The localization of ecto-ATPase in the rat liver

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The bile canalicular membrane of the mammalian hepatocyte contains several transporters that are members of the superfamily of ABC transporter and canalicular ectoenzyme. Bile secretion requires intrahepatic trafficking and regulation of the canalicular ABC transporters. It was reported that after biosynthesis, these canalicular proteins were transferred from the Golgi to the basolateral membrane and subsequently reach the bile canaliculus by transcytosis. Based on these results, it was proposed that all newly synthesized canalicular proteins including ecto-ATPase are targeted via this route. We studied the intracellular trafficking of ecto-ATPase in the rat liver. Adult male rats were injected with LPS (2mg/kg, at every two days for 10 days) or starved for 2-3 weeks. The liver was fixed in 2% glutaraldehyde and cut into slices (40-50 μm) with a Microslicer. Slices were incubated in a reaction medium for detection of ectoATPase activity. The ecto-ATPase activity was localized only at the bile canalicular membrane in the normal rat liver. In the liver of rat injected LPS or starved for 2-3 weeks, the ecto-ATPase activity was mainly localized at the basolateral membrane. If the starved rats were refeeded, the ecto-ATPase activity was quickly relocalized at the canalicular membrane. The results showed that the newly synthesized ecto-ATPase was targeted to the basolateral membrane and subsequently reach the bile canaliculus by transcytosis.
日本組織細胞化学会の論文

The localization of ecto-ATPase in the rat liver

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