Regulation of lipase activities in rat brain in vitro.
Regulation of acid and neutral lipase activities in rat brain was examined in vitro. Both activities were decreased by SDS, CuCl2 and ZnCl2 and by delipidation. The neutral lipase activity was also markedly reduced by N-ethylmaleimide and PbCl2. The activity of delipidated preparation was increased by addition of phosphatidyl choline at both pH 5.5 and 7.5 and by phosphatidyl serine at acidic pH value. Pretreatments of the enzyme preparation with phospholipase A and trypsin reduced the lipase activities at both pH values. It is suggested that phospholipids play an important role on lipase activity in brain.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D005033:Ethylmaleimide / Q000494:pharmacology; D066298:In Vitro Techniques; D008049:Lipase / Q000032:analysis*; D008297:Male; D010743:Phospholipids / Q000494:pharmacology; D051381:Rats; D014280:Triglycerides / Q000378:metabolism
D010743:Phospholipids; D014280:Triglycerides; D008049:Lipase; D005033:Ethylmaleimide