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  • American Physiological Society  (3)
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  • American Physiological Society  (3)
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  • 1
    Online Resource
    Online Resource
    Geldanamycin prevents hemorrhage-induced ATP loss by overexpressing inducible HSP70 and activating pyruvate dehydrogenase
    American Physiological Society ; 2006
    In:  American Journal of Physiology-Gastrointestinal and Liver Physiology Vol. 291, No. 1 ( 2006-07), p. G117-G127
    Details
    In: American Journal of Physiology-Gastrointestinal and Liver Physiology, American Physiological Society, Vol. 291, No. 1 ( 2006-07), p. G117-G127
    Abstract: Hemorrhage in mice results in decreased ATP levels in the jejunum, lung, kidney, heart, and brain but not in liver tissue lysates, albeit at variable levels and time kinetics. The decreased protein expression and activity of pyruvate dehydrogenase (PDH) accounted for the hemorrhage-induced ATP loss. Treatment with geldanamycin (GA; 1 μg/g body wt), a known inducer of heat shock protein (HSP)70, inhibited the hemorrhage-induced ATP loss in the jejunum, lung, heart, kidney, and brain. GA was found to increase PDH protein, preserve PDH enzymatic activity, and inhibit mucosal injury in jejunum tissues. GA-induced HSP70i was found to form complexes with PDH protein. HSP70 gene transfer into intestinal epithelial cells promoted PDH and ATP levels, whereas HSP70 short interfering RNA limited them. We conclude that agents able to increase the expression of HSP70 and PDH may be of value in reducing pathology resulting from hemorrhage-associated ATP loss.
    Type of Medium: Online Resource
    ISSN: 0193-1857 , 1522-1547
    URL: Article
    DOI: 10.1152/ajpgi.00397.2005
    Language: English
    Publisher: American Physiological Society
    Publication Date: 2006
    detail.hit.zdb_id: 1477329-6
    SSG: 12
    Location Call Number Limitation Availability
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    Online Resource
  • 2
    Online Resource
    Online Resource
    Geldanamycin treatment inhibits hemorrhage-induced increases in KLF6 and iNOS expression in unresuscitated mouse organs: role of inducible HSP70
    American Physiological Society ; 2004
    In:  Journal of Applied Physiology Vol. 97, No. 2 ( 2004-08), p. 564-569
    Details
    In: Journal of Applied Physiology, American Physiological Society, Vol. 97, No. 2 ( 2004-08), p. 564-569
    Abstract: The aim of this study was to determine whether hemorrhage affects the levels of a variety of stress-related proteins and whether changes can be inhibited by drugs reported to provide protection from ischemia and reperfusion injury. Male Swiss Webster mice were subjected to a 40% hemorrhage without resuscitation. Western blot analysis indicated that c-Jun (an AP-1 protein), Kruppel-like factor 6 (KFL6), and inducible nitric oxide synthase (iNOS) were upregulated sequentially in that order. Pretreatment of mice with geldanamycin (GA) 16 h before hemorrhage effectively inhibited the expression of the proteins KLF6 and iNOS, whereas caffeic acid phenethyl ester did not. GA pretreatment increased inducible heat shock protein (HSP) 70 but not HSP90 in both sham and hemorrhagic tissues. The overexpressed inducible HSP70 formed complexes with KLF6 and iNOS. These results suggest that GA may be therapeutically useful for reducing hemorrhage-induced injury when used as a presurgical treatment or when added to resuscitation fluids.
    Type of Medium: Online Resource
    ISSN: 8750-7587 , 1522-1601
    URL: Article
    DOI: 10.1152/japplphysiol.00194.2004
    RVK:
    WA 15000
    RVK:
    XA 52094
    Language: English
    Publisher: American Physiological Society
    Publication Date: 2004
    detail.hit.zdb_id: 1404365-8
    SSG: 12
    SSG: 31
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  • 3
    Online Resource
    Online Resource
    N ω -nitro- l -arginine inhibits inducible HSP-70 via Ca 2+ , PKC, and PKA in human intestinal epithelial T84 cells
    American Physiological Society ; 2002
    In:  American Journal of Physiology-Gastrointestinal and Liver Physiology Vol. 282, No. 3 ( 2002-03-01), p. G415-G423
    Details
    In: American Journal of Physiology-Gastrointestinal and Liver Physiology, American Physiological Society, Vol. 282, No. 3 ( 2002-03-01), p. G415-G423
    Abstract: The nitric oxide (NO) synthase inhibitor N ω -nitro-l-arginine (l-NNA) inhibits heat stress (HS)-induced NO production and the inducible 70-kDa heat shock protein (HSP-70i) in many rodent organs. We used human intestinal epithelial T84 cells to characterize the inhibitory effect of l-NNA on HS-induced HSP-70i expression. Intracellular Ca 2+ concentration ([Ca 2+ ] i ) was measured using fura-2, and protein kinase C (PKC), and PKA activities were determined. HS increased HSP-70i mRNA and protein in T84 cells exposed to 45°C for 10 min and allowed to recover for 6 h. l-NNA treatment for 1 h before HS inhibited the induction of HSP-70i mRNA and protein, with an IC 50 of 0.0471 ± 0.0007 μM. Because the HS-induced increase in HSP-70i mRNA and protein is Ca 2+ dependent, we measured [Ca 2+ ] i after treating cells withl-NNA. l-NNA at 100 μM significantly decreased resting [Ca 2+ ] i . Likewise, treatment with 1 μM GF-109203X or H-89 (inhibitors of PKC and PKA, respectively) for 30 min also significantly decreased [Ca 2+ ] i and inhibited HS-induced increase in HSP-70i. GF-109203X- or H-89-treated cells failed to respond tol-NNA by further decreasing [Ca 2+ ] i and HSP-70i. l-NNA effectively blocked heat shock factor-1 (HSF1) translocation from the cytosol to the nucleus, a process requiring PKC phosphorylation. These results suggest that l-NNA inhibits HSP-70i by reducing [Ca 2+ ] i and decreasing PKC and PKA activity, thereby blocking HSF1 translocation from the cytosol to the nucleus.
    Type of Medium: Online Resource
    ISSN: 0193-1857 , 1522-1547
    URL: Article
    DOI: 10.1152/ajpgi.00138.2001
    Language: English
    Publisher: American Physiological Society
    Publication Date: 2002
    detail.hit.zdb_id: 1477329-6
    SSG: 12
    Location Call Number Limitation Availability
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    Online Resource
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