Ectonucleotidases of Avian Gizzard Smooth Muscle and Liver Plasma Membranes: A Comparative Study

1999 ◽  
Vol 362 (1) ◽  
pp. 46-58 ◽  
Author(s):  
Charles C. Caldwell ◽  
Michael D. Davis ◽  
Aileen F. Knowles
Keyword(s):  
Smooth Muscle ◽  
Comparative Study ◽  
Plasma Membranes ◽  
Liver Plasma Membranes

scholarly journals Gs mediates hormonal inhibition of the calcium pump in liver plasma membranes.

1993 ◽  
Vol 268 (4) ◽  
pp. 2368-2372
Author(s):  
C. Jouneaux ◽  
Y. Audigier ◽  
P. Goldsmith ◽  
F. Pecker ◽  
S. Lotersztajn
Keyword(s):  
Plasma Membranes ◽  
Calcium Pump ◽  
Liver Plasma Membranes

scholarly journals Quantitative Aspects of the Insulin-Receptor Interaction in Liver Plasma Membranes

1974 ◽  
Vol 249 (7) ◽  
pp. 2249-2257 ◽  
Author(s):  
C. Ronald Kahn ◽  
Pierre Freychet ◽  
Jesse Roth ◽  
David M. Neville
Keyword(s):  
Insulin Receptor ◽  
Plasma Membranes ◽  
Receptor Interaction ◽  
Liver Plasma Membranes

scholarly journals The NSILA-s receptor in liver plasma membranes. Characterization and comparison with the insulin receptor

1975 ◽  
Vol 250 (23) ◽  
pp. 8990-8996 ◽  
Author(s):  
K Megyesi ◽  
CR Kahn ◽  
J Roth ◽  
DM Neville ◽  
SP Nissley ◽  
...  
Keyword(s):  
Insulin Receptor ◽  
Plasma Membranes ◽  
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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