Cellular and Molecular Neurobiology

, Volume 21, Issue 3, pp 285–296

Butyrylcholinesterase-Mediated Enhancement of the Enzymatic Activity of Trypsin

Authors

  • Sultan Darvesh
    • Department of Medicine (Neurology and Geriatric Medicine)
    • Department of Anatomy and NeurobiologyDalhousie University
    • Department of ChemistryMount Saint Vincent University
  • Rohit Kumar
    • Department of Anatomy and NeurobiologyDalhousie University
  • Sheila Roberts
    • Department of ChemistryMount Saint Vincent University
  • Ryan Walsh
    • Department of ChemistryMount Saint Vincent University
  • Earl Martin
    • Department of ChemistryMount Saint Vincent University
Article

DOI: 10.1023/A:1010947205224

Cite this article as:
Darvesh, S., Kumar, R., Roberts, S. et al. Cell Mol Neurobiol (2001) 21: 285. doi:10.1023/A:1010947205224

Abstract

1. Acetylcholinesterase (AChE, EC 3.1.1.7) and butyrylcholinesterase (BuChE, EC 3.1.1.8) are enzymes that catalyze the hydrolysis of esters of choline.

2. Both AChE and BuChE have been shown to copurify with peptidases.

3. BuChE has also been shown to copurify with other proteins such as transferrin, with which it forms a stable complex. In addition, BuChE is found in association with β-amyloid protein in Alzheimer brain tissues.

4. Since BuChE copurifies with peptidases, we hypothesized that BuChE interacts with these enzymes and that this association had an influence on their catalytic activities. One of the peptidases that copurifies with cholinesterases has specificity similar to trypsin, hence, this enzyme was used as a model to test this hypothesis.

5. Purified BuChE causes a concentration-dependent enhancement of the catalytic activity of trypsin while trypsin does not influence the catalytic activity of BuChE.

6. We suggest that, in addition to its esterase activity, BuChE may assume a regulatory role by interacting with other proteins.

butyrylcholinesteraseacetylcholinesterasetrypsinAlzheimer

Copyright information

© Plenum Publishing Corporation 2001