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Original Article

A novel function of haptoglobin: haptoglobin-haemoglobin complex induces apoptosis of hepatocarcinomatous Hep 3B cells

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Pages 529-535 | Received 20 Jan 1995, Accepted 20 May 1995, Published online: 29 Mar 2011

References

  • Shim B-S, Bearn A G. Immunological and biochemical studies on serum haptoglobin. J Exp Med 1964; 120: 611–28
  • Shim B-S, Lee T-H, Kang Y-S. Immunological and biochemical investigations of human serum haptoglobin: composition of haptoglobin-haemoglobin intermediate, haemoglobin-binding sites and presence of additional alleles for β-chain. Nature 1965; 207: 1264–7
  • Sutton H E. The haptoglobins. Progress in medical genetics, A G Steinberg, A G Bearn. Grune and Stratton, New York 1970; 7: 163–216
  • Laurell C-B, Nyman M. Studies on the serum haptoglobin level in hemoglobinemia and its influence on renal excretion of hemoglobin. Blood 1957; 12: 493–506
  • Whitten C F. Studies on serum haptoglobin. A functional inquiry. N Engl J Med 1962; 266: 529–34
  • Snellman O, Sylven B. Haptoglobin acting as a natural inhibitor of cathepsin B activity. Nature 1967; 216: 1033
  • Eaton J W, Brandt P, Mahoney J R, Lee J T., Jr. Haptoglobin: a natural bacteriostat. Science 1982; 215: 691–3
  • Owen J A, Smith R, Paranyi R, Martin J. Serum haptoglobin in disease. Clin Sci 1964; 24: 1–60
  • Shim B-S. Increase in serum haptoglobin stimulated by prostaglandins. Nature 1976; 259: 326–7
  • Jue D-M, Shim B-S, Kang Y-S. Inhibition of prostaglandin synthase activity of sheep seminal vesicular gland by human serum haptoglobin. Mol Cell Biochem 1983; 51: 141–7
  • Shim B-S, Yang S-J, Kwon O-J, Kim I-K. Study on the natural healing mechanism in tumors. Korean J Biochem 1985; 17: 177–82
  • Fanelli A R, Antonini E, Caputo A. Studies on the structure of hemoglobin. I. Physiological property of human globin. Biochim Biophys Acta 1958; 30: 608–15
  • Bradford M M. A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding. Analyt Biochem 1976; 72: 248–54
  • Shim B-S, Park Y-H, Kim H-C, Kim Y-C, Lee T-H. Paper electrophoretic estimation of the serum haptoglobin level and an ultramicrohemoglobinometry. J Cath Med Coll (Seoul) 1959; 3: 176–82
  • Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Meth 1983; 65: 55–63
  • Mori H, Takada Y, Kondoh H, Tamaya T. Augmentation of antiproliferative activity of recombinant human tumor necrosis factor with Δ12-prostaglandin J2. J Biol Resp Mod 1990; 9: 260–3
  • Kaufmann S H. Induction of endonucleolytic DNA cleavage in human acute myelogenous leukemia cells by etoposide, camptothecin, and other cytotoxic anticancer drugs: a cautionary note. Cancer Res 1989; 49: 5870–8
  • Goelz S E, Hamilton S R, Vogelstein B. Purification of DNA from formaldehyde fixed and paraffin embedded human tissue. Biochem Biophys Res Commun 1985; 130: 118–26
  • Park S-C, Lee Y-C, Kim S-H, Kim S-Y, Choi K-H, Song K-Y, et al. Changes of transglutaminase activities in the process of regeneration and carcinogenesis of rat liver tissues. Korean J Biochem 1991; 23: 39–46
  • Kino K, Tsunoo H, Higa Y, Takami M, Nakajima H. Kinetic aspects of hemoglobin haptoglobin-receptor interaction in rat liver plasma membranes, isolated liver cells, and liver cells in primary culture. J Biol Chem 1982; 257: 4828–33
  • Wyllie A H, Kerr J FR, Currie A R. Cell death: the significance of apoptosis. Int Rev Cytol 1982; 68: 251–306
  • Fesus L, Thomazy V, Autori F, Ceru M P, Tarcsa E, Piacentini M. Apoptotic hepatocytes become insoluble in detergents and chaotropic agents as a result of transglutaminase action. FEBS Lett 1989; 245: 150–4
  • Nauts H C, Fowler G A, Eibley F R, Bogatko F H. Review of the influence of bacterial infection and of bacterial products (Coley's toxins) on malignant tumors in man. Acta Med Scand 1953; 45, Suppl 276
  • Old L J, Boyse E S. Current enigmas in cancer research. Harvey lectures. Academic Press, New York 1973; 273–315, Series 67
  • Carswell E A, Old L J, Kasse R L, Green S, Fiore N, Williamson B. An endotoxin-induced serum factor that causes necrosis of tumor. Proc Natl Acad Sci USA 1975; 72: 3666–750
  • Brandslund I, Petersen P H, Struge P, Hole P, Worth V. Haemolytic uraemic syndrome and accumulation of haemoglobin-haptoglobin complexes in plasma in serum sickness caused by penicillin drugs. Haemostasis 1980; 9: 193–203
  • Badr K F, Brenner B M. Haemolytic uremic syndrome (HUS) and thrombotic thrombocytopenic purpura (TTP). Harrison's principles of internal medicine. 13th ed, K J Isselbacher, E Braunwald, J D Wilson, J B Martin, A S Fauci, D W Kasper. McGraw-Hill, New York 1994; 1320–1
  • Shim B-S, Kim I-K. Local Shwartzman-like phenomenon prepared with haptoglobin-hemoglobin complex and provoked with prostaglandin. Vox Sang 1978; 35: 414–9
  • Knyszinski A, Burger M. Increase of haptoglobin concentration in mouse serum by endotoxin and by a serum factor. Experientia 1971; 27: 838–9
  • Santoro M G, Philpott G W, Jaffe B M. Inhibition of tumor growth in vivo, in vitro by prostaglandin E. Nature 1976; 263: 777–9
  • Narumiya S, Fukushima M. Δ12-Prostaglandin J2, an ultimate metabolite of prostaglandin D2 exerting cell growth inhibition. Biochem Biophys Res Commun 1985; 127: 739–45
  • Shim B-S, Kim I-K, Kwon O-J, Lee J-H. The antitumor effect of prostaglandins and synergistic antitumor activity of prostaglandin E2 and haptoglobin-hemoglobin complex. J Korean Med Assoc 1989; 32: 407–12
  • Ruff M R, Gifford G E. Tumor necrosis factor. Lymphokines, E Pick. Academic Press, New York 1981; 235–72
  • Puisieux A, Galvin K, Troalen F, Bressac B, Marcais C, Galun E, et al. Retinoblastoma and p53 tumor suppressor genes in human hepatoma cell lines. FASEB J 1993; 7: 1407–13
  • Lowe S W, Bodis S, McClatchey A, Remington L, Ruley H E, Fisher D E, et al. p53 status and the efficiency of cancer therapy in vivo. Science 1994; 266: 807–10
  • Smith A B, Esko J D, Hajduk S L. Killing of trypanosomes by the human haptoglobin-related protein. Science 1995; 268: 284–6
  • Boyd W. The spontaneous regression of cancer. Charles C. Thomas, Springfield 1966
  • National Cancer Institute. Conference on Spontaneous Regression of Cancer, Bethesda, Maryland, 1973, Monograph 44
  • Wanebo H J, Green S, Marshall D, Pace R C. Antitumor effect of a normal serum factor (Normal human globin 1) on human tumor cells in vitro. J Natl Cancer Inst 1984; 72: 545–55
  • Shim B-S, Kim I-K. Inhibition of the local Shwartzman reaction by turpentine, prostaglandin E2 and carbon tetrachloride. Vox Sang 1978; 35: 420–2
  • Hwang P I, Greer J. Interaction between hemoglobin subunits in the hemoglobin-haptoglobin complex. J Biol Chem 1980; 255: 3038–41
  • Chiancone E, Alfsen A, Ioppolo C, Vecchini P, Agro A F, Wyman J, et al. Studies on the reaction of haptoglobin with haemoglobin and haemoglobin chains. J Mol Biol 1968; 34: 347–56
  • Ip S HC, Johnson M L, Ackers G K. Kinetics of deoxyhemoglobin subunit dissociation determined by haptoglobin binding. Biochemistry 1976; 15: 654–60

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