Biliary intervention augments chemotactic reaction and aggravates cholestatic liver injury in rats

Journal of Surgical Research

Volumn 120, Issue 2, 2004, Pages 210-218

  Chuang, Jiin Haur ^a,b   Chang, Nyuk Kong ^a   Huang, Chao Cheng ^b   Lo, Sing Kai ^c   Wang, Hsiu Chuan ^b   Chen, Ching Mei ^a,b   Wu, Chia Ling ^b   Chou, Ming Huei ^a   Lin, Tsu Kung ^a,b  

^a CHANG GUNG UNIVERSITY   (Taiwan)

^b CHANG GUNG MEMORIAL HOSPITAL   (Taiwan)

^c UNIVERSITY OF SYDNEY   (Australia)

Author keywords

chemokine; macrophage inflammatory protein 2 (MIP 2); malondialdehyde; monocyte chemoattractant protein 1 (MCP 1); myeloperoxidase; obstructive jaundice

Indexed keywords

ALANINE AMINOTRANSFERASE; ALPHA CHEMOKINE; BETA CHEMOKINE; MACROPHAGE INFLAMMATORY PROTEIN 2; MALONALDEHYDE; MONOCYTE CHEMOTACTIC PROTEIN 1; MYELOPEROXIDASE; SODIUM CHLORIDE;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; APOPTOSIS; ARTICLE; BILE DUCT LIGATION; CELL COUNT; CELL DEATH; CHEMOTAXIS; CHOLESTASIS; CONTROLLED STUDY; ENZYME LINKED IMMUNOSORBENT ASSAY; IMMUNOHISTOCHEMISTRY; INDWELLING CATHETER; KUPFFER CELL; LIPID PEROXIDATION; LIVER INJURY; MALE; MONOCYTE; NEUTROPHIL; NICK END LABELING; NONHUMAN; PARENCHYMA; PRIORITY JOURNAL; PROTEIN BLOOD LEVEL; RAT;

ANIMALS; BILE DUCTS; CATHETERS, INDWELLING; CHEMOKINE CCL2; CHEMOKINES, CXC; CHEMOTAXIS; CHOLESTASIS; ECTODYSPLASINS; INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS; LIGATION; LIVER; MALE; MALONDIALDEHYDE; MEMBRANE PROTEINS; PEROXIDASE; PROTEIN ISOFORMS; PROTEINS; RATS; RATS, SPRAGUE-DAWLEY; SODIUM CHLORIDE;

EID: 3042661983     PISSN: 00224804     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jss.2004.03.020     Document Type: Article

References (33)

1. Scott-Conner C.E.H., Grogan J.B. The pathophysiology of biliary obstruction and its effect on phagocytic and immune function. J. Surg. Res. 57:1994;316
2. Benyon R.C., Arthur M.J.P. Mechanisms of hepatic fibrosis. J. Pediatr. Gastroenterol. Nutr. 27:1998;75
3. Martignoni M.E., Wagner M., Krahenbuhl L., Redaelli C.A., Friess H., Buchler M.W. Effect of preoperative biliary drainage on surgical outcome after pancreaticoduodenectomy. Am. J. Surg. 181:2001;52
4. Ahuja V., Garg P.K., Kumar D., Goindi G., Tandon R.K. Presence of white bile associated with lower survival in malignant biliary obstruction. Gastrointest. Endosc. 55:2002;186
5. Pinol V., Castells A., Bordas J.M., Real M.I., Liach J., Montana X., Feu F., Navarro S. Percutaneous self-expanding metal stents versus endoscopic polyethylene endoprostheses for treating malignant biliary obstruction randomized clinical trial. Radiology. 225:2002;27
6. Sokol R.J., Winklhofer-Roob B.M., Devereaux M.W., McKim J.M. Jr. Generation of hydroperoxides in isolated rat hepatocytes and hepatic mitochondria exposed to hydrophobic acids. Gastroenterology. 109:1995;1249
7. Roggin K.K., Kim J.C., Kurkchubasche A.G., Papa E.F., Vezeridis A.M., Tracy T.F. Macrophage phenotype during cholestatic injury and repair the persistent inflammatory response. J. Pediatr. Surg. 36:2001;220
8. Parola M., Leonarduzzi G., Robino G., Albano E., Poli G., Dianzani M.U. On the role of lipid peroxidation in the pathogenesis of liver damage induced by long-standing cholestasis. Free Radic. Biol. Med. 20:1996;351
9. Clements W.D., Erwin P., McCaigue M.D., Halliday I., Barclay G.R., Rowlands B.J. Conclusive evidence of endotoxemia in biliary obstruction. Gut. 42:1998;293
10. Houdijk A.P., van Lambalgen A.A., Thijs L.G., van Leeuwen P.A. Gut endotoxin restriction improves postoperative hemodynamics in the bile duct-ligated rat. Shock. 9:1998;282
11. Gores G.J., Miyoshi H., Botla R., Aguilar H.I., Bronk S.F. Induction of the mitochondrial permeability transition as a mechanism of liver injury during cholestasis a potential role for mitochondrial proteases. Biochim. Biophys. Acta. 1366:1998;167
12. Letteron P., Brahimi-Bourouina N., Robin M.A., Moreau A., Feldmann G., Pessayre D. Glucocorticoids inhibit mitochondrial matrix acyl-coA dehydrogenases and fatty acid β-oxidation. Am. J. Physiol. 272:1997;G1141
13. Saito J.M., Maher J.J. Bile duct ligation in rats induces biliary expression of cytokine-induced neutrophil chemoattractant. Gastroenterology. 118:2000;1157
14. Sprenger H., Kaufmann A., Garn H., Lahme B., Gemsa D., Gressner A.M. Induction of neutrophil-attracting chemokines in transforming rat hepatic stellate cells. Gastroenterology. 113:1997;277
15. Bautista A.P. The role of Kupffer cells and reactive oxygen species during acute and chronic ethanol intoxication. Alcohol Clin. Exp. Res. 22:1998;255
16. Winterboum C.C. Comparative reactivities of various biological compounds with myeloperoxidase-hydrogen peroxide-chloride, and similarity of the oxidant to hypochlorite. Biochim. Biophys. Acta. 840:1985;204
17. Savenkova M.L., Mueller D.M., Heinecke J.W. Tyrosyl radical generated by myeloperoxidase is a physiological catalyst for the initiation of lipid peroxidation in low density lipoprotein. J. Biol. Chem. 269:1994;20394
18. Bidlack W.R., Okita R.T., Hochstein P. The role of NADPH-cytochrome b 5 reductase in microsomal lipid peroxidation. Biochem. Biophys. Res. Commun. 53:1973;459
19. Verbeke G., Molenberghs G. Linear Mixed Models for Longitudinal Data. 2000;Springer, New York
20. Hochberg Y., Benjamini Y. More powerful procedure for multiple significance testing. Stat. Med. 9:1990;811
21. Duch B.U., Andersen H.L., Smith J., Kassab G.S., Gregersen H. Structural and mechanical remodeling of the common bile duct after obstruction. Neurogastroenterol. Motility. 14:2002;111
22. Carlson E., Zukoski C.F., Campbell J., Chvapil M. Morphologic, biophysical, and biochemical consequences of ligation of the common biliary duct in the dog. Am. J. Pathol. 86:1977;301
23. Metz J., Aoki A., Merlo M., Forssmann W.G. Morphological alterations and functional changes of interhepatocellular junctions induced by bile duct ligation. Cell Tissue Res. 182:1977;299
24. Gumpricht E., Dahl R., Yerushalmi B., Devereaux M.W., Sokol R.J. Nitric oxide ameliorates hydrophobic bile acid-induced apoptosis in isolated rat hepatocytes by non-mitochondrial pathways. J. Biol. Chem. 277:2002;25823
25. Polimeno L., Azzarone A., Zeng Q.H., Panella C., Subbotin V., Carr B., Bouzahzah B., Francavilla A., Starzl T.E. Cell proliferation and oncogene expression after bile duct ligation in the rat evidence of a specific growth effect on bile duct cells. Hepatology. 21:1995;1070
26. Hines J.E., Johnson S.J., Burt A.D. In vivo responses of macrophages and perisinusoidal cells to cholestatic liver injury. Am. J. Pathol. 142:1993;511
27. Dijkstra C.D., Dopp E.A., Joling P., Kraal G. The heterogeneity of mononuclear phagocytes in lymphoid organs distinct macrophage subpopulations in the rat recognized by monoclonal antibodies ED1, ED2 and ED3. Immunology. 54:1985;589
28. Armbrust T., Ramadori G. Functional characterization of two different Kupffer cell populations of normal rat liver. J. Hepatol. 25:1996;518
29. MacPhee P.J., Schmidt E.E., Groom A.C. Evidence for Kupffer cell migration along liver sinusoids, from high resolution in vivo microscopy. Am. J. Physiol. 263:1992;G17
30. Kawashima R., Mochida S., Matsui A., YouLuTuz Y., Ishikawa K., Toshima K., Yamanobe F., Inao M., Ikeda H., Ohno A., Nagoshi S., Uede T., Fujiwara K. Expression of osteopontin in Kupffer cells and hepatic macrophages and stellate cells in rat liver after carbon tetrachloride intoxication a possible factor for macrophage migration into hepatic necrotic areas. Biochem. Biphys. Res. Commun. 256:1999;527
31. Ohata M., Ito T. Experimental study on the fine structure of chicken liver parenchyme with special references to extrasinusoidal macrophages and sinusoidal blood cells. Part 2. Sinusoidal blood cells in normal and India ink perfused livers. Arch. Histol. Jpn. 49:1986;199
32. Kettle A.J., Winterbourn C.C. Myeloperoxidase a key regulator of neutrophil oxidant production. Redox. Rep. 3:1997;3
33. Baldus S., Eiserich J.P., Mani A., Castro L., Figueroa M., Chumley P., Ma W., Tousson A., White C.R., Bullard D.C., Brennan M.L., Lusis A.J., Moore K.P., Freeman B.A. Endothelial transcytosis of myeloperoxidase confers specificity to vascular ECM proteins as targets of tyrosine nitration. J. Clin. Invest. 108:2001;1759