Evidence for two cholesterol ester hydrolases in human cerebrospinal fluid.
In the present study, the properties, such as pH optima, detergent requirement, and effects of various lipids, of cholesterol ester hydrolase in human cerebrospinal fluid (CSF) were examined, and the activity levels of the enzyme in CSF from multiple sclerosis (MS) patients and non-MS individuals were compared. Our data indicate that the enzyme in CSF exhibits two pH optima: pH 6.0 in the presence of Triton X-100 and pH 7.0 in the presence of sodium taurocholate. Both phosphatidylethanolamine (PE) and phosphatidylserine (PS) enhanced the hydrolase activity at pH 6.0. The activity at pH 7.0, on the other hand, was enhanced slightly in the presence of PE but was inhibited in the presence of PS. These data suggest the presence of two cholesterol ester hydrolases in CSF and also indicate that the activity at pH 6.0 may be due to microsomal enzyme in brain and that at pH 7.0 may be due to myelin enzyme. The hydrolase activity at pH 7.0 was significantly lower in CSF from MS patients. The activity at pH 6.0 in CSF from MS and non-MS patients, however, did not differ significantly. This indicates that the reduction in pH 7.0 hydrolase activity in CSF may be related to demyelination.
D002265:Carboxylic Ester Hydrolases / Q000134:cerebrospinal fluid*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000134:cerebrospinal fluid*; D007700:Kinetics; D009103:Multiple Sclerosis / Q000201:enzymology; D010743:Phospholipids / Q000494:pharmacology; D002787:Sterol Esterase / Q000134:cerebrospinal fluid*
D007527:Isoenzymes; D010743:Phospholipids; D002265:Carboxylic Ester Hydrolases; D002787:Sterol Esterase