The cAMP effectors Epac and protein kinase a (PKA) are involved in the hepatic cystogenesis of an animal model of autosomal recessive polycystic kidney disease (ARPKD)

Hepatology

Volumn 49, Issue 1, 2009, Pages 160-174

  Banales, Jesús M ^a,b   Masyuk, Tatyana V ^a   Gradilone, Sergio A ^a   Masyuk, Anatoliy I ^a   Medina, Juan F ^b   LaRusso, Nicholas F ^a  

^a Mayo Clinic College of Medicine   (United States)

^b UNIVERSITY OF NAVARRA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIPORTER; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE KINASE 1; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN EPAC; PROTEIN EPAC1; PROTEIN EPAC2; PROTEIN KINASE A REGULATORY PROTEIN I BETA; PROTEIN KINASE A REGULATORY PROTEIN II ALPHA; PROTEIN KINASE A REGULATORY PROTEIN II BET; PROTEIN KINASE B; REGULATOR PROTEIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; CALCIUM; CYCLIC AMP DEPENDENT PROTEIN KINASE REGULATORY SUBUNIT IBETA; EPAC 1 PROTEIN, RAT; EPAC 2 PROTEIN, RAT; EPAC-1 PROTEIN, RAT; EPAC-2 PROTEIN, RAT; GUANINE NUCLEOTIDE EXCHANGE FACTOR; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; AUTOSOMAL RECESSIVE DISORDER; CALCIUM CELL LEVEL; CELL CULTURE; CELL PROLIFERATION; CONFOCAL MICROSCOPY; CONTROLLED STUDY; GENE SILENCING; KIDNEY POLYCYSTIC DISEASE; LIVER CYST; NONHUMAN; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN BLOOD LEVEL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; RAT; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SIGNAL TRANSDUCTION; SPRAGUE DAWLEY RAT; WESTERN BLOTTING; ANIMAL; BILE DUCT; BIOLOGICAL MODEL; BIOSYNTHESIS; CYST; CYTOLOGY; DISEASE MODEL; DRUG EFFECT; ENZYME ACTIVATION; LIVER; LIVER DISEASE; METABOLISM; PATHOPHYSIOLOGY; PHYSIOLOGY;

ANIMALS; BILE DUCTS; CALCIUM; CELL PROLIFERATION; CELLS, CULTURED; CYCLIC AMP; CYCLIC AMP-DEPENDENT PROTEIN KINASE RIBETA SUBUNIT; CYCLIC AMP-DEPENDENT PROTEIN KINASES; CYSTS; DISEASE MODELS, ANIMAL; ENZYME ACTIVATION; GUANINE NUCLEOTIDE EXCHANGE FACTORS; LIVER; LIVER DISEASES; MAP KINASE KINASE KINASES; MITOGEN-ACTIVATED PROTEIN KINASE 1; MITOGEN-ACTIVATED PROTEIN KINASE 3; MODELS, BIOLOGICAL; POLYCYSTIC KIDNEY, AUTOSOMAL RECESSIVE; RATS; RNA, MESSENGER;

EID: 58949089448     PISSN: 02709139     EISSN: None     Source Type: Journal    
DOI: 10.1002/hep.22636     Document Type: Article

References (29)

1. Shneider BL, Magid MS. Liver disease in autosomal recessive polycystic kidney disease. Pediatr Transplant 2005;9:634-639.
2. Nagasawa Y, Matthiesen S, Onuchic LF, Hou X, Bergmann C, Esquivel E, et al. Identification and characterization of Pkhd1, the mouse orthologue of the human ARPKD gene. J Am Soc Nephrol 2002;13:2246-2258.
3. Ward CJ, Hogan MC, Rossetti S, Walker D, Sneddon T, Wang X, et al. The gene mutated in autosomal recessive polycystic kidney disease encodes a large, receptor-like protein. Nat Genet 2002;30:259-269.
4. Masyuk TV, Huang BQ, Ward CJ, Masyuk AI, Yuan D, Splinter PL, et al. Defects in cholangiocyte fibrocystin expression and ciliary structure in the PCK rat. Gastroenterology 2003;125:1303-1310.
5. Masyuk AI, Masyuk TV, Splinter PL, Huang BQ, Stroope AJ, LaRusso NF. Cholangiocyte cilia detect changes in luminal fluid flow and transmit them into intracellular Ca2+ and cAMP signaling. Gastroenterology 2006;131:911-920.
6. Mayuk AI, Gradilone SA, Banales JM, Huang BQ, Masyuk TV, Lee SO, et al. Cholangiocyte primary cilia are chemosensory organelles that detect biliary nucleotides via P2Y12 purinergic receptors. Am J Physiol Gastrointest Liver Physiol 2008; doi:10.1152/ajpgi.90265.2008. Available at: Http://ajpgi.physiology.org.
7. Gradilone SA, Masyuk AI, Splinter PL, Banales JM, Huang BQ, Tietz PS, et al. Cholangiocyte cilia express TRPV4 and detect changes in luminal tonicity inducing bicarbonate secretion. Proc Natl Acad Sci U S A 2007; 104:19138-19143.
8. Banales JM, Masyuk TV, Gradilone SA, Masyuk AI, Medina JF, LaRusso NF. Hepatic cystogenesis is associated with abnormal expression and location of ion transporters and water channels in an animal model of ARPKD. Am J Pathol. In press.
9. Sanzen T, Harada K, Yasoshima M, Kawamura Y, Ishibashi M, Nakanuma Y. Polycystic kidney rat is a novel animal model of Caroli's disease associated with congenital hepatic fibrosis. Am J Pathol 2001;158:1605-1612.
10. Masyuk TV, Masyuk AI, Torres VE, Harris PC, LaRusso NF. Octreotide inhibits hepatic cystogenesis in a rodent model of polycystic liver disease by reducing cholangiocyte adenosine 3′,5′-cyclic monophosphate. Gastroenterology 2007;132:1104-1116.
11. Yamaguchi T, Hempson SJ, Reif GA, Hedge AM, Wallace DP. Calcium restores a normal proliferation phenotype in human polycystic kidney disease epithelial cells. J Am Soc Nephrol 2006;17:178-187.
12. Yamaguchi T, Wallace DP, Magenheimer BS, Hempson SJ, Grantham JJ, Calvet JP. Calcium restriction allows cAMP activation of the B-Raf/ERK pathway, switching cells to a cAMP-dependent growth-stimulated phenotype. J Biol Chem 2004;279:40419-40430.
13. Fabris L, Cadamuro M, Fiorotto R, Roskams T, Spirli C, Melero S, et al. Effects of angiogenic factor overexpression by human and rodent cholangiocytes in polycystic liver diseases. HEPATOLOGY 2006;43:1001-1012.
14. Seino S, Shibasaki T. PKA-dependent and PKA-independent pathways for cAMP-regulated exocytosis. Physiol Rev 2005;85:1303-1342.
15. Roscioni SS, Elzinga CR, Schmidt M. Epac: Effectors and biological functions. Naunyn Schmiedebergs Arch Pharmacol 2008;377:345-357.
16. de Rooij J, Zwartkruis FJ, Verheijen MH, Cool RH, Nijman SM, Wittinghofer A, et al. Epac is a Rap1 guanine-nucleotide-exchange factor directly activated by cyclic AMP. Nature 1998;396:474-477.
17. Ueno H, Shibasaki T, Iwanaga T, Takahashi K, Yokoyama Y, Liu LM, et al. Characterization of the gene EPAC2: Structure, chromosomal localization, tissue expression, and identification of the liver-specific isoform. Genomics 2001;78:91-98.
18. Yamaguchi T, Pelling JC, Ramaswamy NT, Eppler JW, Wallace DP, Nagao S, et al. cAMP stimulates the in vitro proliferation of renal cyst epithelial cells by activating the extracellular signal-regulated kinase pathway. Kidney Int 2000;57:1460-1471.
19. Yang J, Zhang S, Zhou Q, Guo H, Zhang K, Zheng R, et al. PKHD1 gene silencing may cause cell abnormal proliferation through modulation of intracellular calcium in autosomal recessive polycystic kidney disease. J Biochem Mol Biol 2007;40:467-474.
20. Banales JM, Arenas F, Rodriguez-Ortigosa CM, Saez E, Uriarte I, Doctor RB, et al. Bicarbonate-rich choleresis induced by secretin in normal rat is taurocholate-dependent and involves AE2 anion exchanger. HEPATOLOGY 2006;43:266-275.
21. Salter KD, Roman RM, LaRusso NR, Fitz JG, Doctor RB. Modified culture conditions enhance expression of differentiated phenotypic properties of normal rat cholangiocytes. Lab Invest 2000;80:1775-1778.
22. Enserink JM, Christensen AE, de Rooij J, van Triest M, Schwede F, Genieser HG, et al. A novel Epac-specific cAMP analogue demonstrates independent regulation of Rap1 and ERK. Nat Cell Biol 2002;4:901-906.
23. Ogreid D, Ekanger R, Suva RH, Miller JP, Doskeland SO. Comparison of the two classes of binding sites (A and B) of type I and type II cyclic-AMP-dependent protein kinases by using cyclic nucleotide analogs. Eur J Biochem 1989;181:19-31.
24. Ciardiello F, Tortora G. Interactions between the epidermal growth factor receptor and type I protein kinase A: Biological signi.cance and therapeutic implications. Clin Cancer Res 1998;4:821-828.
25. Banales JM, Prieto J, Medina JF. Cholangiocyte anion exchange and biliary bicarbonate excretion. World J Gastroenterol 2006;12:3496-3511.
26. + signaling. Biochem Biophys Res Commun 2005;338:880-889.
27. Wang S, Zhang J, Nauli SM, Li X, Starremans PG, Luo Y, et al. Fibrocystin/polyductin, found in the same protein complex with polycystin-2, regulates calcium responses in kidney epithelia. Mol Cell Biol 2007;27:3241-3252.
28. Wu Y, Dai XQ, Li Q, Chen CX, Mai W, Hussain Z, et al. Kinesin-2 mediates physical and functional interactions between polycystin-2 and fibrocystin. Hum Mol Genet 2006;15:3280-3292.
29. Ward CJ, Yuan D, Masyuk TV, Wang X, Punyashthiti R, Whelan S, et al. Cellular and subcellular localization of the ARPKD protein; fibrocystin is expressed on primary cilia. Hum Mol Genet 2003;12:2703-2710.