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Progression and reversibility of early light-induced alterations in rat retinal rods (1986)

Moriya, Megumi ; Baker, Barbara N. ; Williams, Theodore P.

Springer

Cell & tissue research 246 (1986), S. 607-621

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ISSN: 1432-0878

Keywords: Rod photoreceptor ; Light damage ; Albino rat ; Ultrastructure ; Reversible change

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine

Notes: Summary The temporal sequence of ultrastructural changes induced in the rat rod photoreceptor by 80 lux light-stress has been studied. The changes seen were compared with those produced by a much dimmer (3 lux) illumination. Some of the early signs of abnormality were (1) degradation of some disk membranes at the tips of outer segments, (2) disaggregation and detachment of ribosomes, (3) lighter matrices in swollen mitochondria, (4) disappearance of the Golgi apparatus, (5) proliferation of autophagic bodies in the inner segments, and (6) appearance of perimitochondrial membrane whorls in the synaptic terminals. No single change could be identified that would inexorably lead to cell death. The overall picture, however, suggested that an inability of the cell to maintain its anabolic balance is responsible for the pyknosis that occurs when the 80 lux exposure exceeds 12–15 h. All changes were reversible when exposure duration did not exceed 12 h, the normal length of the light cycle for these rats.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00215203

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An electron microscopic and enzymic study of rat liver peroxisomal nucleoid core and its association with urate oxidase (1977)

Lata, Gene F. ; Mamrak, Frank ; Bloch, Phillip ; [et al.]

New York, N.Y. : Wiley-Blackwell

Journal of Supramolecular Structure 7 (1977), S. 419-434

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ISSN: 0091-7419

Keywords: peroxisome ; microbody ; nucleoid core ; urate oxidase ; starvation effects ; rat liver enzymes ; catalase ; cell organelle ; Life Sciences ; Molecular Cell Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: The appearance of the characteristic crystalloid core of rat liver peroxisomes is emulated by the electron microscopic (EM) appearance of highly purified urate oxidase prepared from the same tissue. The purity of the enzyme preparation was established by gel electrophoresis under various conditions and the specific enzyme activity was at least as high as any previously reported. The amino acid composition of urate oxidase was determined. As additional evidence for close association of the peroxisomal core with urate oxidase, it was demonstrated that the biphasic changes in rat liver urate oxidase activity in response to prolonged starvation were paralleled by changes in the EM appearance of peroxisomes. Under comparable conditions catalase, another peroxisomal enzyme, did not show the same changes in activity as did urate oxidase. Evidence for the possible identity of urate oxidase with the peroxisomal crystalloid of rat liver has been presented, all materials having been obtained from, and experiments performed with, the rat.

Additional Material: 7 Ill.