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British Journal of Cancer logoLink to British Journal of Cancer
. 1992 Feb;65(2):300–302. doi: 10.1038/bjc.1992.60

An evaluation of the prognostic significance of alpha-1-antitrypsin expression in adenocarcinomas of the lung: an immunohistochemical analysis.

M Higashiyama 1, O Doi 1, K Kodama 1, H Yokouchi 1, R Tateishi 1
PMCID: PMC1977730  PMID: 1739634

Abstract

Expression of alpha-1-antitrypsin (AAT) in tumour cells of 102 surgically resected lung adenocarcinomas was examined by immunohistochemical method using anti-AAT antiserum. While only 13 cases (13%) were negative for AAT expression, 89 cases (87%) contained AAT at varying degrees. The degree of AAT-positive tumour cells was significantly higher in advanced cases than in early cases. Clinical follow-up study of the patients, particularly in stage I, showed that strongly AAT-positive cases have poor prognosis than weak-to-moderately AAT-positive or AAT-negative cases. Thus, AAT expression status in tumour cells of lung adenocarcinoma may be a biological marker of prognostic significance in regard to tumour growth.

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Selected References

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  1. Ades E. W., Hinson A., Chapuis-Cellier C., Arnaud P. Modulation of the immune response by plasma protease inhibitors. I. Alpha 2-macroglobulin and alpha 1-antitrypsin inhibit natural killing and antibody-dependent cell-mediated cytotoxicity. Scand J Immunol. 1982 Jan;15(1):109–113. doi: 10.1111/j.1365-3083.1982.tb00628.x. [DOI] [PubMed] [Google Scholar]
  2. Aroni K., Kittas C., Papadimitriou C. S., Papacharalampous N. X. An immunocytochemical study of the distribution of lysozyme, a1-antitrypsin and a1-antichymotrypsin in the normal and pathological gall bladder. Virchows Arch A Pathol Anat Histopathol. 1984;403(3):281–289. doi: 10.1007/BF00694904. [DOI] [PubMed] [Google Scholar]
  3. Arora P. K., Miller H. C., Aronson L. D. alpha1-Antitrypsin is an effector of immunological stasis. Nature. 1978 Aug 10;274(5671):589–590. doi: 10.1038/274589a0. [DOI] [PubMed] [Google Scholar]
  4. Beatty K., Bieth J., Travis J. Kinetics of association of serine proteinases with native and oxidized alpha-1-proteinase inhibitor and alpha-1-antichymotrypsin. J Biol Chem. 1980 May 10;255(9):3931–3934. [PubMed] [Google Scholar]
  5. Beatty K., Travis J., Bieth J. The effect of alpha 2-macroglobulin on the interaction of alpha 1-proteinase inhibitor with porcine trypsin. Biochim Biophys Acta. 1982 Jun 4;704(2):221–226. doi: 10.1016/0167-4838(82)90149-2. [DOI] [PubMed] [Google Scholar]
  6. Eisen A. Z., Bloch K. J., Sakai T. Inhibition of human skin collagenase by human serum. J Lab Clin Med. 1970 Feb;75(2):258–263. [PubMed] [Google Scholar]
  7. Geboes K., Ray M. B., Rutgeerts P., Callea F., Desmet V. J., Vantrappen G. Morphological identification of alpha-I-antitrypsin in the human small intestine. Histopathology. 1982 Jan;6(1):55–60. doi: 10.1111/j.1365-2559.1982.tb02701.x. [DOI] [PubMed] [Google Scholar]
  8. Glasgow J. E., Bagdasarian A., Colman R. W. Functional alpha 1 protease inhibitor produced by a human hepatoma cell line. J Lab Clin Med. 1982 Jan;99(1):108–117. [PubMed] [Google Scholar]
  9. Hsu S. M., Raine L., Fanger H. Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: a comparison between ABC and unlabeled antibody (PAP) procedures. J Histochem Cytochem. 1981 Apr;29(4):577–580. doi: 10.1177/29.4.6166661. [DOI] [PubMed] [Google Scholar]
  10. Karashima S., Kataoka H., Itoh H., Maruyama R., Koono M. Prognostic significance of alpha-1-antitrypsin in early stage of colorectal carcinomas. Int J Cancer. 1990 Feb 15;45(2):244–250. doi: 10.1002/ijc.2910450207. [DOI] [PubMed] [Google Scholar]
  11. Kataoka H., Nabeshima K., Komada N., Koono M. New human colorectal carcinoma cell lines that secrete proteinase inhibitors in vitro. Virchows Arch B Cell Pathol Incl Mol Pathol. 1989;57(3):157–165. doi: 10.1007/BF02899077. [DOI] [PubMed] [Google Scholar]
  12. Kittas C., Aroni K., Kotsis L., Papadimitriou C. S. Distribution of lysozyme, alpha 1-Antichymotrypsin and alpha 1-Antitrypsin in adenocarcinomas of the stomach and large intestine. An immunohistochemical study. Virchows Arch A Pathol Anat Histopathol. 1982;398(2):139–147. doi: 10.1007/BF00618865. [DOI] [PubMed] [Google Scholar]
  13. Kittas C., Aroni K., Matani A., Papadimitriou C. S. Immunocytochemical demonstration of a1-Antitrypsin and a1-Antichymotrypsin in human gastrointestinal tract. Hepatogastroenterology. 1982 Dec;29(6):275–277. [PubMed] [Google Scholar]
  14. Koj A., Chudzik J., Pajdak W., Dubin A. The occurrence of common inhibitors of trypsin and of leucocyte neutral proteinase in human serum. Biochim Biophys Acta. 1972 Apr 7;268(1):199–206. doi: 10.1016/0005-2744(72)90215-x. [DOI] [PubMed] [Google Scholar]
  15. Krugliak L., Meyer P. R., Taylor C. R. The distribution of lysozyme, alpha-1-antitrypsin, and alpha-1-antichymotrypsin in normal hematopoietic cells and in myeloid leukemias: an immunoperoxidase study on cytocentrifuge preparations, smears, and paraffin sections. Am J Hematol. 1986 Jan;21(1):99–109. doi: 10.1002/ajh.2830210112. [DOI] [PubMed] [Google Scholar]
  16. McKeehan W. L., Sakagami Y., Hoshi H., McKeehan K. A. Two apparent human endothelial cell growth factors from human hepatoma cells are tumor-associated proteinase inhibitors. J Biol Chem. 1986 Apr 25;261(12):5378–5383. [PubMed] [Google Scholar]
  17. Mignatti P., Robbins E., Rifkin D. B. Tumor invasion through the human amniotic membrane: requirement for a proteinase cascade. Cell. 1986 Nov 21;47(4):487–498. doi: 10.1016/0092-8674(86)90613-6. [DOI] [PubMed] [Google Scholar]
  18. Perlmutter D. H., Daniels J. D., Auerbach H. S., De Schryver-Kecskemeti K., Winter H. S., Alpers D. H. The alpha 1-antitrypsin gene is expressed in a human intestinal epithelial cell line. J Biol Chem. 1989 Jun 5;264(16):9485–9490. [PubMed] [Google Scholar]
  19. Ray M. B., Desmet V. J. Immunohistochemical demonstration of alpha-1-antitrypsin in the islet cells of human pancreas. Cell Tissue Res. 1978 Feb 14;187(1):69–77. doi: 10.1007/BF00220619. [DOI] [PubMed] [Google Scholar]
  20. Redelman D., Hudig D. The mechanism of cell-mediated cytotoxicity. I. Killing by murine cytotoxic T lymphocytes requires cell surface thiols and activated proteases. J Immunol. 1980 Feb;124(2):870–878. [PubMed] [Google Scholar]
  21. Reintoft I., Hägerstrand I. Demonstration of alpha 1-antitrypsin in hepatomas. Arch Pathol Lab Med. 1979 Sep;103(10):495–498. [PubMed] [Google Scholar]
  22. Rimon A., Shamash Y., Shapiro B. The plasmin inhibitor of human plasma. IV. Its action on plasmin, trypsin, chymotrypsin, and thrombin. J Biol Chem. 1966 Nov 10;241(21):5102–5107. [PubMed] [Google Scholar]
  23. Sawaya R., Zuccarello M., Highsmith R. Alpha-1-antitrypsin in human brain tumors. J Neurosurg. 1987 Aug;67(2):258–262. doi: 10.3171/jns.1987.67.2.0258. [DOI] [PubMed] [Google Scholar]
  24. Soini Y., Miettinen M. Alpha-1-antitrypsin and lysozyme. Their limited significance in fibrohistiocytic tumors. Am J Clin Pathol. 1989 May;91(5):515–521. doi: 10.1093/ajcp/91.5.515. [DOI] [PubMed] [Google Scholar]
  25. Tahara E., Ito H., Taniyama K., Yokozaki H., Hata J. Alpha 1-antitrypsin, alpha 1-antichymotrypsin, and alpha 2-macroglobulin in human gastric carcinomas: a retrospective immunohistochemical study. Hum Pathol. 1984 Oct;15(10):957–964. doi: 10.1016/s0046-8177(84)80125-2. [DOI] [PubMed] [Google Scholar]
  26. Tryggvason K., Höyhtyä M., Salo T. Proteolytic degradation of extracellular matrix in tumor invasion. Biochim Biophys Acta. 1987 Nov 25;907(3):191–217. doi: 10.1016/0304-419x(87)90006-0. [DOI] [PubMed] [Google Scholar]
  27. Tuttle W. C., Jones R. K. Fluorescent antibody studies of alpha-1-antitrypsin in adult human lung. Am J Clin Pathol. 1975 Oct;64(4):477–482. doi: 10.1093/ajcp/64.4.477. [DOI] [PubMed] [Google Scholar]
  28. Wittekind C., Wachner R., Henke W., von Kleist S. Localization of CEA, HCG, lysozyme, alpha-1-antitrypsin, and alpha-1-antichymotrypsin in gastric cancer and prognosis. Virchows Arch A Pathol Anat Histopathol. 1986;409(5):715–724. doi: 10.1007/BF00713436. [DOI] [PubMed] [Google Scholar]
  29. Zucker S. A critical appraisal of the role of proteolytic enzymes in cancer invasion: emphasis on tumor surface proteinases. Cancer Invest. 1988;6(2):219–231. doi: 10.3109/07357908809077049. [DOI] [PubMed] [Google Scholar]

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