Skip to main content
SpringerLink
Log in

Activity of Hydrolytic Enzymes in Various Regions of Normal Human Brain Tissue

  • Original Article
  • Published:
Indian Journal of Clinical Biochemistry Aims and scope Submit manuscript

Abstract

The activity of six hydrolytic enzymes-carboxyl esterase, acid phosphatase, alkaline phosphatase, β-galactosidase, β-glucosidase and β-hexosaminidase, were studied in different regions of the normal human brain tissue obtained at autopsy. Protein estimation and activities of the hydrolytic enzymes with respective substrates were assayed by spectrophotometric and spectroflourometric methods. Amongst the eight regions of the brain-frontal, parietal, occipital, temporal, thalamus, cerebellum and hippocampus, the pineal gland showed highest activity for all hydrolytic enzymes studied except for carboxyl esterase. Among six hydrolases studied, hexosaminidase exhibited highest activity in all regions of the human brain while alkaline phosphatase activity was the least amongst all regions studied. A majority of the enzymes studied showed higher activity in gray matter as compared to the white matter except acid phosphatase and β-glucosidase which exhibited higher activity in the white matter. The most significant finding in the present study was the high activity of all hydrolytic enzymes noted in the pineal gland as compared to all other regions of the human brain. Such a finding has not been hitherto reported earlier in human brain tissue samples. If the specific activities of these enzymes are to be considered as any functional index, then pineal gland may be more metabolically active tissue with respect to the hydrolytic function as compared to the other regions of the brain.

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

Access this article

Log in via an institution

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

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3

Similar content being viewed by others

References

  1. Robins E, Smith DE, Daesch GE, Payne KE. The validation of the quantitative histochemical method for use on post mortem material—II: the effects of fever and uremia. J Neurochem. 1958;3:19–27.

    Article  PubMed  CAS  Google Scholar 

  2. Ramsey RB, Smith KR Jr., Crafts DC, Chung HD, Fredericks M. Hydrolytic enzyme activities of the nervous system. Arch Neurol. 1980;37(6):356–9.

    Article  PubMed  CAS  Google Scholar 

  3. Wielgat P, Walczuk U, Szajda S, Bien M, Zimnoch L, Mariak Z, Zwierz K. Activity of lysosomal exoglycosidases in human gliomas. J Neurooncol. 2006;80(3):243–9.

    Article  PubMed  CAS  Google Scholar 

  4. Cataldo AM, Hamilton DJ, Barnett JL, Paskevich PA, and Nixon RA. Properties of the endosomal-lysosomal system in the human central nervous system: disturbances maik most neurons in populations at risk to degenerate in Alzheimer’s disease. J Neurosci 1996; 16(1):186–l99.

    Google Scholar 

  5. Futerman AH, Gerrit VM. The cell biology of lysosomal storage disorders. Nat Rev Mol Cell Biol. 2004;5:554–65.

    Article  PubMed  CAS  Google Scholar 

  6. Guner G, Kokoglu E, Guner A. Acid and alkaline phosphatase activities in homogenates and subcellular fractions of human brain tumors. Cancer Lett. 1985;29(3):339–43.

    Article  PubMed  CAS  Google Scholar 

  7. Wolleman M. Hydrolytic enzymes. In: Wollemann M (ed) Biochemistry of brain tumors. The Macmillan press Ltd., London; 1974, pp. 123–158.

  8. Friede RL, Knoller M. A quantitative mapping of acid phosphatase in the brain of the rhesus monkey. J Neurochem. 1965;12:150–441.

    Article  Google Scholar 

  9. Zhang W, Xu G, McLeod HL. Comprehensive evaluation of carboxylesterase-2 expression in normal human tissues using tissue array analysis. Appl Immunohistochem Mol Morphol. 2002; 10(4): 374–80.

    Google Scholar 

  10. Sinha L and Sinha AK. Lysosomal Hydrolases in developing human brain regions. J Neurochem 1980;1080–1086.

  11. Hirsch HE. Differential determination of Hexosaminidases A and B and two forms of β-galactosidase, in the layers of the human cerebellum. J Neurochem. 1972;19(6):1513–7.

    Article  PubMed  CAS  Google Scholar 

  12. Lowry OH, Rosebrough NJ, Farr AR, Randoll RJ. Protein measurement with the Folin-phenol reagent. J Biol Chem. 1951;193:265–75.

    PubMed  CAS  Google Scholar 

  13. Hartree EF. Determination of proteins: a modification of the Lowry method that gives a linear photometric response. Anal Biochem. 1972;48:422–7.

    Article  PubMed  CAS  Google Scholar 

  14. Gomori G. The distribution of phosphatase in normal organs and tissues. J Cell Comp Physiol. 1941;17:71–83.

    Article  CAS  Google Scholar 

  15. Asperen VK. A study of housefly esterases by means of a sensitive colorimetric method. J Insect Physiol 1962;8:401–16.

    Google Scholar 

  16. Lam WK, Lai LC, Yam LT. Tartrate-resistant (Band 5) acid phosphatase activity measured by electrophoresis on acrylamide gel. Clin Chem. 1978;24(2):309–12.

    PubMed  CAS  Google Scholar 

  17. Fernley H. Mammalian alkaline phosphatases. In: P. Boyer, editor. The Enzymes, 3rd edn. New York: Academic Press. 1971. p. 417.

  18. McComb RB, Bowers GN Jr., Posen S. Alkaline phosphatase. New York: Plenum Press, c1979:1926.

  19. Falck B. Observations on the possibilities of the cellular localization of monoamines by a fluorescence method. Acta Physiol Scand. 1962;56(Suppl):197.

    Google Scholar 

  20. Peters SP, Coyle P, Glew RH. Differentiation of β-glucocerebrosidase from β-glucosidase in human tissues using sodium taurocholate. Arch Biochem Biophys. 1976;175:569–82.

    Article  PubMed  CAS  Google Scholar 

  21. O’Brien JS, Okada S, Chen A, Fillerup DL. Tay Sach’s disease: detection of heterozygotes and homozygotes by serum hexosaminidase assay. N Engl J Med. 1970;283(1):15–20.

    Article  PubMed  Google Scholar 

  22. Leaback DH, Walker PG. Studies on glucosaminidase 4. The fluorimetric assay of N-acetyl-β-glucosaminidase. Biochem J. 1961;78:151–6.

    PubMed  CAS  Google Scholar 

  23. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227(259):680–5.

    Article  PubMed  CAS  Google Scholar 

  24. Hojring N, Svensmark O. Carboxylesterases with different substrate Specificity in human brain extracts. J Neurochem. 1976;27(2):523–8.

    Article  Google Scholar 

  25. Hardy JA, Dodd PR. Metabolic and functional studies on post-mortem human brain. Neurochem Int 1983; 5(3): 253–66. (Commentary).

    Google Scholar 

  26. Schiffer D, Vesco C, Piazza L. Contribution to the histochemical demonstration and distribution of phosphatases and non-specific esterase in human nervous tissue. Psychiat Neurol (Basel). 1962;144:34–7.

    Article  CAS  Google Scholar 

  27. Fleischhacker HH. Studies on the brain phosphatases. J Ment Sci. 1938;84:947–59.

    CAS  Google Scholar 

  28. Hirsch HE, Robins E. Fed Proc. 1961;20:342.

    Google Scholar 

  29. Tallman JF, Johnson WG, Brady RO. The metabolism of Tay-Sachs ganglioside: catabolic studies with lysosomal enzymes from normal and Tay-Sachs brain tissue. J Clin Invest. 1972;51(9):2339–45.

    Article  PubMed  CAS  Google Scholar 

  30. Prabha.M, Ravi V, Shetty KT, Swamy NR. Pineal gland of elevated hydrolytic enzyme activities and similar carboxyl esterase activity to the rest of the brain regions. Proceedings of the National conference in Chemistry. Sept 27–29, Bangalore, 2006.

  31. Prabha M. A Comparative biochemical study on hydrolytic enzymes in normal postmortem human brain, brain tumors and in their derived cell lines. Dissertation. Bangalore University; 2005.

Download references

Author information

Authors and Affiliations

  1. Department of Biochemistry, Central College, Bangalore, 560001, India

    M. Prabha

  2. Departments of Neurovirology and Neurochemistry, NIMHANS, Bangalore, 560029, India

    M. Prabha & V. Ravi

  3. Department of Biotechnology, MSRIT, Bangalore, 560001, India

    M. Prabha

  4. Department of Biochemistry, Central college, Bangalore University, Bangalore, India

    N. Ramachandra Swamy

Authors
  1. M. Prabha
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. V. Ravi
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. N. Ramachandra Swamy
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to M. Prabha.

Electronic supplementary material

Below is the link to the electronic supplementary material.

Supplementary material 1 (DOC 56 kb)

Rights and permissions

Reprints and permissions

About this article

Cite this article

Prabha, M., Ravi, V. & Ramachandra Swamy, N. Activity of Hydrolytic Enzymes in Various Regions of Normal Human Brain Tissue. Ind J Clin Biochem 28, 283–291 (2013). https://doi.org/10.1007/s12291-012-0273-0

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12291-012-0273-0

Keywords

Search

Navigation