Oleate stimulation of diacylglycerol formation from phosphatidylcholine through effects on phospholipase D and phosphatidate phosphohydrolase
نویسندگان
چکیده
منابع مشابه
The effect of oleate and spermine on the subcellular distribution of phosphatidate phosphohydrolase (PAH, EC 3.1.34).
Phospha t i d a t e p h o s p h o h y d r o l a s r (PAH) c a t a l y s e s t h e c o n v e r s i o n o f phospha t i d a t e t o d i a c y l g l y c r r o l and is a n i m p o r i a n t r e g u l a t o r y s t e p i n t r i a c y l g l y r e r o l synthesis. Long t e r m c o n t r o l o f enzyme a c t i v i t y is m e d i a t r d by hormones r i t h e r v i a i n c r r a s e d r n z y m c s y ...
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The effects of steroid hormones, glucagon and insulin on rat liver phosphatidate phosphohydrolase (PAP) activity were studied both in vitro and in vivo. Incubation of rat hepatocytes with each hormone showed that dehydroepiandrosterone (DHEA), progesterone and testosterone increase PAP activity by 44.6, 37 and 36.9%, respectively. Estradiol, however, decreased enzyme activity by 13.6% under...
متن کاملDiacylglycerol-rich domain formation in giant stearoyl-oleoyl phosphatidylcholine vesicles driven by phospholipase C activity.
We have studied the effect of phospholipase C from Bacillus cereus and Clostridium perfringens (alpha-toxin) on giant stearoyl-oleoyl phosphatidylcholine (SOPC) vesicles. Enzyme activity leads to a binary mixture of SOPC and the diacylglycerol SOG, which phase separates into a SOPC-rich bilayer phase and a SOG-rich isotropic bulk-like domain embedded within the membrane, as seen directly by pha...
متن کاملThe Relationship between Cation-Induced Substrate Configuration and Enzymatic Activity of Phosphatidate Phosphohydrolase from Human Liver
The mechanism by which bi-and trivalent cations affect human liver phosphatidatephosphohydrolase (PAP) activity was investigated. Bivalent cations up to 1 mM increased PAP activity whereas at higher concentrations the activity of the enzyme decreased. The stimulatory concentration for trivalent cations such as Al3+ and Cr3+, however, was much lower being 2 m M and 1 m M, respectively. All catio...
متن کاملA rapid sensitive assay for phosphatidate phosphohydrolase.
For a purified preparation of the soluble form of phosphatidate phosphohydrolase (EC 3.1.3.4) from guinea pig cerebral cortex, I-O-alkyl-racglycerol 3-phosphate was found to be accepted as a substrate. This substrate analog was tritium-labeled in order to serve in a rapid sensitive assay for the enzyme, in which labeled I-alkyl glycerol is released. Heat denaturation and enzyme activity depende...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1992
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1992.tb17460.x