BACKGROUND: Biochemical and histochemical studies have both previously indicated plasma membrane-associated carbonic anhydrase (CA) activity in hepatocytes which has been assumed to be @entity30266 . However, immunohistochemical data did not support this assignment. Recent northern blotting results indicated the presence of mRNA for the most recently discovered membrane-bound CA isozyme, @entity54643 , in the liver. The present study was designed to examine whether @entity54643 could contribute to the CA activity described in the hepatocytes. METHODS: Tissue samples from @entity19 liver were subjected to immunohistochemical staining using the antibodies raised against recombinant @entity19 @entity54643 and @entity30266 . RT-PCR and western blotting were also performed for @entity54643 . RESULTS: A strong immunofluorescent signal was observed in the plasma membrane of @entity19 hepatocytes. Although @entity54643 was expressed on both the apical and basolateral surfaces, the staining was more prominent at the apical (canalicular) membrane domain. The expression of @entity54643 in the liver was confirmed by RT-PCR and western blotting. CONCLUSIONS: The presence of @entity54643 in the hepatocyte plasma membrane places this novel enzyme at a strategic site to control pH regulation and ion transport between the hepatocytes, sinusoids and bile canaliculi.

The plasma membrane carbonic anhydrase in XXXX hepatocytes identified as isozyme XIV.

@entity19 :: ('10090', 'Species') :: ['mouse'] @entity30266 :: ('12351(Tax:10090)', 'Gene') :: ['CA IV'] @entity54643 :: ('23831(Tax:10090)', 'Gene') :: ['CA XIV']
@entity19 :: (10090,Species) :: ['murine']
