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  • Guinea pig  (1)
  • cytotoxicity  (1)
  • Springer  (2)
  • 1
    ISSN: 1573-0832
    Keywords: nephrotoxin ; Penicillium aurantiogriseum ; Balkan Nephropathy ; mycotoxin ; glycopeptide ; cytotoxicity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Water-soluble components of a nephrotoxic isolate of Penicillium aurantiogriseum have been fractionated by sequential ion-exchange, size-exclusion gel filtration, reverse-phase silica chromatography and HPLC. Nephrotoxicity in the rat was confined to a size-exclusion fraction approximating to 1500 daltons, which also inhibited DNA synthesis in cultured kidney cells. The more sensitive in vitro assay allowed toxicity to be followed to a sub-fraction from gradient-elution HPLC which in further HPLC resolved into a small group of glycopeptides. Recent Yugoslavian P. aurantiogriseum isolates, from a village in which the idiopathic human disease Balkan Nephropathy is hyperendemic, elicited a similar nephropathology and were acutely cytotoxic, reinforcing a need to regard this novel Penicillium nephrotoxin as a potential factor in human nephropathy.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 253 (1988), S. 447-455 
    ISSN: 1432-0878
    Keywords: Lysosomes ; Muscle damage ; Calcium ; Lysosomotropic agents ; Phospholipase A2 ; Frog (Rana temporaria) ; Guinea pig
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Experiments with lysosomotropic agents suggest that the sarcotubular system subserves some of the functions of the lysosomal apparatus in frog skeletal muscle. Dinitrophenol or A23187 trigger lysosome labilization and myofilament damage in mammalian cardiac muscle. Lysolecithin labilizes isolated liver lysosomes, but has no action following phospholipase A2 activation in vivo. Zinc ions or a pHi of 7.5 do not protect against myofilament damage. In fractions from mammalian cardiac muscle, calcium and calmodulin do not cause lysosomal labilization whereas cGMP does but only at high concentration (10-4 M). It is concluded that lysosomal hydrolases play no significant part in rapid muscle damage. It is suggested that rises in [Ca]i activate two separate pathways causing (i) myofilament damage; (ii) sarcolemmal (and possibly lysosomal) membrane damage via phospholipase A2 and lipoxygenase activity. Dinitrophenol triggers both pathways independently and thus may cause lysosome labilization. The possibility that the sarcoplasmic reticulum is the site generating myofilament damage is discussed.
    Type of Medium: Electronic Resource
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