Biology of Human Alkaline Phosphatases with Special Reference to Cancer

References

• Kay H. D. Plasma phosphatase. II. The enzyme in disease particularly in bone disease. J Biol Chem 1930; 89: 249–66
   Google Scholar
• Franseen C. C., McLean R. The phosphatase activity of tissues and plasma in tumors of bone. Am J Cancer 1935; 24: 299–317
   Google Scholar
• Robison R. The possible significance of hexosephosphoric esters in ossification. Biochem J 1923; 17: 286–93
   PubMedGoogle Scholar
• Fernley H. N. Mammalian alkaline phosphatases. The enzymes, P. D. Boyer. Academic Press, New York 1971; Vol. 4.: 414–47
   Google Scholar
• Fishman W. H. Perspectives on alkaline phosphatase isoenzymes. Am J Med 1974; 56: 617–50
   PubMed Web of Science ®Google Scholar
• McComb R. B., Bowers GN, Posen S. Alkaline phosphatases. Plenum, New York 1979
   Google Scholar
• Moss D. W. Isoenzymes. Chapman and Hall Ltd., Great Britain 1982
   Google Scholar
• Harris H. The human alkaline phosphatases: what we know and what we don't know. Clin Chim Acta 1990; 186: 133–150
   PubMed Web of Science ®Google Scholar
• De Broe M. E., Moss D. W. Recent developments in alkaline phosphatase research. Clin Chem 1992; 38: 2484–546
   PubMedGoogle Scholar
• Griffin C. A., Smith M., Henthom PS, et al. Human placental alkaline phosphatase genes map to 2q34-q37. Am J Hum Genet 1987; 1: 1025–34
   Google Scholar
• Martin D., Tucker D. F., Gorman P., et al. The human placental alkaline phosphatase gene and related sequences map to chromosomes 2 band q37. Ann Hum Genet 1987; 51: 145–52
   PubMedGoogle Scholar
• Raimondi E., Talarico D., Moro L., et al. Regional mapping of the human placental alkaline phosphatase gene (ALPP) to 2q37 by in situ hybridization. Cytogenet Cell Genet 1988; 47: 98–9
   PubMedGoogle Scholar
• Smith M., Weiss M. J., Griffin C.A., et al. Regional assignment of the gene for human liver/bone kidney alkaline phosphatase to chromosome Ip36.1-p34. J. Genomics 1988; 2: 139–43
   PubMedGoogle Scholar
• Swallow D. M., Povey S., Parkar M., et al. Mapping of the gene coding for the human liver/bone kidney isozyme of alkaline phosphatase to chromosome 1. J Ann Hum Genet 1986; 50: 229–35
   PubMedGoogle Scholar
• Knoll B. J., Rothblum KN, Longley M. Nucleotide sequence of the human placental alkaline phosphatase gene: evolution of the 5' flanking region by deletion/substitution. J Biol Chem 1988; 263: 12020–7
   PubMed Web of Science ®Google Scholar
• Henthom P. S., Raducha M., Kadesch T., et al. Sequence and characterization of the human intestinal alkaline phosphatase gene. J Biol Chem 1988; 263: 12011–9
   PubMedGoogle Scholar
• Millin JL, Manes T. Seminoma-derived Nagao isozyme is encoded by a germ-cell alkaline phosphatase gene. Proc Natl Acad Sci USA 1988; 85: 3024–8
   PubMedGoogle Scholar
• Beckman G., Beckman L., Sikström C., et al. DNA polymorphism of alkaline phosphatase isozyme genes: linkage disequilibria between placental and germ-cell alkaline phosphatase alleles. Am J Hum Genet 1992; 51: 1066–70
   PubMedGoogle Scholar
• Ovitt C. E., Strauss A. W., Alpers D. H., et al. Expression of different-sized placental alkaline phosphatase mRNAs in placenta and choriocarcinoma cells. Proc Natl Acad Sci USA 1986; 83: 3781–5
   PubMedGoogle Scholar
• Gum R. R., Kam J. C., Hicks J. W., et al. Effects of sodium butyrate on human colonic adenocarcinoma cells. J Biol Chem 1987; 262: 1092–7
   PubMed Web of Science ®Google Scholar
• Chou J. Y., Takashashi S. Control of placental alkaline phosphatase gene expression in HeLa cells: induction of synthesis by prednisolone and sodium butyrate. Biochemistry 1987; 26: 3596–601
   PubMedGoogle Scholar
• Weiss M. J., Ray K., Henthom P. S., et al. Structure of the human liver/bone/kidney alkaline phosphatase gene. J Biol Chem 1988; 263: 12002–10
   PubMed Web of Science ®Google Scholar
• Toh Y., Yamamoto M., Endo H., et al. Isolation and characterization of a rat liver alkaline phosphatase gene – a single gene with two promoters. Eur J Biochem 1989; 182: 231–7
   PubMedGoogle Scholar
• Terao M., Studer M., Gianni M., et al. Isolation and characterization of the mouse liver/bone. J kidney-type alkaline phosphatase gene.Biochem J 1990; 268: 641–8
   Google Scholar
• Matsuura S., Kishi F, Kajii T. Characterization of a 5'-flanking region of the human liver. J bone/kidney alkaline phosphatase gene: two kinds of mRNA from a single gene.Biochem Biophys Res Commun 1990; 168: 993–1000
   Google Scholar
• Toh Y., Yamamoto M., Endo H., et al. Duplicate leader exons in the mouse liver-type alkaline phosphatase gene. Biochem Int 1990; 22: 213–8
   PubMedGoogle Scholar
• Toh Y., Yamamoto M., Endo H., et al. Sequence divergence of 5' extremities in rat liver alkaline phosphatase mRNAs. J Biochem 1989; 105: 61–5
   PubMedGoogle Scholar
• Knoll B. J., Rothblum KN, Longley M. Two gene duplication events in the evolution of the human heat-stable alkaline phosphatase. Gene 1987; 60: 267–76
   PubMedGoogle Scholar
• Kam W., Clauser E., Kim Y. S., et al. Cloning, sequencing, and chromosomal localization of human term placental alkaline phosphatase cDNA. Proc Natl Acad Sci USA 1985; 82: 8715–9
   PubMed Web of Science ®Google Scholar
• Millan J. L. Molecular cloning and sequence analysis of human placental alkaline phosphatase. J Biol Chem 1986; 261: 3112–5
   PubMed Web of Science ®Google Scholar
• Henthom P. S., Knoll B. J., Raducha M., et al. Products of two common alleles at the locus for human placental alkaline phosphatase differ by seven amino acids. Proc Natl Acad Sci USA 1986; 83: 5597–601
   PubMedGoogle Scholar
• Weiss M. J., Henthom P. S., Lafferty M. A., et al. Isolation and characterization of a cDNA encoding a human liver/bone/kidney-type alkaline phosphatase. Proc Natl Acad Sci USA 1983; 83: 7182–6
   Google Scholar
• Henthom P. S., Raducha M., Edwards Y. H., et al. Nucleotide and amino acid sequences of human intestinal alkaline phosphatase: close homology to placental alkaline phosphatase. Proc Natl Acad Sci USA 1987; 84: 1234–8
   PubMedGoogle Scholar
• Berger J., Garattini E, Udenfriend S. Cloning and sequencing of human intestinal alkaline phosphatase cDNA. Proc Natl Acad Sci USA 1987; 84: 7182–6
   Google Scholar
• Millán JL. Oncodevelopmental expression and structure of alkaline phosphatase genes. Anticancer Res 1988; 8: 995–1004
   PubMedGoogle Scholar
• Low M. G., Saltiel A. R. Structural and functional roles of glycosylphosphatidylinositol in membranes. Science 1988; 239: 268–75
   PubMed Web of Science ®Google Scholar
• Micanovic R., Bailey C. A., Brink L., et al. Aspartic acid-484 of nascent placental alkaline phosphatase condenses with a phosphatidylinositol glycan to become the carboxyl terminus of the mature enzyme. Proc Natl Acad Sci USA 1988; 85: 1398
   PubMedGoogle Scholar
• Takami N., Ogata S., Oda K., et al. Biosynthesis of placental alkaline phosphatase and its posttranslational modification by glycophospholipid for membrane-anchoring. J Biol Chem 1988; 263: 3016–3021
   PubMedGoogle Scholar
• Endo T., Ohbayashi H., Hayashi Y., et al. Structural study on the carbohydrate moiety of human placental alkaline phosphatase. J Biochem 1988; 103: 182–7
   PubMedGoogle Scholar
• Watanabe T., Wada N, Chou J. Y. Structural and functional analysis of human germ cell alkaline phosphatase by site-directed mutagenesis. Biochemistry 1992; 31: 3051–8
   PubMedGoogle Scholar
• Sowadski J. M., Handschumacher M. D., Murthy HMK, et al. Refined structure of alkaline phosphatase from Escherichia coli at 2.8 Å resolution. J Mol Biol 1985; 186: 417–33
   PubMed Web of Science ®Google Scholar
• Weissig H., Schildge A., Hoylaerts M. F., et al. Cloning and expression of the bovine intestinal alkaline phosphatase gene: biochemical characterization of the recombinant enzyme. Biochem J 1993; 290: 503–8
   PubMedGoogle Scholar
• Micanovic R., Gerber L. D., Berger J., et al. Selectivity of the cleavage/attachment site of phosphatidylinositol-glycan-anchored membrane proteins determined by site-specific mutagenesis at Asp-484 of placental alkaline phosphatase. Proc Natl Acad Sci USA 1990; 87: 157–61
   PubMed Web of Science ®Google Scholar
• Lowe M. E. Site-specific mutations in the COOH-terminus of placental alkaline phosphatase: a single amino acid change converts a phosphatidylinositol-glycan-anchored protein to a secreted protein. J Cell Biol 1992; 116: 799–807
   PubMedGoogle Scholar
• Kodukula K., Gerber L. D., Amthauer R., et al. Biosynthesis of glycosylphosphatidylinositol (GPI)-anchored membrane proteins in intact cells; specific amino acid requirements adjacent to the site of cleavage and GPI attachment. J Cell Biol 1993; 120: 657–64
   PubMed Web of Science ®Google Scholar
• Udenfriend S., Kodukula K, Amthauer R. Cell-free processing of nascent proteins destined to be linked to the plasma membrane by a phosphatidylinositol-glycan anchor. Cell Mol Biol 1992; 38: 1–16
   PubMedGoogle Scholar
• Low M. G., Finean J. B. Release of alkaline phosphatase from membranes by a phosphatidyl inositol-specific phospholipase C. Biochem J 1977; 167: 281–4
   PubMed Web of Science ®Google Scholar
• Ghosh N. K., Fishman W. H. On the mechanism of inhibition of intestinal alkaline phosphatase by L-phenylalanine. I. Kinetic studies. J Biol Chem 1966; 241: 2516–22
   PubMed Web of Science ®Google Scholar
• Fishman W. H., Sie H-G. Organ-specific inhibition of human alkaline phosphatase isoenzymes of liver, bone, intestine and placenta: L-phenylalanine. L-tryptophan and L-homoarginine. Enzymologia 1971; 41: 140–67
   Google Scholar
• Lin C. W., Sie H-G, Fishman W. H. L-Tryptophan: a homosteric, organ-specific uncompetitive inhibitor of human placental alkaline phosphatase. Biochem J 1971; 124: 509–16
   PubMed Web of Science ®Google Scholar
• Doellgast G. J., Fishman W. H. L-Leucine, a specific inhibitor of a rare human placental alkaline phosphatase phenotype. Nature 1976; 259: 49–51
   PubMed Web of Science ®Google Scholar
• Fishman W. H. On the importance of being (stereo) specific. Clin ChimActa 1989; 186: 129–32
   Google Scholar
• Green S., Antiss CL, Fishman W. H. Automated differential analysis, n. The fractionation of serum alkaline phosphatases into “liver”, “intestinal” and “other” components. Enzymologia 1971; 41: 9–26
   PubMedGoogle Scholar
• Mulivor R. A., Plotkin LI, Harris H. Differential inhibition of the products of the human alkaline phosphatase. Ann Hum Genet 1978; 42: 1–13
   PubMed Web of Science ®Google Scholar
• Hummer C., Millan J. L. Gly429 is the major determinant of uncompetitive inhibition of human germ cell alkaline phosphatase by L-leucine. Biochem J 1991; 274: 91–5
   PubMedGoogle Scholar
• Watanabe T., Wada N., Kim E. E., et al. Mutation of a single amino acid converts germ cell alkaline phosphatase to placental alkaline phosphatase. J Biol Chem 1991; 266: 21174–8
   PubMedGoogle Scholar
• Hoylaerts M. F., MillSn J. L. Site-directed mutagenesis and epitope-mapped monoclonal antibodies define a catalytically important conformational difference between human placental and germ cell alkaline phosphatase. Eur J Biochem 1991; 202: 605–16
   PubMedGoogle Scholar
• Hoylaerts M. F., Manes T, Millan J. L. Molecular mechanism of uncompetitive inhibition of human placental and germ cell alkaline phosphatase. Biochem J 1992; 286: 23–30
   PubMed Web of Science ®Google Scholar
• Tsonis P. A., Argraves WS, Millan J. L. A putative functional domain of human placental alkaline phosphatase predicted from sequence comparison. Biochem J 1988; 254: 623–4
   PubMed Web of Science ®Google Scholar
• Millán J. L. Oncodevelopmental alkaline phosphatases: in search for a function. Prog Clin Biol Res 1990; 344: 453–75
   PubMedGoogle Scholar
• Vittur F., Stagni N., Moro L., et al. Alkaline phosphatase binds to coDagen: a hypothesis on the mechanism of extravesicular mineralization in epiphyseal cartilage. Experientia 1984; 40: 836–7
   PubMedGoogle Scholar
• Wu LNY, Genge B. R., Lloyd G. C., et al. Collagen-binding proteins in collagenase-released matrix vesicles from cartilage. J Biol Chem 1991; 266: 1195–203
   PubMed Web of Science ®Google Scholar
• Makiya R., Stigbrand T. Placental alkaline phosphatase has a binding site for the human immunoglobulin-G Fc portion. Eur J Biochem 1992; 205: 341–5
   PubMedGoogle Scholar
• Makiya R., Stigbrand T. Placental alkaline phosphatase is related to human IgG internalization in Hep2 cells. Biochem Biophys Res Comm 1992; 182: 624–30
   PubMed Web of Science ®Google Scholar
• Bossi M., Hoylaerts MF, Millan J. L. Modifications in a flexible surface loop modulate the isozyme-specific properties of mammalian alkaline phosphatases. J Biol Chem 1993; 268: 25409–16
   PubMedGoogle Scholar
• Millán J. L., Stigbrand T. Antigenic determinants of human placental and testicular placental-like alkaline phosphatase as mapped by monoclonal antibodies. Eur J Biochem 1983; 136: 1–7
   PubMedGoogle Scholar
• Millán JL, Beckman G., Jeppsson A., et al. Genetic variants of placental alkaline phosphatase as detected by a monoclonal antibody. Hum Genet 1982; 60: 145–9
   PubMedGoogle Scholar
• Millán J. L., Stigbrand T., Ruoslahti E., et al. Characterization and use of an allotype-specific monoclonal antibody to placental alkaline phosphatase in the study of cancer-related phosphatase polymorphism. Cancer Res 1982; 42: 2444–9
   PubMed Web of Science ®Google Scholar
• Stigbrand T., Jemmerson R., Millan J. L., et al. A hidden antigenic determinant on membrane-bound human placental alkaline phosphatase. Tumor Biol. 1987; 8: 34–44
   PubMedGoogle Scholar
• Jemmerson R., Stigbrand T. Monoclonal antibodies block the trypsin cleavage site on human placental alkaline phosphatase. FEBS Lett 1984; 173: 357–9
   PubMedGoogle Scholar
• Jemmerson R., Millan J. L., Klier G., et al. Monoclonal antibodies block the bromelain-mediated release of human placental alkaline phosphatase from cultured cancer cells. FEBS Lett 1985; 179: 316–20
   PubMedGoogle Scholar
• Takeya M., Klier FG, Fishman W. H. Molecular dimensions of the SS and FF phenotypes of human placental alkaline phosphatase: rotary shadowing and negative staining electron microscope measurements. J Mol Biol 1984; 173: 253–64
   PubMedGoogle Scholar
• Harris H. The principles of human biochemical genetics.3rd ed. Elsevier/North-Holland, Amsterdam 1980
   Google Scholar
• Robson E. B., Harris H. Generics of the alkaline phosphatase polymorphism of the human placenta. Nature 1965; 207: 1257–9
   PubMed Web of Science ®Google Scholar
• Beckman L., Bjorling G. Christodoulou C. Pregnancy enzymes and placental polymorphism. I. Alkaline phosphatase. Acta Genet (Basel) 1966; 16: 59–73
   PubMedGoogle Scholar
• Donald L. J., Robson E. B. Rare variants of placental alkaline phosphatase. Ann Hum Genet 1974; 37: 303–13
   PubMed Web of Science ®Google Scholar
• Slaughter C. A., Coseo M. C., Cancro M. P., et al. Detection of enzyme polymorphism by using monoclonal antibodies. Proc Natl Acad Sci USA 1981; 78: 1124–8
   PubMedGoogle Scholar
• Wahren B., Hinkula J., Stigbrand T., et al. Phenotypes of placental-type alkaline phosphatase in seminoma sera as defined by monoclonal antibodies. Int J Cancer 1986; 37: 595–600
   PubMedGoogle Scholar
• Hendrix P. G., Hoylaerts M. F., Nouwen E. J., et al. Enzyme immunoassay of human placental and germ-cell alkaline phosphatase in serum. Clin Chem 1990; 36/10: 1793–99
   Google Scholar
• Watanabe S., Watanabe T., Li W. B., et al. Expression of the germ cell alkaline phosphatase gene in human choriocarcinoma cells. J Biol Chem 1989; 264: 12611–9
   PubMed Web of Science ®Google Scholar
• Lowe M. E., Strauss A. W. Expression of a Nagao-type, phosphatidylinositol-glycan-anchored alkaline phosphatase in human choriocarcinomas. Cancer Res 1990; 50: 3956–62
   PubMedGoogle Scholar
• Gum J. R., Hicks J. W., Sack T. L., et al. Molecular cloning of complementary DNAs encoding alkaline phosphatase in human colon cancer cells. Cancer Res 1990; 50: 1085–91
   PubMedGoogle Scholar
• Ray K., Weiss M. J., Dracopoli N. C., et al. Probe 8B/E5' detects a second RFLP at the human liver/bone/kidney alkaline phosphatase (ALPL) locus. Nucleic Acids Res 1988; 16: 2361
   PubMedGoogle Scholar
• Holmgren PÅ, Stigbrand T. Purification and partial characterization of two genetic variants of placental alkaline phosphatase. Biochem Genet 1976; 14: 777–89
   PubMedGoogle Scholar
• Holmgren PÅ, Stigbrand T, Beckman G. Purification and partial characterization of the I variant of placental alkaline phosphatase. Biochem Genet 1977; 15: 521–30
   PubMedGoogle Scholar
• Robson E. B., Harris H. Further studies on the genetics of placental alkaline phosphatase. Ann Hum Genet 1967; 30: 219–32
   PubMedGoogle Scholar
• Beckman G., Beckman L. The placental alkaline phosphatase polymorphism; variations in Hawaiian subpopulations. Hum Hered 1969; 19: 524–9
   PubMedGoogle Scholar
• Hoylaerts M. F., Manes T, Millan J. L. Allelic amino acid substitutions affect the conformation and immunoreactivity of germ cell alkaline phosphatase phenotypes. Clin Chem 1992; 38: 2493–500
   PubMedGoogle Scholar
• Martin D., Spurr NK, Trowsdale J. RFLP of the human placental alkaline phosphatase gene (PLAP). Nucleic Acids Res 1987; 15: 9104
   PubMedGoogle Scholar
• Tsavaler L., Penhallow R. C., Kam W., et al. Pst I restriction fragment length polymorphism of the human placental alkaline phosphatase gene in normal placentae and tumors. Proc Natl Acad Sci USA 1987; 84: 4529–32
   PubMedGoogle Scholar
• Tsavaler L., Penhallow RC, Sussman H. H. Pst I restriction fragment length polymorphism of human placental alkaline phosphatase gene: mendelian segregation and localization of the mutation site in the gene. Proc Natl Acad Sci USA 1988; 85: 7680–4
   PubMedGoogle Scholar
• Beckman G., Beckman L., Lundgren E., et al. Correlation between Rsal restriction fragment length polymorphism and electrophoretic types of human placental alkaline phosphatase. Hum Hered 1989; 39: 41–5
   PubMedGoogle Scholar
• Beckman G., Beckman L., Kivela A., et al. A new Pstl restriction fragment length polymorphism (RFLP) of placental alkaline phosphatase. RFLP haplotypes and correlation with electrophoretic types. Hum Hered 1991; 41: 122–8
   PubMedGoogle Scholar
• Beckman G., Beckman L, Magnusson S. S. Placental alkaline phosphatase phenotypes and prenatal selection. Evidence from studies of spontaneous and induced abortions. Hum Hered 1972; 22: 473–80
   PubMedGoogle Scholar
• Beckman G., Beckman L. The placental alkaline phosphatase variant D and natural selections. Relationship to complications of pregnancy and to “the Regan isoenzyme”. Hereditas 1975; 81: 85–8
   PubMed Web of Science ®Google Scholar
• Stigbrand T., Engvall E. Placental proteins as tumor markers. Tumor markers. Clifton, S. Sell, B. Wahren. Human Press, New Jersey 1982
   Google Scholar
• Hugon J., Borgers M. Ultrastructural localization of alkaline phosphatase activity in the absorbing cells of the duodenum of the mouse. J Histochem Cytochem 1966; 14: 629–35
   PubMedGoogle Scholar
• Fishman L., Miyayama H., Driscoll S. G., et al. Developmental phase-specific alkaline phosphatase isoenzymes of human placenta and their occurrence in human cancer. Cancer Res 1976; 36: 2268–73
   PubMed Web of Science ®Google Scholar
• Heath J. K. Development of mammals, M. H. Johnson. North-Holland, New York 1978
   Google Scholar
• Hustin J., Collette J, Franchimont P. Immunohistochemical demonstration of placental alkaline phosphatase in various states of testicular development and in germ cell tumors. IntJ Androl 1987; 10: 29–35
   PubMedGoogle Scholar
• Goldstein D. J., Rogers C, Harris H. A search for trace expression of placental-like alkaline phosphatase in non-malignant human tissues: demonstration of its occurrence in lung, cervix, testis and thymus. Clin ChimActa 1982; 125: 63–75
   PubMed Web of Science ®Google Scholar
• Ali S. Y., Sajdera SW, Anderson H. C. Isolation and characterization of calcifying matrix vesicles from epiphyseal cartilage. Proc Natl Acad Sci USA 1970; 67: 1531–20
   Google Scholar
• Whyte M. Hypophosphatasia. The metabolic basis of inherited disease.ed. 6th, Slyvalle Beaudet. McGraw-Hill, Scriver 1989; Vol. 2.: 2843–56
   Google Scholar
• Weiss M. J., Cole D. E., Ray K., et al. A missence mutation in the human liver/bone/kidney alkaline phosphatase gene causing a lethal form of hypophosphatasia. Proc Natl Acad Sci USA 1988; 85: 7666–9
   PubMed Web of Science ®Google Scholar
• Henthorn P. S., Raducha M., Fedde K. N., et al. Different missence mutations at the tissue-nonspecific alkaline phosphatase gene locus in autosomal recessively inherited forms of mild and severe hypophosphatasia. Proc Natl Acad Sci USA 1992; 89: 9924–8
   PubMedGoogle Scholar
• Henthom P. S., Whyte M. P. Missense mutations of the tissue-nonspecific alkaline phosphatase gene in hypophosphatasia. Clin Chem 1992; 38: 2501–5
   PubMedGoogle Scholar
• De Broe M. E., Roels F., Nouwen E. J., et al. Liver plasma membrane: the source of high molecular weight alkaline phosphatase in human serum. Hepatology 1983; 3: 614–7
   PubMedGoogle Scholar
• Banwell S. G., Godfrey P. P., Lowe P. J., et al. Biliary protein output by isolated perfused rat livers. Effects of bile salts. Biochem J 1983; 210: 549–57
   PubMedGoogle Scholar
• Hamilton R. L., Havel R. J., Kane J. L., et al. Cholestasis: lamellar structure of the abnormal human serum lipoprotein. Science 1071; 172: 415–78
   Google Scholar
• Brocklehurst D., Wilde CE, Doar JWH. The incidence and likely origins of serum particulate alkaline phosphatase and lipoprotein-X in liver disease. Clin Chim Acta 1978; 88: 509–15
   PubMedGoogle Scholar
• Alpers D. H., Eliakim R, deSchryver-Kecskemeti K. Secretion of hepatic and intestinal alkaline phosphatases: similarities and differences. Clin Chim Acta 1989; 186: 211–24
   Google Scholar
• Berteloot A., Chabot J-G, Hugon J. S. Organ culture of the adult mouse intestine. Vesiculation of the brush border membrane during the culture. Biol Cell 1981; 42: 109–14
   Google Scholar
• De Broe M. E., Wieme R. J., Logghe G. N., et al. Spontaneous shedding of plasma membrane fragments by human cells in vivo and in vitro. Clin Chim Acta 1977; 81: 237–45
   PubMed Web of Science ®Google Scholar
• Eliakim R., Deschryver-Kecskemeti K., Stenson W. F., et al. Isolation and characterization of a small intestinal surfactant-like particle containing alkaline phosphatase and other digestive enzymes. J Biol Chem 1990; 264: 20614–9
   Google Scholar
• Keiding N. R. Intestinal alkaline phosphatase in human lymph and serum. Scand J Clin Lab Invest 1966; 18: 134–40
   PubMed Web of Science ®Google Scholar
• Langman MJS, Lenthold E., Robson E. B., et al. Influence of diet on the intestinal component of serum alkaline phosphatase in people of different ABO blood groups and secretory status. Nature 1966; 212: 41–3
   PubMed Web of Science ®Google Scholar
• Fishman W. H., Bardawil W. A., Habib HBV, et al. Placental isoenzyme of alkaline phosphatase in sera of normal pregnancy. Am J Clin Pathol 1972; 57: 65–74
   PubMedGoogle Scholar
• Sussman H. H., Bowman M, Levis J. L. Placental alkaline phosphatase in maternal serum during normal and abnormal pregnancy. Nature 1968; 218: 359–60
   PubMedGoogle Scholar
• Okamoto T., Seo H., Mano H., et al. Expression of human placenta alkaline phosphatase in placenta during pregnancy. Placenta 1990; 11: 319–27
   PubMedGoogle Scholar
• Holmgren P. A., Stigbrand T., Damber M. G., et al. Double antibody solid phase radioimmunoassay for placental alkaline phosphatase. Clin Chim Acta 1978; 83: 205–10
   PubMedGoogle Scholar
• Holmgren P. A., Stigbrand T., Damber M. G., et al. Serum levels of placental alkaline phosphatase in high-risk pregnancies. Obstet Gynecol 1979; 54: 631–4
   PubMedGoogle Scholar
• Fishman W. H., Manning J. P., Takeda M., et al. Quantitation of potency of antisera to placental alkaline phosphatase by an automated immunoenzyme technique. Anal Biochem 1973; 51: 368–82
   PubMedGoogle Scholar
• Yamaguchi R., Shimozato N. Diagnosis of placental function by prediction curves for heat-stable alkaline phosphatase (HSAP). Tohoku J Exp Med 1978; 124: 73–82
   PubMedGoogle Scholar
• Best R. G., Meyer RE, Shipley C. F. Maternal serum placental alkaline phosphatase as a marker for low birth weight: results of a pilot study. South Med J 1991; 84: 74
   Google Scholar
• Brock D. J., Barron L. Measurement of placental alkaline phosphatase in maternal plasma as an indicator of subsequent low birthweight outcome. Br J Obstet Gynaecol 1988; 95: 79–83
   PubMedGoogle Scholar
• Grozdea J., Brisson-Lougarre A., Vergnes H., et al. IgG/placental alkaline phosphatase complexes in Rh-incompatible pregnancy with fetal hydrops. Vox Sang 1988; 55: 42–3
   PubMedGoogle Scholar
• Zackson S. L., Steinberg M. S. A molecular marker for cell guidance information in the axolotl embryo. Dev Biol 1988; 127: 435–42
   PubMedGoogle Scholar
• French-Constant C., Hollingsworth A., Heasman J., et al. Response to fibronectin of mouse primordial germ cells before, during and after migration. Development 1991; 113: 1365–73
   PubMedGoogle Scholar
• Fishman W. H. Oncotrophoblast gene expression: placental alkaline phosphatase. Adv Cancer Res 1987; 48: 1–35
   PubMed Web of Science ®Google Scholar
• Jacobs E. L., Haskell C. M. Clinical use of tumor markers in oncology. Curr Probl Cancer 1991; 15: 299–360
   PubMedGoogle Scholar
• Fishman W. H., Inglis N. R., Green S, et al. Immunology and biochemistry of Regan isoenzyme of alkaline phosphatase in human cancer. Nature 1968; 2: 9–697
   Google Scholar
• Fishman W. H., Inglis N. R., Stolbach L. L., et al. Serum alkaline phosphatase isoenzyme of human neoplastic cell origin. Cancer Res 1968; 28: 150–4
   PubMed Web of Science ®Google Scholar
• Greene P. J., Sussman H. H. Structural comparison of ectopic and normal placental alkaline phosphatase. Proc Natl Acad Sci USA 1973; 70: 2936–40
   PubMed Web of Science ®Google Scholar
• Nathanson L., Fishman W. H. New observations on the Regan isoenzyme of alkaline phosphatase in cancer patients. Cancer 1971; 27: 1388–97
   PubMed Web of Science ®Google Scholar
• Jacoby B., Bagshawe K. D. Placental-type alkaline phosphatase from human tumor tissue. Clin Chim Acta 1971; 35: 473–81
   PubMed Web of Science ®Google Scholar
• Loose J. H., Damjanov I, Harris H. Identity of the neoplastic alkaline phosphatase as revealed with monoclonal antibodies to the placental form of the enzyme. Am J Clin Pathol 1984; 82: 173–7
   PubMedGoogle Scholar
• Jeppsson A., Wahren B., Brehmer-Andersson E., et al. Eutopic expression of placental-like alkaline phosphatase in testicular tumors. Int J Cancer 1984; 0: 61–757
   Google Scholar
• Paiva J., Damjanov I., Lange P. H., et al. Immunohistochemical localization of placental-like alkaline phosphatase in testis and germ cell tumors using monoclonal antibodies. Am J Clin Pathol 1983; 111: 156–65
   Google Scholar
• Uchida T., Shimoda T., Miyata H., et al. Immunoperoxidase study of alkaline phosphatase in testicular tumors. Cancer Res 1981; 48: 1455–62
   Google Scholar
• Koide O., Iwai S., Baba K., et al. Identification of testicular atypical germ cells by an immunohistochemical technique for PLAP. Cancer 1987; 60: 1325–30
   PubMed Web of Science ®Google Scholar
• Vergote I., Onsrud M, Nustad K. Placental alkaline phosphatase as a tumor marker in ovarian cancer. Obstet Gynecol 1987; 69: 228–32
   PubMed Web of Science ®Google Scholar
• Critchley M., Brownless S., Patten M., et al. Radionuclide imaging of epithelial ovarian tumors with123I-labeled monoclonal antibody (H317) specific for placental-type alkaline phosphatase. Clin Radiol 1986; 31: 107–12
   Google Scholar
• Friedman N. B., van Velde D, Velde R. L. Germ cell tumors in man, pleiotropic mice and continuity of germ plasma and somatoplasm. Hum Pathol 1981; 12: 772–6
   PubMedGoogle Scholar
• De Broe M. E., Pollet D. E. Multicenter evaluation of human placental alkaline phosphatase as a possible tumor-associated antigen in serum. Clin Chem 1988; 34: 1995–9
   PubMed Web of Science ®Google Scholar
• Stendahl U., Lindgren A., Tholander B., et al. Expression of placental alkaline phosphatase in epithelial ovarian tumours. Tumour Biol 1989; 10: 126–32
   PubMedGoogle Scholar
• Mano H., Furuhashi Y., Morikawa Y., et al. Radioimmunoassay of placental alkaline phosphatase in ovarian cancer sera and tissues. Obstet Gynecol 1986; 68: 759–64
   PubMedGoogle Scholar
• Stigbrand T., Ridlund K., Tholander B., et al. Placental alkaline phosphatase (PLAP) PLAP-like alkaline phosphatase as tumour marker in relation to CA 125 and TPA for ovarian epithelial tumours. J Gynecol Oncol 1990; 11: 351–60
   Google Scholar
• Skakkebak N. E., Berthelsen J. G., Giwercman A., et al. Carcinoma in situ of the testis: possible origin from gonocytes and precursor of all types of germ cell tumors except spermatocytic seminoma. Int J Androl 1987; 10: 19–28
   PubMedGoogle Scholar
• Lange P. H., Millán J. L., Stigbrand T., et al. Placental alkaline phosphatase as a tumor marker for seminoma. Cancer Res 1982; 42: 3244–7
   PubMed Web of Science ®Google Scholar
• Jeppsson A., Wahren B., Stigbrand T., et al. A clinical evaluation of serum placental alkaline phosphatase in seminoma patients. Br J Urol 1983; 8–73
   Google Scholar
• von der Maase H., Giwercman A., Müller J., et al. Management of carcinoma-in-situ of the testis. Int J Androl 1987; 20–209
   Google Scholar
• Wahren B., Holmgren PA, Stigbrand T. Placental alkaline phosphatase, alphafetoprotein and carcinoembryonic antigen in testicular tumors. Int J Cancer 1979; 24: 749–53
   PubMed Web of Science ®Google Scholar
• Lange P. H., Millan J. L., Stigbrand T., et al. Placental alkaline phosphatase as a tumor marker for seminoma. Cancer Res 1982; 42: 3244–7
   PubMed Web of Science ®Google Scholar
• Goldstein D. J., Blasco L, Harris H. Placental alkaline phosphatase in nonmalignant human cervix. Proc Natl Acad Sci USA 1980; 77: 4226–9
   PubMed Web of Science ®Google Scholar
• Nozawa S., Ohta H., Izumi S., et al. Heat-stable alkaline phosphatase in the normal female genital organ – with special reference to the histochemical heat-stability test and ^phenylalanine inhibition test. Acta Histochem Cytochem 1980; 13: 521–30
   Web of Science ®Google Scholar
• Chang C. H., Angellis D, Fishman W. H. Occurrence in normal human testis of a heat-stable alkaline phosphatase similar to a rare variant of placental isoenzyme. Scand J Immunol 1978; 8((Suppl 8))543–6
   PubMedGoogle Scholar
• Chang C. H., Angellis D, Fishman W. H. Presence of the rare D-variant heat-stable placental-type alkaline phosphatase in normal human testis. Cancer Res 1980; 10–1506
   Google Scholar
• Benham J. F., Povey MS, Harris H. Placental-like alkaline phosphatase in malignant and benign ovarian tumors. Clin Chim Acta 1978; 86: 201–15
   PubMed Web of Science ®Google Scholar
• Harding U., Toftager-Larsen K., Dreisler A., et al. CA 125, placental alkaline phosphatase, and tissue polypeptide antigen in the monitoring of ovarian carcinoma. A comparative study of three different tumor markers. Gynecol Obstet Invest 1990; 30: 178–83
   PubMedGoogle Scholar
• Nouwen E. J., Buyssens N, De Broe M. E. Heat-stable alkaline phosphatase as a marker for human and monkey type-I pneumocytes. Cell Tissue Res. 1990; 260: 321–35
   PubMed Web of Science ®Google Scholar
• Millán J. L., Nustad K, Norgaard-Pedersen B. Highly sensitive solid-phase immunoenzymometric assay for placental and placental-like alkaline phosphatases with a monoclonal antibody and monodisperse polymer particles. Clin Chem 1985; 31: 54–9
   PubMedGoogle Scholar
• Tonik S. E., Ortmeyer A. E., Shindelman J. E., et al. Elevations of serum placental alkaline phosphatase levels in cigarette smokers. Int J Cancer 1983; 31: 51–3
   PubMed Web of Science ®Google Scholar
• Higashino K., Hashinotsume M., Kang K-Y, et al. Studies on a variant alkaline phosphatase in sera of patients with hepatocellular carcinoma. Clin Chim Acta 1972; 40: 67–81
   PubMed Web of Science ®Google Scholar
• Higashino K., Kodo S., Yamamura Y. Further investigation of a variant of the placental alkaline phosphatase in human hepatic carcinoma. Cancer Res 1974; 34: 3347–51
   PubMedGoogle Scholar
• Higashino K., Otani R., Kudo S., et al. Hepatocellular carcinoma and a variant alkaline phosphatase. Ann Internal Med 1975; 83: 74–8
   PubMedGoogle Scholar
• Higashino K., Otani R., Kudo S., et al. A fetal intestinal-type alkaline phosphatase in hepatocellular carcinoma tissue. Clin Chem 1977; 23: 1615–23
   PubMedGoogle Scholar
• Hada T., Higashino K., Okochi T., et al. Kasahara-variant alkaline phosphatase in a renal cell carcinoma. Clin Chim Acta 1978; 89: 311–6
   PubMed Web of Science ®Google Scholar
• Hada T., Higashino K., Okochi T., et al. Another Kasahara-variant alkaline phosphatase in renal cell carcinomas. Gann 1979; 70: 503–8
   PubMedGoogle Scholar
• Higashino K., Kudo S., Yamamura Y., et al. Possible identity between the hepatoma alkaline phosphatase and an isozyme of human amniotic membrane (FL cells). Clin Chim Acta 1975; 60: 267–72
   PubMedGoogle Scholar
• Imanishi H., Hada T., Muratani K., et al. An alkaline phosphatase reacting with both monoclonal antibodies to intestinal and placental isoenzymes. Clin Chim Acta 1989; 186: 309–14
   Google Scholar
• Higashino K., Muratani K., Hada T., et al. Purification and some properties of the fast migrating alkaline phosphatase in FL-amnion cells (the Kasahara isozyme) and its cDNA cloning. Clin Chim Acta 1989; 186: 151–65
   Google Scholar
• Leung K. S., Fung K. P., Sher A. H., et al. Plasma bone-specific alkaline phosphatase as an indicator of osteoblastic activity. J Bone Jt Surg Br 1993; 75: 288–92
   PubMedGoogle Scholar
• Bacci G., Picci P., Ferrari S., et al. Prognostic significance of serum alkaline phosphatase measurements in patients with osteosarcoma treated with adjuvant or neoadjuvant chemotherapy. Cancer 1993; 71: 1224–30
   PubMed Web of Science ®Google Scholar
• Stieber P., Nagel D., Ritzke C., et al. Significance of bone alkaline phosphatase, CA 15–3 and CEA in the detection of bone metastasis during the follow-up of patients suffering from breast carcinoma. Eur J Clin Chem Clin Biochem 1993; 30: 809–14
   Google Scholar
• Moro L., Gazzarrini C., Crivellari D., et al. Biochemical markers for detecting bone metastasis in patients with breast cancer. Clin Chem 1993; 39: 131–4
   PubMedGoogle Scholar
• Curatolo C., Ludovico G. M., Correale M., et al. Advanced prostate cancer follow-up with prostate-specific antigen, prostatic acid phosphatase, osteocalcin and bone isozyme of alkaline phosphatase. Eur Urol. 1992; 21: 105–7
   PubMedGoogle Scholar
• Walach N., Gur Y. Leukocyte alkaline phosphatase and carcinoembryonic antigen in lung cancer patients. Oncology 1993; SO: 84–279
   Google Scholar
• Tholander B., Taube A., Lindgren A., et al. Pretreatment serum levels of CA-125, carcinoembryonic antigen, tissue polypeptide antigen, and placental alkaline phosphatase, in patients with ovarian carcinoma, borderline tumors, or benign adnexal masses: relevance for differential diagnosis. Gynecol Oncol 1990; 39: 16–25
   PubMed Web of Science ®Google Scholar
• Nozawa S., Udagawa Y., Ohkura H., et al. Serum placental alkaline phosphatase (PLAP) in gynecologic malignancies – with special reference to the combination of PLAP and CA54. J 61 assay.Clin ChimActa 1990; 186: 275–84
   PubMedGoogle Scholar
• Stendahl U., Lindgren A., Tholander B., et al. Expression of placental alkaline phosphatase in epithelial ovarian tumours. Tumour Biol 1989; 10: 126–32
   PubMedGoogle Scholar
• Mano H., Furuhashi Y., Morikawa Y., et al. Radioimmunoassay of placental alkaline phosphatase in ovarian cancer sera and tissues. Obstet Gynecol 1986; 68: 759–64
   PubMedGoogle Scholar
• Vergote I., Onsrud M, Nustad K. Placental alkaline phosphatase as a tumor marker in ovarian cancer. Obstet Gynecol 1987; 69: 228–32
   PubMed Web of Science ®Google Scholar
• Stigbrand T., Riklund K., Tholander B., et al. Placental alkaline phosphatase (PLAP) PLAP-like alkaline phosphatase as tumour marker in relation to CA 125 and TPA for ovarian epithelial tumours. J Gynaecol Oncol 1990; 11: 351–60
   Google Scholar
• van De Voorde A., Serreyn R., de Boever J., et al. The occurrence of human placental alkaline phosphatase (PLAP) in extracts of normal, benign and malignant tissues of the female genital tract. Tumour Biol. 1985; 6: 545–53
   PubMedGoogle Scholar
• Hamilton-Dutoit S. J., Lou H, Pallesen G. The expression of placental alkaline phosphatase (PLAP) and PLAP-like enzymes in normal and neoplastic human tissues. An immunohistological survey using monoclonal antibodies. APMIS 1990; 98: 797–811
   PubMed Web of Science ®Google Scholar
• Hirano K., Domar U. M., Yamamoto H., et al. Levels of alkaline phosphatase isozymes in human seminoma tissue. Cancer Res 1987; 47: 2543–6
   PubMedGoogle Scholar
• Latham K. M., Stanbridge E. J. Identification of the HeLa tumor-associated antigen, p75/150, as intestinal alkaline phosphatase and evidence for its transcriptional regulation. Proc Natl Acad Sci USA 1990; 87: 1263–7
   PubMedGoogle Scholar
• Latham K. M., Stanbridge E. J. Examination of the oncogenic potential of a tumor-associated antigen, intestinal alkaline phosphatase, in HeLa X fibroblast cell hybrids. Cancer Res 1992; 52: 616–22
   PubMedGoogle Scholar
• Cox R. P., MacLeod C. M. Hormonal induction of alkaline phosphatase in tissue culture. Nature 1961; 190: 85–7
   PubMedGoogle Scholar
• Singer R. M., Fishman W. H. Specific isozyme profiles of alkaline phosphatase in prednisolone-treated human cell populations. development biology, C. L. Markert, HI. Isozymes. Academic Press, New York 1975; 753–774
   Google Scholar
• Hamilton T. A., Sussman H. H. The effect of bromodeoxyuridine and dibutyryl cyclic AMP on the induction of placental alkaline phosphatase in human choriocarcinoma cells. Biochem J 1981; 198: 29–35
   PubMedGoogle Scholar
• Hanford W. C., Kottel RH, Fishman W. H. Alkaline phosphatase protein increases in response to prednisolone in HeLa cells. BiochemJ 1981; 200: 461
   PubMedGoogle Scholar
• Ito F., Chou J. Y. Biosynthesis and processing of placental alkaline phosphatase. Biochem BiophysRes Commun 1983; 111: 611–8
   PubMedGoogle Scholar
• Kottel R. H., Fishman W. H. Modulation of HeLa cell alkaline phosphatase isoenzyme expression by prednisolone. Carcinoembryonic proteins: recent progress. Blackwell Scientific Publications. 1978; 571–574
   Google Scholar
• Singer R. M., Fishman W. H. Characterization of two HeLa sublines: TCRC-1 produces Regan isoenzyme and TCRC-2, non-Regan isoenzyme. J Cell Biol 1974; 60: 777–80
   PubMedGoogle Scholar
• Tokumitsu S. I., Tokumitsu K., Kohnoe K., et al. Characterization of liver-type alkaline phosphatase from human gastric carcinoma cells (KMK-2) in vitro. Cancer Res 1979; 39: 4732–8
   PubMed Web of Science ®Google Scholar
• Herz F., Halwer M. Preferential alkaline phosphatase isoenzyme induction by sodium butyrate. Biochim Biophys Acta 1983; 762: 289–93
   PubMedGoogle Scholar
• Herz F., Schermer A., Halver M., et al. Alkaline phosphatase in HT-29, a human colon cancer cell line: influence of sodium butyrate and hyperosmolarity. Arch Biochem Biophys 1981; 210: 581–91
   PubMedGoogle Scholar
• Takahara N., Herz F, Hirano A. Alkaline phosphatase activity in cultured meningioma cells. Acta Neuropathol. 1982; 57: 45–50
   PubMedGoogle Scholar
• Honda T., Kurabori T., Ishigami S., et al. An alkaline phosphatase of FL cells. Igaku-no-Azumi 1973; 86: 313–4
   Google Scholar
• Fishman W. H., Singer R. M. Regulatory controls of oncotrophoblast proteins and developmental alkaline phosphatases in cancer cells. Cancer Res 1976; 36: 4256–61
   PubMed Web of Science ®Google Scholar
• Higashino K., Kudo S., Ohtani R., et al. A hepatoma-associated alkaline phosphatase, the Kasahara isoenzyme, compared with one of the isozymes of FL-amnion cells. Ann NY Acad Sci. 1975; 259: 337–46
   PubMed Web of Science ®Google Scholar
• Higashino K., Hashinotsume M., Kang Y., et al. Studies on a variant alkaline phosphatase in sera of patients with hepatocellular carcinoma. Clin Chim Acta 1972; 24: 67–81
   Google Scholar
• Griffin M. J., Price G. H., Bazzell K. L., et al. A study of adenosine 3':5'-cyclic monophosphate, sodium butyrate and Cortisol as inducers of HeLa alkaline phosphatase. Arch Biochim Biophys 1974; 164: 619–23
   PubMedGoogle Scholar
• Deutsch S. I., Ghosh NK, Cox R. P. Increased alkaline phosphatase activity in HeLa cells mediated by aliphatic monocarboxylates and inhibitors of DNA synthesis. Biochim Biophys Acta 1977; 499: 382–91
   PubMedGoogle Scholar
• Chou J. Y. Regulation of the induction of alkaline phosphatase in choriocarcinoma cells by sodium butyrate. In Vitro 1979; 15: 789–95
   PubMedGoogle Scholar
• Littlefield B. A., Cidlowski NB, Cidlowski J. A. Modulation of glucocorticoid effects and steroid receptor binding in butyrate-treated HeLa S3 cells. Arch Biochem Biophys 1980; 201: 174–84
   PubMedGoogle Scholar
• Cox G. S. Synthesis of the glycoprotein hormone a subunit and placental alkaline phosphatase by HeLa cells: effect of tunicamycin, 2-deoxyglucose and sodium butyrate. Biochemistry 1981; 20: 4893–900
   PubMed Web of Science ®Google Scholar
• Tokumitsu S. I., Tokumitsu K, Fishman W. H. Intracellular alkaline phosphatase activity in cultured human cancer cells. Histochemistry 1981; 73: 1–13
   PubMedGoogle Scholar
• Xue S., Rao P. N. Sodium butyrate blocks HeLa cells preferentially in early Gl phase of the cell cycle. J Cell Sci 1981; 51: 163–71
   PubMed Web of Science ®Google Scholar
• Riggs M. G., Whitaker R. G., Neumann J. F., et al. n-Butyrate causes histone modification in HeLa and Friend erythroleukaemia cells. Nature 1977; 268: 462–4
   PubMed Web of Science ®Google Scholar
• Candido EPM, Reeves R, Davie J. R. Sodium butyrate inhibits histone deacetylation in cultured cells. Cell 1978; 14: 105–13
   PubMed Web of Science ®Google Scholar
• Prasad K. N. Butyric acid: a small fatty acid with diverse biological functions. Life Sci 1980; 27: 1351–8
   PubMed Web of Science ®Google Scholar
• Fallon R. J., Cox R. P. Relation of cell cycle position and chromatin decondensation to ectopic hormone synthesis in HeLa cells. Somatic Cell Genet. 1981; 7: 193–204
   PubMedGoogle Scholar
• Herz F. Human alkaline phosphatases, T. Stigbrand, W. H. Fishman. Liss, New York 1984; 139–166
   Google Scholar
• Durbin H, Milligan E. M., Marther S. J., et al. Monoclonal antibodies to placental alkaline phosphatase: preclinical evaluation in a human xenograph tumour model of F(ab's)2 and Fab fragments. Int J Cancer Suppl. 1988; 2: 59–66
   PubMedGoogle Scholar
• Hendrix P. G., Dauwe S. E., Van de Voorde A., et al. Radiolocalisation and imaging of stably HPLAP-transfected M04 tumours with monoclonal antibodies and fragments. Br J Cancer 1991; 64: 8–1060
   Google Scholar
• Jeppsson A., Wahren B., Millan J. L., et al. Tumor and cellular localization by use of monoclonal and polyclonal antibodies to placental alkaline phosphatase. Br J Cancer 1984; 49: 123–8
   PubMed Web of Science ®Google Scholar
• Stigbrand T., Hietala S. O., Johansson B., et al. Tumour radioimmunolocalization in nude mice by use of antiplacental alkaline phosphatase monoclonal antibodies. Tumour Biol 1989; 10: 243–51
   PubMedGoogle Scholar
• Epenetos A. A., Carr D., Johnson P. M., et al. Antibody-guided radiolocalisation of tumours in patients with testicular or ovarian cancer using two radioiodinated monoclonal antibodies to placental alkaline phosphatase. Br J Radiol 1986; 59: 117–25
   PubMed Web of Science ®Google Scholar
• Tzukazaki K., Hayman EG, Ruoslahti E. Effects of ricin A chain conjugates of monoclonal antibodies to human alpha-fetoprotein and placental alkaline phosphatase on antigen-producing tumor cells in culture. Cancer Res 1985; 45: 8–1834
   Google Scholar
• Riklund K. E., Makiya R. A., Sundstrom B. E., et al. Experimental radioimmunotherapy of HeLa tumours in nude mice with 1311-labeled monoclonal antibodies. Anticancer Res 1990; 10: 379–84
   PubMedGoogle Scholar
• Riklund K. E., Makiya R. A., Sundstrom B. E., et al. Inhibition of growth of HeLa cell tumours in nude mice by125I-labeled anticytokeratin and anti PLAP monoclonal antibodies. Anticancer Res. 1990; 11: 555–60
   Google Scholar
• Kalofonos H. P., Kosmas C., Pawlikowska T. R., et al. Immunolocalisation of testicular tumours using radiolabelled monoclonal antibody to placental alkaline phosphatase. J Nucl Med Allied Sci 1990; 34: 294–8
   PubMedGoogle Scholar
• Fjeld J. G., Bruland O. S., Benestad H. B., et al. Radioimmunotargeting of human rumour cells in immunocompetent animals. Br J Cancer 1990; 62: 573–8
   PubMed Web of Science ®Google Scholar
• Snook D. E., Rowlinson-Busza G., Sharma H. L., et al. Preparation and in vivo study of114I-labelled monoclonal antibody H17E2 in a human tumour xenograft model. A prelude to positron emission tomography (PET). Br J Cancer Suppl. 1990; 10: 89–91
   PubMedGoogle Scholar
• Kalofonos H. P., Pawlikowska T. R., Hemingway A., et al. Antibody guided diagnosis and therapy of brain gliomas using radiolabeled monoclonal antibodies against epidermal growth factor receptor and placental alkaline phosphatase. J Nucl Med 1989; 30: 1636–45
   PubMed Web of Science ®Google Scholar
• Durbin H., Milligan E. M., Mather S. J., et al. Monoclonal antibodies to placental alkaline phosphatase: preclinical evaluation in a human xenograft tumour model of F(ab02 and Fab fragments. Int J Cancer Suppl. 1988; 2: 59–66
   PubMedGoogle Scholar
• Athanassiou A., Pectasides D., Pateniotis K., et al. 13I-labelled monoclonal antibody H17E2 in the detection of subcutaneous metastasis from gestational choriocarcinoma. Anticancer Res 1990; 10: 913–5
   PubMedGoogle Scholar
• Narisawa S., Smans K., Avis J., et al. Transgenic mice expressing the tumor marker germ cell alkaline phosphatase: an in vivo tumor model for human cancer antigens. Proc Natl Acad Sci USA 1993; 90: 5081–5
   PubMedGoogle Scholar