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Vitamin E protection of cell morphology under oxidative stress is related to cytoskeletal proteins in rat hepatocytes (1997)

Kuo, Jyh-Huang ; Chen, Haw-Wen ; Chou, Rong-Ghi R. ; [et al.]

Springer

Archives of toxicology 71 (1997), S. 231-237

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ISSN: 1432-0738

Keywords: Key words Vitamin E ; Cell surface blebs ; Actin ; Hepatocytes ; Rat

Source: Springer Online Journal Archives 1860-2000

Topics: Medicine

Notes: Abstract A significant change in cell morphology was observed in hepatocytes treated with t-butyl hydroperoxide (t-BH). This morphological change of multiple bleb formation on cell plasma membranes was related to cell damage, and the subsequent rupture of these blebs resulted in cell death. In cells incubated with α-tocopherol before t-BH treatment, bleb formation was significantly inhibited. Using fluorescence microscopy, actin organization was shown to be related to α-tocopherol status as demonstrated by early changes in the actin network of cells in the absence of α-tocopherol. Results from SDS-polyacrylamide gel elecrophoresis further indicated that, under oxidative stress, actin molecules (45 kDa) decreased in amount and were accompanied by the formation of high molecular weight molecules. In the presence of the thiol reducing agent, dithiothreitol, both the decrease in monomeric actin and formation of high molecular weight molecules disappeared. The loss of actin showed a time-dependent response and could be observed after 15 min with t-BH treatment either in the presence or absence of α-tocopherol; however the extent was much more significant in cells with no α-tocopherol. Depletion of total membrane protein thiols was also related to vitamin E and was greater in cells with no α-tocopherol. The amount of cell damage, as determined by lactate dehydrogenase (LDH) leakage in cells with t-BH treatment over 120 min was decreased in the presence of α-tocopherol compared with the rapid increase of LDH leakage in the absence of α-tocopherol. These results indicate that vitamin E protection of cell morphology under oxidative stress is related to actin, with thiol groups in actin probably playing a key role.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/s002040050381

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Substructure of cytoplasmic dense bodies and changes in distribution of desmin and α-actinin in developing smooth muscle cells (1994)

Chou, Rong-Ghi R. ; Stromer, Marvin H. ; Robson, Richard M. ; [et al.]

New York, NY : Wiley-Blackwell

Cell Motility and the Cytoskeleton 29 (1994), S. 204-214

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ISSN: 0886-1544

Keywords: intermediate filaments ; cytoskeleton ; filament attachment sites ; immunogold labeling ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Medicine

Notes: The substructure of assembling cytoplasmic dense bodies (CDBs) and changes in the distribution of desmin and α-actinin during development of smooth muscle were studied in gizzard samples from 10- and 16-day embryos and from 1- and 7-day post-hatch chickens. CDBs in these cells lack the density of CDBs in mature or adult smooth muscle cells and, thus, allow observations of the changes inside CDBs. The random filament orientation seen in younger embryonic cells is first modified to include relatively small patches of IFs that are somewhat straighter and are approaching a side-by-side arrangement. As development proceeds, the IFs in these arrays become straighter, are parallel over longer lengths of the IFs and later acquire the density characteristic of mature CDBs. Anti-desmin labeling in embryonic 10- and 16-day cells showed that desmin intermediate filaments (IFs) were located in the myofilament compartment but were concentrated in or near assembling CDBs. Anti-desmin labeling shifted to the perimeter of CDBs after hatching. Cross sections, longitudinal sections, and stereo pairs all show that IF profiles are present inside unlabeled assembling CDBs. Anti-α-actinin labeling was directly on CDBs and was often associated with the cross-connecting filaments (CCFs) (average diameter of 2-3nm) inside CDBs. We propose, based on these data, that desmin IFs, α-actinin-containing CCFs, and actin filaments are the principal components of the substructure of assembling CDBs. We also present a proposed model for CDB assembly. © 1994 Wiley-Liss, Inc.

Additional Material: 7 Ill.