Effect of fasting on the lipid composition and enzyme activity of rat liver plasma membranes

1980 ◽  
Vol 36 (6) ◽  
pp. 642-643 ◽  
Author(s):  
G. Renaud ◽  
Jacqueline Marais ◽  
R. Infante
Keyword(s):  
Enzyme Activity ◽  
Rat Liver ◽  
Lipid Composition ◽  
Plasma Membranes ◽  
Liver Plasma Membranes ◽  
Rat Liver Plasma Membranes

Effect of clofibrate on the enzyme activity of rat liver plasma membranes

1980 ◽  
Vol 36 (3) ◽  
pp. 281-281
Author(s):  
G. Renaud ◽  
A. Foliot ◽  
J. Marais ◽  
R. Infante
Keyword(s):  
Enzyme Activity ◽  
Rat Liver ◽  
Plasma Membranes ◽  
Liver Plasma Membranes ◽  
Rat Liver Plasma Membranes

Phospholipid modifications influence acyl-CoA:1-acyl-glycero-3-phosphocholine O-acyltransferase in rat liver plasma membranes

1991 ◽  
Vol 69 (9) ◽  
pp. 643-648 ◽  
Author(s):  
Albena B. Momchilova ◽  
Tania T. Markovska ◽  
Svetlana E. Koshlukova ◽  
Kamen S. Koumanov ◽  
Roumen G. Pankov
Keyword(s):  
Membrane Fluidity ◽  
Rat Liver ◽  
Lipid Composition ◽  
Plasma Membranes ◽  
Physical State ◽  
Membrane Lipid ◽  
Lipid Transfer ◽  
Acyltransferase Activity ◽  
Liver Plasma Membranes ◽  
Rat Liver Plasma Membranes

The influence of the membrane lipid composition and physical state on the activity of acyl-CoA: 1-acyl-sn-glycero-3-phosphocholine O-acyltransferase in rat liver plasma membranes has been investigated. The membrane's lipid composition has been modified either by lipid transfer proteins or by partial delipidation with exogenous phospholipases. The results indicate that membrane fluidity is of particular importance for membrane-bound palmitoyl-CoA: and oleoyl-CoA: 1-acyl-glycero-3-phosphocholine acyltransferase. The incorporation of phospholipids that induce membrane fluidization such as dioleoylphosphatidylcholine, egg yolk phosphatidylcholine, phosphatidylinositol, phosphatidylserine, and phosphatidylethanolamine was accompanied by an elevation of acyltransferase activity. On the contrary, the phospholipids causing augmentation of membrane rigidity induced a decrease of this activity. A suggestion is made concerning the possible role of the membrane physical state for the deacylation–reacylation cycle in rat liver plasma membranes.Key words: acyltransferase, plasma membranes, membrane fluidity, phospholipids.

scholarly journals Lipid Composition of Rat Liver Plasma Membranes

1969 ◽  
Vol 244 (20) ◽  
pp. 5528-5536 ◽  
Author(s):  
Tapas K. Ray ◽  
Vladimir P. Skipski ◽  
Marion Barclay ◽  
Edward Essner ◽  
Francis M. Archibald
Keyword(s):  
Rat Liver ◽  
Lipid Composition ◽  
Plasma Membranes ◽  
Liver Plasma Membranes ◽  
Rat Liver Plasma Membranes

scholarly journals Lysophosphatidylcholines can modulate the activity of the glucagon-stimulated adenylate cyclase from rat liver plasma membranes

1979 ◽  
Vol 178 (1) ◽  
pp. 217-221 ◽  
Author(s):  
M D Houslay ◽  
R W Palmer
Keyword(s):  
Adenylate Cyclase ◽  
Rat Liver ◽  
Plasma Membranes ◽  
Hormone Receptors ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Liver Plasma Membranes ◽  
Rat Liver Plasma Membranes ◽  
Increased Sensitivity

1. Synthetic lysophosphatidylcholines inhibit the glucagon-stimulated adenylate cyclase activity of rat liver plasma membranes at concentrations two to five times lower than those needed to inhibit the fluoride-stimulated activity. 2. Specific 125I-labelled glucagon binding to hormone receptors is inhibited at concentrations similar to those inhibiting the fluoride-stimulated activity. 3. At concentrations of lysophosphatidylcholines immediately below those causing inhibition, an activation of adenylate cyclase activity or hormone binding was observed. 4 These effects are essentially reversible. 5. We conclude that the increased sensitivity of glucagon-stimulated adenylate cyclase to inhibition may be due to the lysophosphatidylcholines interfering with the physical coupling between the hormone receptor and catalytic unit of adenylate cyclase. 6. We suggest that, in vivo, it is possible that lysophosphatidylcholines may modulate the activity of adenylate cyclase only when it is in the hormone-stimulated state.

scholarly journals The roles of phospholipase D and a GTP-binding protein in guanosine 5′-[γ-thio]triphosphate-stimulated hydrolysis of phosphatidylcholine in rat liver plasma membranes

1990 ◽  
Vol 272 (3) ◽  
pp. 749-753 ◽  
Author(s):  
K M Hurst ◽  
B P Hughes ◽  
G J Barritt
Keyword(s):  
Rat Liver ◽  
Phospholipase D ◽  
Plasma Membranes ◽  
Regulatory Protein ◽  
Gtp Binding ◽  
Liver Plasma Membranes ◽  
Low Concentrations ◽  
Rat Liver Plasma Membranes ◽  
Triton X ◽  
Hydrolysis Of

1. Guanosine 5′-[gamma-thio]triphosphate (GTP[S]) stimulated by 50% the rate of release of [3H]choline and [3H]phosphorylcholine in rat liver plasma membranes labelled with [3H]choline. About 70% of the radioactivity released in the presence of GTP[S] was [3H]choline and 30% was [3H]phosphorylcholine. 2. The hydrolysis of phosphorylcholine to choline and the conversion of choline to phosphorylcholine did not contribute to the formation of [3H]choline and [3H]phosphorylcholine respectively. 3. The release of [3H]choline from membranes was inhibited by low concentrations of SDS or Triton X-100. Considerably higher concentrations of the detergents were required to inhibit the release of [3H]phosphorylcholine. 4. Guanosine 5′-[beta gamma-imido]triphosphate and guanosine 5′-[alpha beta-methylene]triphosphate, but not adenosine 5′-[gamma-thio]-triphosphate, stimulated [3H]choline release to the same extent as did GTP[S]. The GTP[S]-stimulated [3H]choline release was inhibited by guanosine 5′-[beta-thio]diphosphate, GDP and GTP but not by GMP. 5. It is concluded that, in rat liver plasma membranes, (a) GTP[S]-stimulated hydrolysis of phosphatidylcholine is catalysed predominantly by phospholipase D with some contribution from phospholipase C, and (b) the stimulation of phosphatidylcholine hydrolysis by GTP[s] occurs via a GTP-binding regulatory protein.

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