Alteration of myo-inositol monophosphatase in Alzheimer's disease brains.

Abstract

myo-Inositol monophosphatase (E.C.3.1.3.25) catalyzes the hydrolysis of myo-inositol 1-phosphate in the presence of Mg2+ at a physiologic pH to form free myo-inositol, maintaining a supply that represents the precursor for inositol phospholipid second messenger signaling systems. In the present study the activity and protein level of myo-inositol monophosphatase were investigated in samples from normal human and Alzheimer's disease (AD) postmortem brains. The separation profile on Sephadex G-100 gel filtration chromatography revealed one major form of myo-inositol monophosphatase in crude extracts from both normal human and AD brains. In AD brains myo-inositol monophosphatase activity and its protein level were significantly higher than in control brains. The activity of myo-inositol monophosphatase per enzyme molecule was similar in control and AD brains. These results suggest that myo-inositol monophosphatase is upregulated in AD, probably reflecting compensatory mechanisms concerned with phospholipid metabolism.

• Authors: S Shimohama, H Tanino, Y Sumida, J Tsuda, S Fujimoto
• Journal: Neuroscience letters (Neurosci Lett) Vol. 245 Issue 3 Pg. 159-62 (Apr 10 1998) ISSN: 0304-3940 [Print] Ireland
• PMID: 9605480 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Phospholipids
• Phosphoric Monoester Hydrolases
• myo-inositol-1 (or 4)-monophosphatase

Topics

• Aged
• Aged, 80 and over
• Alzheimer Disease (enzymology)
• Animals
• Brain (enzymology)
• Humans
• Phospholipids (metabolism)
• Phosphoric Monoester Hydrolases (analysis, metabolism)
• Rats
• Rats, Wistar