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R A Quinlan

Publications and source records attributed to R A Quinlan.

57 records · Page 4Linked to original sources

Binding of parbendazole to tubulin and its influence on microtubules in tissue-culture cells as revealed by immunofluorescence microscopy.

We have shown that the benzimidazole carbamate, parbendazole, is a potent inhibitor of microtubule assembly in vitro and in vivo. Radiolabelled parbendazole was shown to bind to purified tubulin. Immunofluorescence studies using antitubulin antibody showed that parbendazole effectively depolymerizes cytoplasmic microtubules in animal cells leaving only one or two microtubules associated with one centriole. The usefulness of parbendazole and other benzimidazole carbamates as inhibitors of microtubule functions is discussed.

Animals↗

The influence of the microtubule inhibitor, methyl benzimidazol-2-yl-carbamate (MBC) on nuclear division and the cell cycle in Saccharomyces cerevisiae.

Methyl benzimidazol-2-yl-carbamate (MBC), at a concentration of 100 microM, has a pronounced effect on the growth of Saccharomyces cerevisiae, resulting in the accumulation of cells as large doublets. We have determined a specific execution point for the effect of MBC on the yeast cell cycle, and have shown that this execution point is between the cycle events of spindle pole body duplication and spindle pole body separation. An ultrastructural examination of the MBC-treated cells revealed the absence of cytoplasmic and spindle microtubules. MBC treatment also produced an altered spindle pole body morphology, causing the disappearance of the outer component. Nuclear size was also markedly increased in the MBC-induced doublet cells, although the septa were completely absent from these doublet cells. It is proposed that MBC inhibits microtubule polymerization, rather than causing the depolymerization of stable microtubules.

Benzimidazoles↗