue research 223 (1982), S. 313-323 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF01258492
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