Skip to main content
Log in

Characterization of the antigen identified by Po66

A monoclonal antibody raised against a lung squamous cell carcinoma

  • Original Articles
  • Published:
Cancer Immunology, Immunotherapy Aims and scope Submit manuscript

Summary

The mouse monoclonal antibody (mAb) Po66 has been shown in previous work to be localized in nude mice xenografts of human lung tumours when injected intravenously [Dazord L et al. (1987) Cancer Immunol Immunother 24: 263–268] and to be suitable for the scintigraphic detection of lung cancers in patients [Dazord L, et al. (1987) in Klapdor (ed) New tumour markers and their monoclonal antibodies. Georg Thieme, Stuttgart, New York, pp 444–450]. The nature of the antigen recognized by Po66 has been investigated in the present work and comparisons are made with antigens recognized by other mAbs prepared in the laboratory. These mAbs were raised either against lung squamous cell carcinoma (mAbs Po43, Po60), or against a bronchio-alveolar carcinoma (mAbs BAM33, BAM45, BAM54 and BAM69). Radioiodinated purified Po66 did not compete for cell binding with any other mAb. All Po and BAM mAbs reacted with tumour cells both cultured in vitro and grown in vivo. They recognized cytoplasmic antigens as judged by immunofluorescence examination of fixed cells or by immunoperoxidase staining of cancer tissues, but could never be visualized by immunofluorescence on the surface membrane of culture cells. The mAbs of the BAM series reacted with vimentin as demonstrated by immunofluorescence staining, showing alterations in the aspect of the filaments under the effect of colchicin. Radiolabelled mAbs Po43, BAM33 and BAM45 bound to partially purified cytoplasmic cytoskeleton components. In contrast, Po66 was never seen associated with intermediary filaments. The sensitivity to enzyme digestion of the antigen associated with Po66 was studied in comparison with those associated with Po43, BAM33 and BAM45. All antigens were sensitive to protease digestion while only the Po66-identified antigen was sensitive to periodate, neuraminidase and α-fucosidase. Thus, mAb Po66 identified an antigen of 47 kDa (as determined before) present in the cytoplasm but not related to the cytoskeleton, not detected on the cell surface and glycoproteic in nature.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. Blaschek MA, Boehme M, Jouquan J, Simitzis AM, Fifas S, Le Goff P, Youinou P (1988) Relation of antivimentin antibodies to anticardiolipin antibodies in systemic lupus erythematosus. Ann Rheum Dis 47:708–716

    Google Scholar 

  2. Blobel GA, Moll R, Franke WW, Vogt-Moykopf I (1984) Cytokeratins in normal lung and lung carcinomas. I. Adenocarcinomas, squamous cell carcinomas and cultured cell lines. Virchows Arch [8] 45:407–429

    Google Scholar 

  3. Bolton AE (1980) Radioiodination techniques. Amersham Review no. 18

  4. Chatal JF, Fumoleau L, Saccavini JC, Thedrez P, Curtet C, Bianco-Arco A, Chetanneau A, Peltier P, Kremer M, Guillard Y (1987) Immunoscintigraphy of recurrences of gynecological carcinomas. J Nucl Med 28:1807–1819

    Google Scholar 

  5. Dazord L, Bourel D, Martin A, Bourguet P, Jbohy, Saccavini JC, Delaval Ph, Louvet M, Toujas L (1987) A monoclonal antibody (Po66) directed against human lung squamous cell carcinoma. Immunolocalization of tumor xenografts in nude mice. Cancer Immunol Immunother 24:263–268

    Google Scholar 

  6. Dazord L, Martin A, Bourguet P, Bourel B, Saccavini JC, Collet B, Gedouin B, Ramee MP, Toujas L (1987) A monoclonal antibody (Po66) reactive with human lung squamous cell carcinoma. Cell reactivity in vitro and preliminary scintigraphic trials. In: Klapdor (ed) New tumour markers and their monoclonal antibodies. Georg Thieme, Stuttgart, New York, pp 440–450

    Google Scholar 

  7. Doyle LA, Cuttita F, Mulshine JL, Bunn PA, Minna JD (1987) Markedly different antibody responses to immunized small cell and non small cell lung cancer cells. Cancer Res 47:5009–5013

    Google Scholar 

  8. Drezniek J (1973) Substrate specificity of neuraminidase. Histochemical J 5:271–290

    Google Scholar 

  9. Geisler N, Weber K (1981) Comparison of the proteins of two immunologically distinct intermediate-sized filaments by amino acid sequence analysis: desmin and vimentin. Proc Natl Acad Sci USA 78:4120–4123

    Google Scholar 

  10. Godding JW (1983) Monoclonal antibodies: principles and practice: production and application of monoclonal antibodies in cell biology, biochemistry and immunology. Academic Press London, Orlando

    Google Scholar 

  11. Gown AM, Volle AM (1982) Monoclonal antibodies to intermediate filament proteins: unique and cross-reacting antibodies. J Cell Biol 95:414–424

    Google Scholar 

  12. Hellstrom I, Horn D, Linskey P, Brown JP, Brankovan V, Hellstrom KE (1986) Monoclonal mouse antibodies raised against human lung carcinoma. Cancer Res 46:3917–3923

    Google Scholar 

  13. Lazarides E (1980) Mediate filaments as mechanical integrators of cellular space. nature 283:49–256 (La vimentine apparait dans les cellules épithéliales en culture)

    Google Scholar 

  14. Mach JP, Chatal JF, Lumbroso JD, Buchegger F, Forni M, Ritschard J, Berch C, Douillard JY, Carrel S, Herlyn M, Steplewski Z, Koprowski H (1983) Tumor localization in patients by radiolabeled monoclonal antibodies against colon carcinoma. Cancer Res 43:5593–5600

    Google Scholar 

  15. McNutt MA, Bolen JW, Gown AM, Hammar SP, Vogel AM (1985) Coexpression of intermediate filaments in human epithelial neoplasms. Ultrastruct Pathol 9:31–43

    Google Scholar 

  16. Myoken Y, Moroyama T, Miyauchi S, Takada K, Namba M (1987) Monoclonal antibodies against human oral squamous cell carcinoma reacting with keratin proteins. Cancer 60:2927–2937

    Google Scholar 

  17. Osborn M, Altmannsberger M, Debus E, Weber K (1985) Differentiation of the major human tumor groups using conventional and monoclonal antibodies specific for individual intermediate filament proteins. Ann NY Acad Sci: 649–668

  18. Paw E (1985) Heterogenous expression of cell-surface antigens in normal epithelia and their tumours, revealed by monoclonal antibodies. Br J Cancer 51:149

    Google Scholar 

  19. Pruss RM, Mirskey R, Raff MC, Thorpe R, Dowding AJ, Anderson BH (1981) All classes of intermediate filaments share a common antigenic determinant defined by a monoclonal antibody. Cell 27:419–428

    Google Scholar 

  20. Siccardi AG, Buraggi GL, Callegaro L, Mariani G, Natali PG, Abbati A, Bestagno M, Caputo V, Mansi L, Masi R, Paganelli G, Riva P, Salvatore M, Sanguineti M, Troncone L, Turco GL, Scassellati GA, Ferrone S (1986) Multicenter study of immunoscintigraphy with radiolabelled monoclonal antibodies in patients with melanoma. Cancer Res 46:4817–4822

    Google Scholar 

  21. Wagenaar SJ, Hilgers J, Smitz du Moulin F, Schol D, Verstijnen C, Hilkens J, Osanto S, Vanderschueren RM (1984) Patterns of expression of some new antigens of human bronchial carcinomas. Protides Biol Fluids 521–524

  22. West CM (1986) Current ideas on the significance of protein glycosylation. Mol Cell Biochem 72:3–20

    Google Scholar 

  23. Youinou P, Le Goff P, Colaco CB, Thivolet J, Tater D, Viac J, Shipley M (1985) Antikeratin antibodies in serum and synovial fluid show specificity for rheumatoid arthritis in a study of connective tissue diseases. Ann Rheum Dis 44:450–454

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Martin, A., Pellen, P., Guitton, C. et al. Characterization of the antigen identified by Po66. Cancer Immunol Immunother 29, 118–124 (1989). https://doi.org/10.1007/BF00199286

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00199286

Keywords

Navigation