Abstract
Cutplasmic dynein is a microtubule-dependent motor protein, which plays a role in intracellular transport. However, there have been a few studies regarding the role of cytoplasmic dynein in the liver. Purification of cytoplasmic dynein from rabbit liver took advantage of the affinity of microtubule-dependent motor proteins for microtubules. Purified dynein contained heavy chain (450 kDa), intermediate chain (75 kDa), light chains (45–58 kDa) and dynactin (150 kDa). The subunit composition was consistent with previously reported data on brain cytolplasmic dynein. Microtubules prepared from bovine brain were driven by purified cytoplasmic dynein from rabbit liver, and movements of microtubules were visualized by video-enhanced differential interference contrast microscopy. The mean velocity of the motile microtubules was 1.09±0.13 μm/s. Our study provides evidence of rapid intracellular transport in hepatocytes controlled by cytoplasmic dynein.
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