Skip to main content
NCBI home page
Japanese Journal of Cancer Research : Gann logoLink to Japanese Journal of Cancer Research : Gann
. 1991 Jul;82(7):862–870. doi: 10.1111/j.1349-7006.1991.tb02714.x

Detection of Bone‐type Alkaline Phosphatase by Monoclonal Antibodies Reacting with Human Osteosarcoma‐associated Antigen

Satoshi Nagoya 1, Toshimitsu Uede 1,2, Takuro Wada 3, Seiichi Ishii 3, Shinya Yamawaki 4, Kokichi Kikuchi 1
PMCID: PMC5918541  PMID: 1715340

Abstract

The antigen detected by monoclonal antibodies reacting with human osteosarcoma‐associated antigen was shown to he a phosphatidyl‐inositol (Pl)‐glycan‐anchored protein, which can be released from the cell surface by PI‐specific phospholipase C‐treatment. The antigen detected by 2D3 and 2H10 antibodies exhibited alkaline phosphatase activity. Both antibodies strongly reacted with bone‐type alkaline phosphatase. However, importantly, immunohistochemical analysis demonstrated that 2D3 and 2H10 did not react with alkaline phosphatase present in kidney or liver. In addition, neither placental nor intestinal alkaline phosphatase was recognized by 2D3 and 2H10 antibodies. These results indicated that two monoclonal antibodies, 2D3 and 2H10, are highly specific for bone‐type alkaline phosphatase and can distinguish bone alkaline phosphatase from liver alkaline phosphatase in spite of the fact that liver and bone alkaline phosphatase are encoded by the same gene.

Keywords: Bone‐type alkaline phosphatase, Monoclonal antibody, Osteosarcoma

Full Text

The Full Text of this article is available as a PDF (1.1 MB).

REFERENCES

  • 1. ) Farley , J. R. and Baylink , D. J.Skeletal alkaline phosphatase activity as a bone formation index in vitro . Metabolism , 35 , 563 – 571 ( 1986. ). [DOI] [PubMed] [Google Scholar]
  • 2. ) Tsang , K. Y. , Warren , R. Q. , Bishop , L. , Pathak , S. , Koger , B. and Lavia , M. F.Monoclonal antibodies to human osteosarcoma‐associated antigen(s) . J. Natl Cancer Inst. , 77 , 1175 – 1180 ( 1986. ). [PubMed] [Google Scholar]
  • 3. ) Hosoi , S. , Nakamura , T. , Yamamuro , T. , Toyama , S. , Shinomiya , K. and Mikawa , H.Detection of human osteosarcoma‐associated antigen(s) by monoclonal antibodies . Cancer Res. , 42 , 654 – 659 ( 1982. ). [PubMed] [Google Scholar]
  • 4. ) Tanaka , C. , Yamamuro , T. , Masuda , T. , Tanaka , H. , Matsumoto , M. , Katoura , Y. , Tsuji , T. , Toguchida , J. , Miyama‐Inaba , M. and Ueda , M.Recognition of serum alkaline phosphatase by murine monoclonal antibodies against human osteosarcoma cells . Cancer Res. , 46 , 4863 – 4857 ( 1986. ). [PubMed] [Google Scholar]
  • 5. ) Wada , T. , Uede , T. , Ishii , S.Matsuyama , K. , Yamawaki , S. , and Kikuchi , K.Monoclonal antibodies that detect different antigenic determinants of the same Human osteosarcoma‐associated antigen . Cancer Res. , 48 , 2273 – 2279 ( 1988. ). [PubMed] [Google Scholar]
  • 6. ) Tsai , C. C. , McGuire , M. H. , Mellitt , R. J. , Ritter , R. A. , III , Xu , J. , Litwicki , D. J. and Roodman , S. T.Monoclonal antibody to human osteosarcoma: a novel Mr 26,000 protein recognized by murine hybridoma TMMR.2 . Cancer Res. , 50 , 152 – 158 ( 1990. ). [PubMed] [Google Scholar]
  • 7. ) Seargeant , L. E , and Stinson , R. A.Evidence that three structural genes code for human alkaline phosphatases . Nature , 281 , 152 – 154 ( 1979. ). [DOI] [PubMed] [Google Scholar]
  • 8. ) Weiss , M. J. , Henthorn , P. S. , Lafferty , M. A. , Slaughter , C. , Raducha , M. and Harris , H.Isolation and characterization of a cDNA encoding a human liver/bone/kidney‐type alkaline phosphatase . Proc. Natl. Acad. Sci. USA , 83 , 7182 – 7186 ( 1986. ). [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 9. ) Lawson , G. M. , Katzmann , J. A. , Kimlinger , T. K. and O'Brien , F.Isolation and preliminary characterization of a monoclonal antibody that interacts preferentially with the liver isoenzyme of human alkaline phosphatase . Clin. Chem. , 31 , 381 – 385 ( 1985. ). [PubMed] [Google Scholar]
  • 10. ) Rosalki , S. B. and Ying Foo , A.Two new methods for separation and quantifying bone and liver alkaline phosphatase isoenzymes in plasma . Clin. Chem. , 30 , 1182 – 1186 ( 1984. ). [PubMed] [Google Scholar]
  • 11. ) Moss , D. W. and Whitby , L. G.A simplified heat‐inactivation method for investigating alkaline phosphatase isoenzymes in serum . Clin. Chim. Acta , 61 , 63 – 71 ( 1975. ). [DOI] [PubMed] [Google Scholar]
  • 12. ) Goseki , M. , Oida , S. and Sasaki , S.Detection of minor immunological differences among human universal‐type alkaline phosphatases . J. Cell. Biochem. , 38 , 155 – 163 ( 1988. ). [DOI] [PubMed] [Google Scholar]
  • 13. ) Billian , A. , Edy , V‐G. , Heremans , H. , Damme , J. V. , Desmyter , J. , Georgiades , J. A. and Somer , P. D.Human interferon: mass production in a newly established cell line, MG63 . Antimicrob. Agents Chemother. , 12 , 11 – 15 ( 1977. ). [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 14. ) Griffin , J. D. , Ritz , J. , Naddler , L. M. and Schlossman , S. F.Expression of myeloid differentiation antigens on normal and malignant myeloid cells . J. Clin. Invest. , 68 , 932 – 941 ( 1981. ). [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 15. ) Uede , T. , Kohda , H. , Yuasa , H. , Osawa , H. , Diamantstein , T. , Yodoi , J. , Ishii , Y. and Kikuchi , K.5C6‐F4, a novel 100KD rat lymphocyte activation antigen defined by monoclonal antibody . J. Immunol. , 136 , 3968 – 3976 ( 1986. ). [PubMed] [Google Scholar]
  • 16. ) Kind , P. R. N. and King , E. J.Estimation of plasma phosphatase by determination of hydrolysed phenol with amino‐antipyrine . J. Clin. Pathol , 7 , 322 – 326 ( 1954. ). [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 17. ) Home , M. , Cornish , C. J. and Posen , S.The use of urea denaturation in the identification of human alkaline phosphatases . J. Lab. Clin. Med. , 72 , 905 – 915 ( 1968. ). [PubMed] [Google Scholar]
  • 18. ) Behr , W. and Barnert , J.Quantification of bone alkaline phosphatase in serum by precipitation with wheat‐germ lectin: a simplified method and its clinical plausibility . Clin. Chem. , 32 , 1960 – 1966 ( 1986. ). [PubMed] [Google Scholar]
  • 19. ) Schreiber , W. E. and Sadro , L. C.Agarose gel patterns of alkaline phosphatase isoenzymes before and after treatment with neuraminidase . Am. J. Clin. Pathol. , 89 , 181 – 186 ( 1988. ). [DOI] [PubMed] [Google Scholar]
  • 20. ) Lorentz , K.Katalytische Konsentration, multiple Formen und Lektin affinitat von mikrosomalen Enzymen menschliches Gewebe . J. Clin. Chem. Clin. Biochem. , 19 , 1181 – 1187 ( 1981. ). [PubMed] [Google Scholar]
  • 21. ) Lehmann , F. G.Differentiation of human alkaline phosphatases by lectin binding affinity . Klin. Wochenshr. , 58 , 947 – 951 ( 1980. ). [DOI] [PubMed] [Google Scholar]
  • 22. ) Seabrook , R. N. , Bailyes , E. M. , Price , C. P. , Siddle , K. and Luzio , J. P.The distinction of bone and liver isoenzymes of alkaline phosphatase in serum using a monoclonal antibody . Clin. Chim. Acta , 172 , 261 – 266 ( 1988. ). [DOI] [PubMed] [Google Scholar]
  • 23. ) Low , M. G. and Satiel , A. R.Structural and functional roles of glycosylphosphatidylinositol in membranes . Science , 239 , 268 – 275 ( 1988. ). [DOI] [PubMed] [Google Scholar]
  • 24. ) Low , M. G.Glycosyl‐phosphatidylinositol: a versatile anchor for cell surface proteins . FASEB J. , 3 , 1600 – 1608 ( 1989. ). [DOI] [PubMed] [Google Scholar]

Articles from Japanese Journal of Cancer Research : Gann are provided here courtesy of Wiley

RESOURCES