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17. Effects of Hydroquinone on Cytoskeletal Organization and Intracellular Transport in Cultured Xenopus laevis Melanophores and Fibroblasts.

Author

Aspengren, Sara, Norström, Elisabeth, and Wallin, Margareta

Subjects
HYDROQUINONE, XENOPUS laevis, MELANOPHORES, FIBROBLASTS, MELANOCYTES, CELL migration, CELL culture
Abstract

Hydroquinone is used as a skin-lightening agent, it is also present in different chemical products and cigarette smoke. It is believed to inhibit melanin production in melanocytes by inhibiting the key enzyme tyrosinase. In the present study, we show that hydroquinone had severe effects on microtubules and actin filaments in cultured Xenopus laevis melanophores as studied by immunohistochemistry. It affected the intracellular transport of melanosomes, induced bundling of microtubules and disassembly of actin filaments at 10 and 50 µM, and at 100 µM proper adhesion to the substrate was lost. Effects occurred at lower concentrations than what previously has been stated to be cytotoxic, and the results show that tyrosinase is not the only cellular target. The cytoskeleton is of utmost importance for the function of all cells and across species. Our data has therefore to be considered in the discussions about the use of hydroquinone for bleaching of skin. [ABSTRACT FROM AUTHOR]

Published
2012
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30. Dependency of microtubule-associated proteins (MAPS) for tubulin stability and assembly; use of estramustine phosphate in the study of microtubules.

Author

Fridén, Bo and Wallin, Margareta

Abstract

Microtubule-associated proteins (MAPS) were separated from tubulin with several different methods. The ability of the isolated MAPs to reinduce assembly of phosphocellulose purified tubulin differed markedly between the different methods. MAPs isolated by addition of 0.35 M NaCl to taxol-stabilized microtubules stimulated tubulin assembly most effectively, while addition of 0.6M NaCl produced MAPs with a substantially lower ability to stimulate tubulin assembly. The second best preparation was achieved with phosphocellulose chromatographic separation of MAPs with 0.6 M NaCl elution. The addition of estramustine phosphate to microtubules reconstituted of MAPS prepared by 0.35 M NaCl or phosphocellulose chromatography, induced less disassembly than for microtubules assembled from unseparated proteins, and was almost without effect on microtubules reconstituted from MAPs prepared by taxol and 0.6 M NaCl. Estramustine phosphate binds to the tubulin binding part of the MAPs, and the results do therefore indicate that the MAPs are altered by the separation methods. Since the MAPs are regarded as highly stable molecules, one probable alteration could be aggregation of the MAPs, as also indicated by the results. The purified tubulin itself seemed not to be affected by the phosphocellulose purification, since the microtubule proteins were unchanged by the low buffer strenght used during the cromatography. However, the assembly competence after a prolonged incubation of the microtubule proteins at 4° C was dependent on intact bindings between the tubulin and MAPs. [ABSTRACT FROM AUTHOR]

Published
1991
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