1. Volume 39, Issue 5, Pages 693-702 (November 2003)
Changes in the expression and localization of hepatocellular transporters and radixin in primary biliary cirrhosis 
Hideyuki Kojima, Anne T Nies, Jörg König, Wolfgang Hagmann, Herbert Spring, Masahito Uemura, Hiroshi Fukui, Dietrich Keppler 
Journal of Hepatology 
Volume 39, Issue 5, Pages (November 2003)
DOI: /S (03)

2. Fig. 1
Immunofluorescence staining of OATP2 and OATP8 in control and PBC livers. Cryosections of human livers, which had been immediately deep-frozen after needle-biopsy, were incubated with the ESL antibody for OATP2 and with the SKT antibody for OATP8. OATP2 was distributed evenly throughout the liver lobule (A–D), whereas OATP8 showed a zonal distribution (E–H). The staining intensities were unchanged in PBC I and II (B, C, F, G), but in PBC III, fluorescence was uneven and reduced in intensity (D, H). Bar, 50 μm.
Journal of Hepatology  , DOI: ( /S (03) )

3. Fig. 2
NTCP immunofluorescence staining in control and PBC livers. Cryosections were incubated with the GNG antibody. Control livers showed a strong basolateral staining (A). NTCP staining was unchanged in PBC I and II (B, C), but PBC III showed an uneven and reduced NTCP immunofluorescence (D). Bar, 20 μm.
Journal of Hepatology  , DOI: ( /S (03) )

4. Fig. 3
Immunofluorescence staining of MRP2 and MRP3 in control and PBC livers. Cryosections were incubated with the EAG5 antibody for MRP2 and with the FDS antibody for MRP3. MRP2 staining was thin and marked the canalicular domain in control liver (A). The staining intensity of MRP2 was similar between control and PBC livers (A–D), but a broad and irregular staining was observed in PBC III (D). Basolateral MRP3 staining was weak in control and PBC livers (E–H), and it was not enhanced even in PBC III (H). Bar, 10 μm.
Journal of Hepatology  , DOI: ( /S (03) )

5. Fig. 4
Confocal laser scanning micrographs of cryosections from control and PBC III livers double-stained for MRP2 (green in A,D,G; M2III-6 antibody in A, D; EAG5 antibody in G), tight junctions (red in B, E; anti-ZO-1 antibody), or P-glycoproteins (red in H; C219 antibody). In control livers, MRP2 is localized mainly to the canalicular space bordered by the ZO-1 staining (A–C). In PBC III, a redistribution of MRP2 into intracellular structures, represented by an irregular staining inside the cytoplasm of hepatocytes, was observed (D–F). P-glycoproteins had a similar staining pattern as MRP2 (G–I). Bar, 20 μm.
Journal of Hepatology  , DOI: ( /S (03) )

6. Fig. 5
Confocal laser scanning micrographs of the localization of radixin and moesin in human liver. Liver cryosections were double-stained with the EAG5 antibody (green) and either 38/87 antibody against radixin and moesin (red in A and C) or M22 against moesin (red in D and F). Radixin and moesin staining with the 38/87 antibody was mainly detected in the canalicular domain as shown by the colocalization with MRP2; in addition, a weak staining was observed at the sinusoidal domain (A–C). Specific moesin staining using the M22 antibody was observed at the sinusoidal domain, but not detected in the canalicular domain (D–F). The absence of moesin from the canalicular domain indicates that the canalicular signal by the 38/87 antibody exclusively represents radixin staining. Bar, 20 μm.
Journal of Hepatology  , DOI: ( /S (03) )

7. Fig. 6
Confocal laser scanning micrographs of cryosections from control, AIH, and PBC III livers double-stained for MRP2 (green; EAG5 antibody) and radixin (red; 38/87 antibody). In control (A–C) and cholestatic, non-icteric autoimmune hepatitis (AIH; D–F; AIH patient 1) livers, staining of MRP2 and radixin was thin and colocalized in the canalicular domain. In PBC III livers (G–L), however, staining intensities of MRP2 and radixin were disproportionate and radixin staining almost disappeared in areas with irregular MRP2 staining (arrows). Note that areas of irregular MRP2 staining were present next to areas with a ‘proper’ canalicular staining of MRP2 and radixin (arrowheads in J–L). Bar, 10 μm.
Journal of Hepatology  , DOI: ( /S (03) )

8. Fig. 7
Proposed radixin–MRP2 interaction. Radixin may bind to MRP2 directly or via additional coupling proteins such as PDZ domain-interacting proteins at its N-terminus and to actin filaments at its C-terminus [6,34] and thus may anchor MRP2 in the canalicular membrane via a connection with actin filaments. In addition, ERM proteins including radixin associate with protein kinase A [35], suggesting that radixin may be involved in the cAMP-regulated localization of MRP2 into the canalicular membrane.
Journal of Hepatology  , DOI: ( /S (03) )