Skip to main content
Log in

The demonstration of acid phosphatase in cultured 3T3 mouse cells

  • Published:
Histochemistry Aims and scope Submit manuscript

Summary

Acid phosphatase has been demonstrated ultrastructurally in 3T3 and SV40-3T3 mouse cells using sodium β-glycerophosphate and p-nitrophenyl phosphate as substrate. The former substrate only demonstrates the enzyme in lysosomes and elements of the Golgi apparatus while the latter demonstrates it in the cisternae of the endoplasmic reticulum and in the cell surface as well as at lysosomal sites. The significance of surface acid phosphatase activity is discussed in terms of sublethal autolysis.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Beadle, D.J., Dawson, A.L., Amos, S., Black, P.: The distribution of ingested ferritin and acid phosphatase activity in the vacuolar system of normal and virus-transformed mouse 3T3 cells. Cytobios in press (1976)

  • Beadle, D.J., Gahan, P.B.: Cytochemical studies of the types and localisation of acid phosphatases in the various regions of the midgut epithelium of Carausius morosus. Histochem. J. 1, 539–549 (1969)

    Google Scholar 

  • Biberfeld, P.: A method for the study of monolayer cultures with preserved cell orientation and interrelationship. J. Ultrastruct. Res. 25, 158–159 (1968)

    Google Scholar 

  • Bosmann, H.B.: Glycoprotein degradation. Glycosidases in fibroblasts transformed by oncogenic viruses. Exp. Cell Res. 54, 217–221 (1969)

    Google Scholar 

  • Bosmann, H.B.: Elevated glycosidases and proteolytic enzymes in cells transformed by RNA tumour virus. Biochim biophys. Acta (Amst.) 262, 339–343 (1972)

    Google Scholar 

  • Bosmann, H.B.: Release of specific protease during mitotic cycle of L5178Y murine leukaemic cells by sublethal autolysis. Nature (Lond.) 249, 144–145 (1974)

    Google Scholar 

  • Bosmann, H.B., Lockwood, T., Morgan, H.R.: Surface biochemical changes accompanying primary infection with Rous sarcoma virus. Exp. Cell Res. 83, 25–30 (1974)

    Google Scholar 

  • Brunk, V.T., Ericsson, J.L.E.: The demonstration of acid phosphatase in in vitro cultured tissue cells. Studies on the significance of fixation, tonicity and permeability. Histochem. J. 4, 349–63 (1972)

    Google Scholar 

  • Butterworth, J.: Histochemistry of non-specific phosphatases: the use of p-nitrophenyl phosphate and β-glycerophosphate as substrates. Histochem. J. 3, 477–487 (1971)

    Google Scholar 

  • Dowson, A.L.: Some aspects of the ultrastructure and enzyme cytochemistry of normal and virustransformed cells. In preparation

  • Dawson, A.L., Beadle, D.J., Livingston, D.C., Fisher, S.W.: A histochemical study of acid phosphatase in normal and virus-transformed cultured fibroblasts. Histochem. J. 7, 77–84 (1975)

    Google Scholar 

  • Elligsen, J.D., Thompson, J.E., Frey, H.E.: An evaluation of lysosomal enzyme leakage as a factor influencing the behaviour of transformed cells. Exp. Cell Res. 92, 87–94 (1975)

    Google Scholar 

  • Horvat, A., Acs, G.: Induction of lysosomal enzymes in contact-inhibited 3T3 cells. J. Cell Physiol. 83, 59–68 (1974)

    Google Scholar 

  • Lin, C.W., Fishman, W.H.: Microsomal and lysosomal acid phosphatase isoenzymes of mouse kidney: characterization and separation. J. Histochem. Cytochem. 20, 487–498 (1972)

    Google Scholar 

  • Maciero-Coelho, A., Garcia-Giralt, E., Adrian, M.: Changes in lysosomal associated structures in human fibroblasts kept in resting phase.Proc. Soc. exp. Biol. (N.Y.) 138, 712–18 (1971)

    Google Scholar 

  • Maggi, V., Franks, L. M., Carbonell, A. W.: Histochemical study of a number of hydrolases, including a new acid phosphatase, in various tissues of men an mice. Histochemie 6, 305–316 (1966)

    Google Scholar 

  • Miyayama, H., Solomon, R., Sasaki, M., Lin, C., Fishman, W.H.: Demonstration of lysosomal and extralysosomal sites for acid phosphatase in mouse kidney tubule cell with p-nitrophenylphosphate lead-salt technique. J. Histochem. Cytochem. 23, 439–451 (1975)

    Google Scholar 

  • Neil, N.W., Horner, M.W.: The acid p-nitrophenyl phosphatase activity of adult guinea pig liver subcellular fractions. Biochem. J. 84, 32P (1962)

  • Nelson, D.: Rat liver acid phosphatases. Differences in lysosomal and cytoplasmic forms. Proc. Soc. exp. Biol. (N.Y.) 121, 998–1001 (1962)

    Google Scholar 

  • Poste, G.: Sub-lethal autolysis. Modification of cell periphery by lysosomal enzymes. Exp. Cell Res. 67, 11–16 (1971)

    Google Scholar 

  • Ryder, T.A., Bowen, I.D.: A method for the fine structural localisation of acid phosphatase activity using p-nitrophenyl phosphate as substrate. J. Histochem. Cytochem. 23, 235–237 (1975)

    Google Scholar 

  • Wilson, P.D.: Reversible and irreversible effects of tissue culture on enzyme patterns of sponataneous mouse tumours and mouse and human embryo tissues. Cancer Res. 33, 375–82 (1973)

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Beadle, D.J., Dawson, A.L. & Amos, S. The demonstration of acid phosphatase in cultured 3T3 mouse cells. Histochemistry 48, 161–166 (1976). https://doi.org/10.1007/BF00494554

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00494554

Keywords

Navigation