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. 1985 Jan;59(1):123–131.

Occurrence of cytotoxic autoantibody in rabbits by immunization with heterologous liver arginase: a possible implication in the mechanism of the autoimmune liver diseases.

N Mafune, N Ideta, H Watabe, H Nagura, K Kobayashi
PMCID: PMC1577166  PMID: 3882282

Abstract

Rat liver arginase was isolated from extracts of liver in a pure form. Monospecific antisera raised against the arginase reacted with arginase of liver but not with arginase of kidney, spleen, heart, lung, testis and brain. The antisera were, however, reactive with liver arginase of a variety of animals, including human, mouse, sheep, horse and cow as well as rabbit, a homologous animal used for immunization. The rabbit autoantibodies showed direct cytotoxic activity as well as antibody-dependent cell-mediated cytotoxicity to homologous rabbit hepatocytes. Immunocytochemical electron microscopic examination showed that the arginase was localized on the surfaces of rat hepatocytes and on intracellular organelles. These results suggest that liver arginase could be an important antigen of the liver with implications for the pathogenesis of autoimmune liver diseases.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Behrens U. J., Vernace S., Paronetto F. Studies on "liver-specific" antigens. II. Detection of serum antibodies to liver and kidney cell membrane antigens in patients with chronic liver disease. Gastroenterology. 1979 Nov;77(5):1053–1061. [PubMed] [Google Scholar]
  2. Cochrane A. M., Moussouros A., Thomsom A. D., Eddleston A. L., Wiiliams R. Antibody-dependent cell-mediated (K cell) cytotoxicity against isolated hepatocytes in chronic active hepatitis. Lancet. 1976 Feb 28;1(7957):441–444. doi: 10.1016/s0140-6736(76)91472-0. [DOI] [PubMed] [Google Scholar]
  3. Hagan J. J., Dallam R. D. Measurement of arginase activity. Anal Biochem. 1968 Mar;22(3):518–524. doi: 10.1016/0003-2697(68)90293-5. [DOI] [PubMed] [Google Scholar]
  4. Herzfeld A., Raper S. M. The heterogeneity of arginases in rat tissues. Biochem J. 1976 Feb 1;153(2):469–478. doi: 10.1042/bj1530469. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hirsch-Kolb H., Greenberg D. M. Molecular characteristics of rat liver arginase. J Biol Chem. 1968 Dec 10;243(23):6123–6129. [PubMed] [Google Scholar]
  6. Jänne J., Pösö H., Raina A. Polyamines in rapid growth and cancer. Biochim Biophys Acta. 1978 Apr 6;473(3-4):241–293. doi: 10.1016/0304-419x(78)90015-x. [DOI] [PubMed] [Google Scholar]
  7. Kaysen G. A., Strecker H. J. Purification and properties of arginase of rat kidney. Biochem J. 1973 Aug;133(4):779–788. doi: 10.1042/bj1330779. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  9. Leffert H. L., Paul D. Serum dependent growth of primary cultured differentiated fetal rat hepatocytes in arginine-deficient medium. J Cell Physiol. 1973 Feb;81(1):113–124. doi: 10.1002/jcp.1040810114. [DOI] [PubMed] [Google Scholar]
  10. Mancini G., Carbonara A. O., Heremans J. F. Immunochemical quantitation of antigens by single radial immunodiffusion. Immunochemistry. 1965 Sep;2(3):235–254. doi: 10.1016/0019-2791(65)90004-2. [DOI] [PubMed] [Google Scholar]
  11. McLean I. W., Nakane P. K. Periodate-lysine-paraformaldehyde fixative. A new fixation for immunoelectron microscopy. J Histochem Cytochem. 1974 Dec;22(12):1077–1083. doi: 10.1177/22.12.1077. [DOI] [PubMed] [Google Scholar]
  12. Meyer zum Büschenfelde K. H., Manns M., Hütteroth T. H., Hopf U., Arnold W. LM-Ag and LSP--two different target antigens involved in the immunopathogenesis of chronic active hepatitis? Clin Exp Immunol. 1979 Aug;37(2):205–212. [PMC free article] [PubMed] [Google Scholar]
  13. Nagura H., Brandtzaeg P., Nakane P. K., Brown W. R. Ultrastructural localization of J chain in human intestinal mucosa. J Immunol. 1979 Sep;123(3):1044–1050. [PubMed] [Google Scholar]
  14. SCHIMKE R. T. THE IMPORTANCE OF BOTH SYNTHESIS AND DEGRADATION IN THE CONTROL OF ARGINASE LEVELS IN RAT LIVER. J Biol Chem. 1964 Nov;239:3808–3817. [PubMed] [Google Scholar]
  15. Tabor C. W., Tabor H. 1,4-Diaminobutane (putrescine), spermidine, and spermine. Annu Rev Biochem. 1976;45:285–306. doi: 10.1146/annurev.bi.45.070176.001441. [DOI] [PubMed] [Google Scholar]
  16. Venkatakrishnan G., Reddy S. R. A comparative polyacrylamide gel electrophoretic study of arginase in vertebrate tissues. Enzyme. 1983;29(3):145–152. doi: 10.1159/000469626. [DOI] [PubMed] [Google Scholar]
  17. Yip M. C., Knox W. E. Function of arginase in lactating mammary gland. Biochem J. 1972 May;127(5):893–899. doi: 10.1042/bj1270893. [DOI] [PMC free article] [PubMed] [Google Scholar]

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