Abstract
Alkaline phosphatase (ALP) is a substance thought to participate in active transport. Formerly it was thought that only diseases of the bone, liver or bileduct result in a rise of serum ALP. However, owing to improved methods for the analysis of isoenzymes, e.g., electrophoresis and various inhibition tests, it is now possible to identify ALP isoenzymes originating not only in the bone or liver, but also in the small intestine or placenta.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Baker JR: The histochemical recognition of lipine. Quart J Micr Sci 87: 441, 1946.
Burstone MS: Histochemical comparison of naphthol As-phosphates for the demonstration of phosphatases. J Nat Canc Inst 20: 601, 1958.
Fishman WH, Inglis NR, Stolbach LL, Krant MJ: A serum alkaline phosphatase isoenzyme of human neoplastic cell origin. Cancer Res 28: 150, 1968.
Fishman WH: Carcinoplacental isoenzyme antigens. In Weber G (ed): Advances in enzyme regulation, Vol XI. New York: Pergamon Press, 1973, pp 293–321.
Greenstein TP: Biochemistry of cancer, 2nd ed. New York: Academic Press, 1954.
Holt SJ: Factors governing the validity of staining methods for enzymes, and their bearing upon the Gomori acid phosphatase technique. Exp Cell Res Suppl VII, 1, 1959.
Izumi S: Histochemical characterization of reserve cell alkaline phosphatase — with a special reference to heat stability test and L-phenylalanine test. Acta Obst Gynec Jpn 29: 149, 1977.
Jensen H, Lynghye J, Davidsen S: Histochemical investigation of the thermostable alkaline phosphatase in the normal full-term placenta. Acta Obst Gynec Scandinav 47: 437, 1968.
Kellen JA, Bush RS, Malkin A: Placenta-like alkaline phosphatase in gynecological cancers. Cancer Res 36: 269, 1976.
Malkin A, Kellen JA, Caplan B: The presence of placenta-like alkaline phosphatase in normal human uterine cervix and endometrium. In Lehman FG (ed): Carcino-Embryonic Proteins, Vol II. Amsterdam: North Holland: Elsevier, 1979, pp 679–684.
Mayahara H, Hirano H, Saito T, Ogawa K: The new lead citrate method for the ultracytochemical demonstration of activity of non-specific alkaline phosphatase. (Orthophosphoric mono-ester phosphohydrolase). Histochemie 11: 88, 1967.
Nakayama T, Yoshida M, Kitamura M: L-leucine sensitive, heat-stable alkaline-phosphatase isoenzyme detected in a patient with pleuritis carcinomatosa. Clin Chem Acta 30: 546, 1970.
Nathanson L, Fishman WH: New observations on the Regan isoenzyme of alkaline phosphatase in cancer patients. Cancer 27: 1388, 1977.
Nozawa W, Izumi S, Ohta H, Shinozuka T, Tsutsui F, Kurihara S, Watanabe K: Histochemical studies on alkaline phosphatase in uterine cervical reserve cell, precancerous and cancerous lesions. In Shanmugaratnam K (ed): Proc 2nd Asian Cancer Conference. Singapore: Stanford College Press, 1975, pp 324–326.
Nozawa S, Ohta H, Izumi S, Hayashi S, Tsutsui F, Kurihara S: Watanabe K: Heat-stable alkaline phosphatase in normal female genital organ — With special reference to the histochemical heat-stability test and L-phenylalanine inhibition test. Acta Histochem Cytochem 13: 521, 1980.
Nozawa S, Ohta H, Izumi S, Hayashi S, Tsutsui F, Kurihara S: Heat stable alkaline phosphatase in uterine cancer. Histochem J 13: 941, 1981.
Schapira F, Dreyfuss JC, Schapira G: Anomaly of aldolase in primary liver cancer. Nature 200: 995, 1963.
Stolbach LL, Krant MJ, Fishman WH: Ectopic production of an alkaline phosphatase isoenzyme in patients with cancer. Ann NY Acad Sci 166: 760, 1969.
Sugimura T, Matsushima T, Kawachi T, Kogure K, Tanaka N, Miyake S, Hozumi M, Sato H: Disdifferentiation and Decarcinogenesis. Gann Monograph Cancer Res 13: 31, 1972.
Usategui-Gomez M, Yeager FM, Castro AF: Regan isoenzyme in normal human sera. Cancer Res 34: 2544, 1974.
Watanabe K, Fishman WH: Application of stereospecific inhibitor, L-phenylalanine to the enzymorphology of intestinal alkaline phosphatase. J Histochem Cytochem 12: 252, 1964.
Weinhaus S: Homologies in enzymes and metabolic pathways. In Whelam WJ, Schultz J (eds): Metabolic alternative in cancer. Amsterdam: North-Holland, 1970, pp 462.
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1982 Martinus Nijhoff Publishers, The Hague
About this chapter
Cite this chapter
Nozawa, S., Oota, H., Arai, K., Izumi, S., Tsutsui, F., Kurihara, S. (1982). Histochemistry of Alkaline Phosphatase in Cervical Neoplasia. In: Hafez, E.S.E., Smith, J.P. (eds) Carcinoma of the Cervix. Developments in Obstetrics and Gynecology, vol 6. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-7485-2_17
Download citation
DOI: https://doi.org/10.1007/978-94-009-7485-2_17
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-009-7487-6
Online ISBN: 978-94-009-7485-2
eBook Packages: Springer Book Archive