Summary
Bile canalicular phosphatase activity in frog, chicken, rat and cat has been studied with respect to substrate specificity, pH optimum and effect of various stimulators and inhibitors.
It is concluded that three different bile canalicular phosphatase activities may be demonstrated histochemically: 1. A strong non-specific nucleoside diphosphatase able to split ATP and most diphosphates. Its relevance is, however, uncertain and requires confirmation by biochemical studies. 2. A non-specific alkaline phosphatase, 3. 5′-nucleotidase.
Evidence is presented that the bile oanalicular staining reflects real enzyme activity and not artificial non-enzymatic hydrolysis.
Similar content being viewed by others
References
Abel, J.H.: Electron microscopic demonstration of adenosinetriphosphate phosphohydrolase activity in herring gull salt glands. J. Histochem. Cytochem. 17, 570–584 (1966).
Coleman, J.R.: Biochemical and cytochemical demonstration of ATP-ase activity in nuclei. J. Cell Biol. 27, 20A (1965).
Essner, E., Novikoff, A.B., Masek, B.: Adenosinetriphosphatase and 5-nucleotidase activities in the plasma membrane of liver cells as revealed by electron microscopy. J. biophys. biochem. Cytol. 4, 711–716 (1958).
Freiman, D.G., Kaplan, N.: Studies on the histochemical differentiation of enzymes hydrolyzing adenosine triphosphate. J. Histochem. Cytochem. 8, 159–170 (1960).
Gomori, G.: Distribution of phosphatase in normal organs and tissues. J. cell. comp. Physiol. 17, 71–83 (1941).
—: Microscopic histochemistry. Chicago: Chicago Univ. Press 1952.
Jacobsen, N.O., Jörgensen, P.L.: A quantitative biochemical and histochemical study of the lead method for localization of adenosine triphosphate-hydrolyzing enzymes. J. Histochem. Cytochem. 17, 443–453 (1969).
Kornberg, A.: Reversible enzymatic synthesis of diphosphopyridine nucleotide and inorganic pyrophosphate. J. biol. Chem. 182, 779–793 (1950).
Marchesi, V.T., Palade, G.T.: The localization of Mg-Na-K-activated adenosinetriphosphatase on red cell ghost membranes. J. Cell Biol. 35, 385–404 (1967).
Mieler, W., Zoellner, H.: Der histochemische Nachweis von Phosphatasen in Leber und Niere mit verschiedenen Substraten. Acta histochem. (Jena) 8, 325–339 (1959).
Moses, H.L., Rosenthal, A.L.: Pitfalls in the use of lead ion for histochemical localization of nucleoside phosphatases. J. Histochem. Cytochem. 16, 530–539 (1968).
Novikoff, A.B.: Enzyme localization with Wachstein-Meisel procedures: Real or artifact. J. Histochem. Cytochem. 15, 353–354 (1967).
—, Drucker, J., Shin, W.Y., Goldfischer, S.: Further studies on the apparent adenosinetriphosphatase activity of cell membranes in formol-calcium-fixed tissues. J. Histochem. Cytochem. 9, 431–451 (1961).
—, Hausman, D.H., Podber, E.: The localization of adenosinetriphosphatase in liver. In situ stained and cell fractionation studies. J. Histochem. Cytochem. 6, 61–71 (1958).
—, Hecht, L., Podber, E., Ryan, J.: Phosphates of rat liver. I. The dephosphorylation of adenosinetriphosphate. J. biol. Chem. 194, 153–170 (1952).
Padykula, H.A., Herman, E.: The specificity of the histochemical method for adenosine triphosphatase. J. Histochem. Cytochem. 3, 170–183 (1955).
Rosenthal, A. S., Moses, H.L., Tice, L., Ganote, C.E.: Lead ion and phosphatase histochemistry. III. The effects of lead and adenosine triphosphate concentration on the incorporation of phosphate into fixed tissue. J. Histochem. Cytochem. 17, 607–612 (1969).
Sandström, B.: Liver fixation for electron microscopy by means of transparenchymal perfusion with glutaraldehyde. Lab. Invest. (1970) (to be published).
—, Westman, J.: Non-freezing light and electron microscopic histochemistry by means of polyetyleneglycol embedding. Histochemie 19, 181–183 (1969).
Vorbrodt, A.: Histochemical studies on thiaminepyrophosphatase localization in the adult, embryonic and neoplastic liver cells using light and electron microscopy. Acta histochem. (Jena) 28, 204–214 (1967).
Wachstein, M., Meisel, E.: Histochemistry of hepatic phosphatases at a physiological pH. Amer. J. clin. Path. 27, 13–23 (1957).
Author information
Authors and Affiliations
Additional information
This study was supported in part by a grant from the Swedish Medical Research Council.
Rights and permissions
About this article
Cite this article
Sandström, B. On the specificity of histochemically demonstrable bile canalicular phosphatase activities. Histochemie 22, 316–323 (1970). https://doi.org/10.1007/BF00277459
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00277459