Multiple forms of the enzyme glycerophosphodiesterase are present in human brain

Lipids
B M RossS J Kish

Abstract

Brain levels of glycerophosphodiesters, including glycerophosphocholine (GPC) and glycerophosphoethanolamine (GPE), are altered in many human central nervous system disorders. Although much information is available on the enzymes responsible for the formation of these phospholipid metabolites, little information is known regarding their catabolism, by glycerophosphodiesterases, in human brain. In both autopsied and biopsied temporal cortex, a phosphocholine-producing glycerophosphodiesterase activity was observed. In the presence of 1 mM EDTA, the enzyme possessed a pH optimum of 9.0, while the addition of 5 mM zinc acetate shifted the pH optimum to 10.5. When assayed at pH 9.0 in the absence of zinc acetate, the Km and Vmax were 104 +/- 2 microM and 77 +/- 18 nmol/h/mg protein, respectively, while assaying at pH 10.5 in the presence of 5mM zinc acetate yielded a Km of 964 +/- 56 microM, and a Vmax of 534 +/- 114 nmol/h/mg protein. Furthermore, whereas submillimolar concentrations of zinc acetate stimulated the activity of the enzyme in a dose-dependent manner when assayed at pH 10.5 (EC50 =20.3 +/- 3.0 microM), this did not result in a reciprocal inhibition of glycerophosphocholine phosphodiesterase (GPC PD) activity when assa...Continue Reading

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Citations

Apr 7, 2000·Movement Disorders : Official Journal of the Movement Disorder Society·B M RossS J Kish
Apr 1, 1997·Lipids·B M RossS J Kish
Apr 13, 2000·Proceedings of the National Academy of Sciences of the United States of America·B ZhengM G Farquhar
Jul 10, 2009·Neurochemical Research·Nguyen Dang HungDai-Eun Sok
Jun 16, 2001·Kidney International·S E RosasH I Feldman
Jun 6, 2003·Kidney International·Sylvia E RosasHarold I Feldman
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