Specific Immunoassays for Placental Alkaline Phosphatase As a Tumor Marker

Stinghen, Sérvio T.; Moura, Juliana F.; Zancanella, Patrícia; Rodrigues, Giovanna A.; Pianovski, Mara A.; Lalli, Enzo; Arnold, Dodie L.; Minozzo, João C.; Callefe, Luis G.; Ribeiro, Raul C.; Figueiredo, Bonald C.

doi:https://doi.org/10.1155/JBB/2006/56087

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Volume 2006 | Article ID 056087 | https://doi.org/10.1155/JBB/2006/56087

Specific Immunoassays for Placental Alkaline Phosphatase As a Tumor Marker

Sérvio T. Stinghen,¹Juliana F. Moura,¹Patrícia Zancanella,¹Giovanna A. Rodrigues,¹Mara A. Pianovski,²Enzo Lalli,³Dodie L. Arnold,⁴João C. Minozzo,⁵Luis G. Callefe,¹Raul C. Ribeiro,⁶and Bonald C. Figueiredo^1,7

Received23 Dec 2005

Revised01 Jun 2006

Accepted06 Jun 2006

Published07 Aug 2006

Abstract

Human placental (hPLAP) and germ cell (PLAP-like) alkaline phosphatases are polymorphic and heat-stable enzymes. This study was designed to develop specific immunoassays for quantifying hPLAP and PLAP-like enzyme activity (EA) in sera of cancer patients, pregnant women, or smokers. Polyclonal sheep anti-hPLAP antibodies were purified by affinity chromatography with whole hPLAP protein (ICA-PLAP assay) or a synthetic peptide (aa 57–71) of hPLAP (ICA-PEP assay); the working range was 0.1–11 U/L and cutoff value was 0.2 U/L EA for nonsmokers. The intra- and interassay coefficients of variation were 3.7%–6.5% (ICA-PLAP assay) and 9.0%–9.9% (ICA-PEP assay). An insignificant cross-reactivity was noted for high levels of unheated intestinal alkaline phosphatase in ICA-PEP assay. A positive correlation between the regression of tumor size and EA was noted in a child with embryonal carcinoma. It can be concluded that ICA-PEP assay is more specific than ICA-PLAP, which is still useful to detect other PLAP/PLAP-like phenotypes.

References

M T Lehto and F J Sharom, “Proximity of the protein moiety of a GPI-anchored protein to the membrane surface: a FRET study,” Biochemistry, vol. 41, no. 26, pp. 8368–8376, 2002.
View at: Publisher Site | Google Scholar
D W Moss, “Perspectives in alkaline phosphatase research,” Clinical Chemistry, vol. 38, no. 12, pp. 2486–2492, 1992.
View at: Google Scholar
M G Low and A RS Prasad, “A phospholipase D specific for the phosphatidylinositol anchor of cell-surface proteins is abundant in plasma,” Proceedings of the National Academy of Sciences of the United States of America, vol. 85, no. 4, pp. 980–984, 1988.
View at: Google Scholar
S Posen, F C Neale, and J S Clubb, “Heat inactivation in the study of human alkaline phosphatases,” Annals of Internal Medicine, vol. 62, pp. 1234–1243, 1965.
View at: Google Scholar
H Harris, “The human alkaline phosphatases: what we know and what we don't know,” Clinica Chimica Acta, vol. 186, no. 2, pp. 133–150, 1990.
View at: Google Scholar
M H Le Du, T Stigbrand, M J Taussig, A Ménez, and E A Stura, “Crystal structure of alkaline phosphatase from human placenta at 1.8 Å resolution: implication for a substrate specificity,” Journal of Biological Chemistry, vol. 276, no. 12, pp. 9158–9165, 2001.
View at: Publisher Site | Google Scholar
G Beckman and L Beckman, “The placental alkaline phosphatase polymorphism. Variations in Hawaiian subpopulations,” Human Heredity, vol. 19, no. 5, pp. 524–529, 1969.
View at: Google Scholar
M Sato, K Furiya, S Tanaka, Y Sakagishi, and T Komoda, “Allelic polymorphism of human placental alkaline phosphatase in three races: sugar chain heterogeneities,” Clinica Chimica Acta, vol. 178, no. 1, pp. 101–108, 1988.
View at: Google Scholar
J L Millán and W M Fishman, “Biology of human alkaline phosphatases with special reference to cancer,” Critical Reviews in Clinical Laboratory Sciences, vol. 32, no. 1, pp. 1–39, 1995.
View at: Google Scholar
J L Millán, A Eriksson, and T Stigbrand, “A possible new locus of alkaline phosphatase expressed in human testis,” Human Genetics, vol. 62, no. 4, pp. 293–295, 1982.
View at: Google Scholar
D Martin, D F Tucker, P Gorman, D Sheer, N K Spurr, and J Trowsdale, “The human placental alkaline phosphatase gene and related sequences map to chromosome 2 band q37,” Annals of Human Genetics, vol. 51, no. pt 2, pp. 145–152, 1987.
View at: Google Scholar
J L Millán and T Manes, “Seminoma-derived Nagao isozyme is encoded by a germ-cell alkaline phosphatase gene,” Proceedings of the National Academy of Sciences of the United States of America, vol. 85, no. 9, pp. 3024–3028, 1988.
View at: Google Scholar
M H Le Du and J L Millán, “Structural evidence of functional divergence in human alkaline phosphatases,” Journal of Biological Chemistry, vol. 277, no. 51, pp. 49808–49814, 2002.
View at: Publisher Site | Google Scholar
L Fishman, H Miyayama, S G Driscoll, and W H Fishman, “Developmental phase specific alkaline phosphatase isoenzymes of human placenta and their occurrence in human cancer,” Cancer Research, vol. 36, no. 7 pt 1, pp. 2268–2273, 1976.
View at: Google Scholar
R Makiya and T Stigbrand, “Placental alkaline phosphatase as the placental IgG receptor,” Clinical Chemistry, vol. 38, no. 12, pp. 2543–2545, 1992.
View at: Google Scholar
G Beckman, L Beckman, S Holm, C Sikstrom, and C Wennberg, “Placental alkaline phosphatase types and transplacental IgG transport,” Human Heredity, vol. 45, no. 1, pp. 1–5, 1995.
View at: Google Scholar
D J Goldstein, C Rogers, and H Harris, “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,” Clinica Chimica Acta, vol. 125, no. 1, pp. 63–75, 1982.
View at: Publisher Site | Google Scholar
J Hustin, J Collette, and P Franchimont, “Immunohistochemical demonstration of placental alkaline phosphatase in various states of testicular development and in germ cell tumours,” International Journal of Andrology, vol. 10, no. 1, pp. 29–35, 1987.
View at: Google Scholar
H A Muensch, W C Maslow, F Azama, M Bertrand, P Dewhurst, and B Hartman, “Placental-like alkaline phosphatase. Re-evaluation of the tumor marker with exclusion of smokers,” Cancer, vol. 58, no. 8, pp. 1689–1694, 1986.
View at: Google Scholar
K Hirano, H Matsumoto, T Tanaka et al., “Specific assays for human alkaline phosphatase isozymes,” Clinica Chimica Acta, vol. 166, no. 2-3, pp. 265–273, 1987.
View at: Google Scholar
G H Williams, P J McLaughlin, and P M Johnson, “Tissue origin of serum placental-like alkaline phosphatase in cigarette smokers,” Clinica Chimica Acta, vol. 155, no. 3, pp. 329–333, 1986.
View at: Google Scholar
W G Haije, J Van Driel, and M EL Van Der Burg, “Catalytic and immunologic activities of placental-like alkaline phosphatase in clinical studies. The value of PLAP in follow-up of ovarian cancer,” Clinica Chimica Acta, vol. 165, no. 2-3, pp. 165–175, 1987.
View at: Google Scholar
L Weissbach, R Bussar-Maatz, and K Mann, “The value of tumor markers in testicular seminomas. Results of a prospective multicenter study,” European Urology, vol. 32, no. 1, pp. 16–22, 1997.
View at: Google Scholar
N Wada and J Y Chou, “Characterization of upstream activation elements essential for the expression of germ cell alkaline phosphatase in human choriocarcinoma cells,” Journal of Biological Chemistry, vol. 268, no. 19, pp. 14003–14010, 1993.
View at: Google Scholar
A ME Nouri, N Torabi-Pour, and A ANPM Dabare, “A new highly specific monoclonal antibody against placental alkaline phosphatase: a potential marker for the early detection of testis tumour,” BJU International, vol. 86, no. 7, pp. 894–900, 2000.
View at: Publisher Site | Google Scholar
H Roelofs, T Manes, T Janszen, J L Millán, J W Oosterhuis, and L HJ Looijenga, “Heterogeneity in alkaline phosphatase isozyme expression in human testicular germ cell tumours: an enzyme-/immunohistochemical and molecular analysis,” Journal of Pathology, vol. 189, no. 2, pp. 236–244, 1999.
View at: Publisher Site | Google Scholar
P G Hendrix, M F Hoylaerts, E J Nouwen, and M E De Broe, “Enzyme immunoassay of human placental and germ-cell alkaline phosphatase in serum,” Clinical Chemistry, vol. 36, no. 10, pp. 1793–1799, 1990.
View at: Google Scholar
M F Hoylaerts and J L Millán, “Site-directed mutagenesis and epitope-mapped monoclonal antibodies define a catalytically important conformational difference between human placental and germ cell alkaline phosphatase,” European Journal of Biochemistry, vol. 202, no. 2, pp. 605–616, 1991.
View at: Google Scholar
A Malkin, J A Kellen, G M Lickrish, and R S Bush, “Carcinoembryonic antigen (CEA) and other tumor markers in ovarian and cervical cancer,” Cancer, vol. 42, no. 3 suppl, pp. 1452–1456, 1978.
View at: Google Scholar
H Mano, Y Furuhashi, Y Morikawa, S E Hattori, S Goto, and Y Tomoda, “Radioimmunoassay of placental alkaline phosphatase in ovarian cancer sera and tissues,” Obstetrics and Gynecology, vol. 68, no. 6, pp. 759–764, 1986.
View at: Google Scholar
S Nozawa, Y Udagawa, H Ohkura et al., “Serum placental alkaline phosphatase (PLAP) in gynecologic malignancies - with special reference to the combination of PLAP and CA54/61 assay,” Clinica Chimica Acta, vol. 186, no. 2, pp. 275–284, 1990.
View at: Google Scholar
J Fisken, R CF Leonard, G Shaw, A Bowman, and J E Roulston, “Serum placental-like alkaline phosphatase (PLAP): a novel combined enzyme linked immunoassay for monitoring ovarian cancer,” Journal of Clinical Pathology, vol. 42, no. 1, pp. 40–45, 1989.
View at: Google Scholar
I B Vergote, V M Abeler, O P Bormer, T Stigbrand, C Trope, and K Nustad, “CA125 and placental alkaline phosphatase as serum tumor markers in epithelial ovarian carcinoma,” Tumor Biology, vol. 13, no. 3, pp. 168–174, 1992.
View at: Google Scholar
J S Berek and R C Jr Bast, “Ovarian cancer screening: the use of serial complementary tumor markers to improve sensitivity and specificity for early detection,” Cancer, vol. 76, no. 10 suppl, pp. 2092–2096, 1995.
View at: Google Scholar
T Ind, R Iles, J Shepherd, and T Chard, “Serum concentrations of cancer antigen 125, placental alkaline phosphatase, cancer-associated serum antigen and free beta human chorionic gonadotrophin as prognostic markers for epithelial ovarian cancer,” British Journal of Obstetrics and Gynaecology, vol. 104, no. 9, pp. 1024–1029, 1997.
View at: Google Scholar
A Jeppsson, B Wahren, T Stigbrand, F Edsmyr, and L Andersson, “A clinical evaluation of serum placental alkaline phosphatase in seminoma patients,” British Journal of Urology, vol. 55, no. 1, pp. 73–78, 1983.
View at: Google Scholar
D F Tucker, R TD Oliver, P Travers, and W F Bodmer, “Serum marker potential of placental alkaline phosphatase-like activity in testicular germ cell tumours evaluated by H17E2 monoclonal antibody assay,” British Journal of Cancer, vol. 51, no. 5, pp. 631–639, 1985.
View at: Google Scholar
T F Ford, D N Butcher, C T Samuell, J R Masters, M C Parkinson, and R T Oliver, “Serum and tissue tumour markers in seminomas,” British Journal of Urology, vol. 57, no. 6, pp. 750–754, 1985.
View at: Google Scholar
M E De Broe and D E Pollet, “Multicenter evaluation of human placental alkaline phosphatase as a possible tumor-associated antigen in serum,” Clinical Chemistry, vol. 34, no. 10, pp. 1995–1999, 1988.
View at: Google Scholar
K Koshida and B Wahren, “Placental-like alkaline phosphatase in seminoma,” Urological Research, vol. 18, no. 2, pp. 87–92, 1990.
View at: Google Scholar
K Koshida, T Uchibayashi, H Yamamoto, K Yokoyama, and K Hirano, “A potential use of a monoclonal antibody to placental alkaline phosphatase (PLAP) to detect lymph node metastases of seminoma,” Journal of Urology, vol. 155, no. 1, pp. 337–341, 1996.
View at: Google Scholar
K Koshida, T Uchibayashi, H Yamamoto, and K Hirano, “Significance of placental alkaline phosphatase (PLAP) in the monitoring of patients with seminoma,” British Journal of Urology, vol. 77, no. 1, pp. 138–142, 1996.
View at: Google Scholar
M D Hofer, T J Browne, L He, R I Skotheim, R A Lothe, and M A Rubin, “Identification of two molecular groups of seminomas by using expression and tissue microarrays,” Clinical Cancer Research, vol. 11, no. 16, pp. 5722–5729, 2005.
View at: Publisher Site | Google Scholar
E S Newlands, L Holden, and K D Bagshawe, “Tumour markers and POMB/ACE chemotherapy in the management of ovarian germ cell tumours (GCTs),” International Journal of Biological Markers, vol. 3, no. 3, pp. 185–192, 1988.
View at: Google Scholar
J Shinoda, H Yamada, N Sakai, T Ando, T Hirata, and Y Miwa, “Placental alkaline phosphatase as a tumor marker for primary intracranial germinoma,” Journal of Neurosurgery, vol. 68, no. 5, pp. 710–720, 1988.
View at: Google Scholar
K Koshida, T Stigbrand, E Munck-Wikland, H Hisazumi, and B Wahren, “Analysis of serum placental alkaline phosphatase activity in testicular cancer and cigarette smokers,” Urological Research, vol. 18, no. 3, pp. 169–173, 1990.
View at: Google Scholar
J F Moura, L DeLacerda, R Sandrini et al., “ELISA for determination of human growth hormone: recognition of helix 4 epitopes,” Journal of Biomedicine and Biotechnology, vol. 2004, no. 3, pp. 143–149, 2004.
View at: Publisher Site | Google Scholar
S A Kates and F Albericio, Solid-Phase Synthesis: A Practical Guide, Marcel Dekker, New York, NY, 2000.
J L Millán and T Stigbrand, ““Sandwich” enzyme immunoassay for placental alkaline phosphatase,” Clinical Chemistry, vol. 27, no. 12, pp. 2014–2018, 1981.
View at: Google Scholar
W G Laver, G M Air, R G Webster, and S J Smith-Gill, “Epitopes on protein antigens: misconceptions and realities,” Cell, vol. 61, no. 4, pp. 553–556, 1990.
View at: Google Scholar
P J McLaughlin, H Gee, and P M Johnson, “Placental-type alkaline phosphatase in pregnancy and malignancy plasma: specific estimation using a monoclonal antibody in a solid phase enzyme immunoassay,” Clinica Chimica Acta, vol. 130, no. 2, pp. 199–209, 1983.
View at: Publisher Site | Google Scholar
C P Price, “Multiple forms of human serum alkaline phosphatase: detection and quantitation,” Annals of Clinical Biochemistry, vol. 30, no. 4, pp. 355–372, 1993.
View at: Google Scholar
E J Nouwen, D E Pollet, M W Eerdekens, P G Hendrix, T W Briers, and M E De Broe, “Immunohistochemical localization of placental alkaline phosphatase, carcinoembryonic antigen, and cancer antigen 125 in normal and neoplastic human lung,” Cancer Research, vol. 46, no. 2, pp. 866–876, 1986.
View at: Google Scholar
A Ben-Arie, Z Hagay, H Ben-Hur, M Open, and R Dgani, “Elevated serum alkaline phosphatase may enable early diagnosis of ovarian cancer,” European Journal of Obstetrics Gynecology and Reproductive Biology, vol. 86, no. 1, pp. 69–71, 1999.
View at: Publisher Site | Google Scholar

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Copyright © 2006 Sérvio T. Stinghen et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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