Assessment of the in vivo hepatic lysosomal processing of horseradish peroxidase

Canadian Journal of Physiology and Pharmacology

Volumn 74, Issue 1, 1996, Pages 89-96

  Marinelli, Raúl A ^a   Pellegrino, José M ^a   Larocca, María C ^a  

^a UNIVERSIDAD NACIONAL DE ROSARIO   (Argentina)

Author keywords

Horseradish peroxidase; Lysosomal processing; Rat liver

Indexed keywords

CHLOROQUINE; HORSERADISH PEROXIDASE; LEUPEPTIN;

ANIMAL EXPERIMENT; ARTICLE; CONTROLLED STUDY; LIVER METABOLISM; LYSOSOME; MALE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; RAT;

EID: 0029922408     PISSN: 00084212     EISSN: None     Source Type: Journal    
DOI: 10.1139/y95-228     Document Type: Article

References (38)

1. Babson, A.L., Read, P.A., and Phillips, G.E. 1959. The importance of the substrate in the assays of acid phosphatase in serum. Am. J. Clin. Pathol. 32: 83-87.
2. Burwen, S.J., Barke, M.E., Goldman, I.S., Hradek, G.T., Aper, S.E., and Jones, A.L. 1984. Transport of epidermal growth factor by rat liver: evidence for a nonlysosomal pathway. J. Cell Biol. 99: 1259-1265.
3. Coffey, R.J., Kost, L.J., Lyons, R.M., Moses, H.L., and LaRusso, N.F. 1987. Hepatic processing of transforming growth factor β in the rat. Uptake, metabolism, and biliary excretion. J. Clin. Invest. 80: 750-757.
4. Coleman, R. 1987. Biochemistry of bile secretion. Biochem. J. 244: 249-261.
5. de Duve, C., Pressman, B.C., Gianetto, R., Wattiaux, R., and Appelmans, F. 1955. Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat liver tissue. Biochem. J. 60: 604-617.
6. de Duve, C., de Barsy, T., Poole, B., Trouet, A., Tulfens, P., and Van Hoof, F. 1974. Lysosomotropic agents. Biochem. Pharmacol. 23: 2495-2531.
7. Donato, H., Doig, M.T., and Priest, D.G. 1988. Enhancement of polyacrylamide gel slice dissolution in hydrogen peroxide by cupric sulfate. J. Biochem. Biophys. Methods, 15: 331-336.
8. Dufour, J.F., Gehr, P., and Reichen, J. 1992. Hepatic accumulation of lysosomes and defective transcytotic vesicular pathways in cirrhotic rat liver. Hepatology, 16: 997-1006.
9. Evans, W.H. 1979. Identification of subcellular fractions, especially those containing plasma membranes. In Laboratory techniques in biochemistry and molecular biology. Vol. 7. Edited by T.S. Work and E. Work. North-Holland Publishing Co., Amsterdam, Netherlands, pp. 93-176.
10. Hayakawa, T., Cheng, O., Ma, A., and Boyer, J.L. 1990. Taurocholate stimulates transcytotic vesicular pathways labeled by horseradish peroxidase in the isolated perfused rat liver. Gastroenterology, 99: 216-228.
11. Jones, A.L., Schumucker, D.L., Reston, R.H., and Murakami, T. 1980. The architecture of bile secretion. A morphological perspective of physiology. Dig. Dis. Sci. 25: 609-629.
12. Kominami, E., Ueno, T., Muno, D., and Katunuma, N. 1991. The selective role of cathepsins B and D in the lysosomal degradation of endogenous and exogenous proteins. FEBS Lett. 287: 189-192.
13. Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London), 227: 680-685.
14. Largman, C., Ray, S.B., Brodrick, J.W., and Geokas, M.C. 1980. Clearance and metabolism of circulating pancreatic proelastase in the rat. Am. J. Physiol. 239: G504-G510.
15. Lenzen, R., and Tavoloni, N. 1993. Glucagon induces biliary protein excretion in guinea pigs. Am. J. Physiol. 264: G961-G966.
16. Limet, J.N., Quintart, J., Schneider, Y.J., and Courtoy, P.J. 1985. Receptor-mediated endocytosis of polymeric IgA and galactosylated serum albumin in rat liver. Evidence for intracellular ligand sorting and identification of distinct endosomal compartments. Eur. J. Biochem. 146: 539-548.
17. Lowe, P.J., Kan, K.S., Barnwell, S.G., Sharma, R.K., and Coleman, R. 1985. Transcytosis and paracellular movements of horseradish peroxidase across liver parenchymal tissue from blood to bile. Effects of α-naphthylisothiocyanate and colchicine. Biochem. J. 229: 529-537.
18. Lowe, P.J., Miyai, K., Steinbach, J.H., and Hardison, W.G. 1988. Hormonal regulation of hepatocyte tight junctional permeability. Am. J. Physiol. 255: G454-G461.
19. Løwry, O.H., Rosebrough, N.J., Farr, A.L., and Randall, R.J. 1951. Protein measurements with the Folin phenol reagent. J. Biol. Chem. 193: 265-275.
20. Marinelli, R.A., and Peñalva, G.L. 1992. Effects of lysosomotropic agents on the taurocholate-stimulated biliary excretion of horseradish peroxidase. Biochem. Pharmacol. 44: 1683-1686.
21. Marinelli, R.A., Carnovale, C.E., and Rodríguez Garay, E.A. 1988. Bile protein in the rat stimulated by taurocholate: effect of chloroquine. Can. J. Physiol. Pharmacol. 66: 749-753.
22. Marinelli, R.A., Roma, M.G., Pellegrino, J.M., and Rodríguez Garay, E.A. 1992. Taurolithocholate-induced inhibition of biliary lipid and protein excretion in the rat. Biochim. Biophys. Acta, 1125: 44-48.
23. 14C]Sucrose - horseradish peroxidase as a probe for both trancytosis and lysosomal processing of protein in liver. Hepatology, 19: 981.
24. Marks, D.L., and LaRusso, N.F. 1993. Vesicle-dependent transport pathways in liver cells. In Hepatic transport and bile secretion: physiology and pathophysiology. Edited by N. Tavoloni and P.D. Berk. Raven Press Ltd., New York. pp. 513-530.
25. Mori, M., Yamaguchi, J., Oyamada, M., Enomoto, K., and Kaneko, A. 1990. Cytochemical examination of the compartments involved in the transcellular transport of horseradish peroxidase in rat hepatocytes. Cell Struct. Funct. 15: 263-271.
26. Ohshita, T. 1993. Chromatographic analysis of lysosomal degradation of unlabeled native proteins in vitro by fluorescein isothiocyanate labeling. Anal. Biochem. 215: 17-23.
27. Pittman, R.C., Green, S.R., Attie, A.D., and Steinberg, D. 1979. Radiolabeled sucrose covalently linked to protein. A device for quantifying degradation of plasma proteins catabolized by lysosomal mechanisms. J. Biol. Chem. 254: 6876-6879.
28. 125I]insulin. Gastroenterology, 78: 1373-1388.
29. Schiff, J.M., Fisher, M.M., and Underdown, B.J. 1984. Receptor-mediated biliary transport of immunoglobulin A and asialoglycoprotein: sorting and missorting of ligands revealed by two radiolabeling methods. J. Cell Biol. 98: 79-89.
30. Sewell, R.B., Grinpukel, S.A., Zinsmeister, A.R., and LaRusso, N.F. 1988. Pharmacologic perturbation of rat liver lysosomes: effects on release of lysosomal enzymes and of lipids into bile. Gastroenterology, 95: 1088-1098.
31. Thirion, J., and Wattiaux, R. 1988. Effect of monensin on fluid phase and receptor mediated endocytosis by rat hepatocyte monolayers. Biochem. Biophys. Res. Commun. 152: 1275-1281.
32. Tolleshaug, H., and Berg, T. 1981. The effect of leupeptin on intracellular digestion of asialofetuin in rat hepatocytes. Exp. Cell Res. 134: 207-217.
33. Van Dyke, R.W. 1993. Acidification of rat liver lysosomes: quantitation and comparison with endosomes. Am. J. Physiol. 265: C901-C917.
34. Worthington Biochemical Corporation. 1978. Enzymes and related biochemicals. In Worthington manual. Worthington Biochemical Life Sciences Division, Freehold, N.J. pp. 145-146.
35. Yamada, H., Hayashi, H., and Natori, Y. 1984. A simple procedure for the isolation of highly purified lysosomes from normal rat liver. J. Biochem. 95: 1155-1160.
36. Yamaguchi, Y., Dalle-Molle, E., and Hardison, W.G.M. 1992. Proteins ordinarily directed to lysosomes reach bile by an endosomal, not lysosomal pathway. Gastroenterology, 102: A912.
37. Yamaguchi, Y., Dalle-Molle, E., and Hardison, W.G.M. 1993. Hepatocyte horseradish peroxidase uptake is saturable and inhibited by mannose-terminal glycoproteins. Am. J. Physiol. 264: G880-G885.
38. Yamazaki, K., and LaRusso, N.F. 1989. The liver and intracellular digestion: how liver cells eat!. Hepatology, 10: 877-886.