scholarly journals The effect of fluoride on the state of aggregation of adenylate cyclase in rat liver plasma membranes

1980 ◽  
Vol 188 (1) ◽  
pp. 137-140 ◽  
Author(s):  
B R Martin ◽  
J M Stein ◽  
E L Kennedy ◽  
C A Doberska
Keyword(s):  
Adenylate Cyclase ◽  
Rat Liver ◽  
Plasma Membranes ◽  
The State ◽  
Target Size ◽  
Liver Plasma Membranes ◽  
Rat Liver Plasma Membranes

Irradiation inactivation was used to monitor changes in the state of adenylate cyclase in rat liver plasma membranes in the presence of F-.F- caused a decrease in the target size from 328000 to 237000 at 0 degrees C and from 329000 to 219000 at 30 degrees C. Adenylate cyclase was activated by F- at both 0 degrees C and 30 degrees C. The effect of F- was biphasic, activating up to a concentration of 10mM and inhibiting at higher concentrations. If adenylate cyclase weas maximally activated with glucagon and p[NH]ppG ([beta gamma-imido]GTP) all concentrations of F- were inhibitory. The implications of the results with respect to the mechanism of activation of adenylate cyclase are discussed.

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.

Effects of 4-hydroxynonenal on adenylate cyclase and 5′-nucleotidase activities in rat liver plasma membranes

1985 ◽  
Vol 53 ◽  
pp. 209-217 ◽  
Author(s):  
Luciana Paradisi ◽  
Carla Panagini ◽  
Maurizio Parola ◽  
Giuseppina Barrera ◽  
Mario U. Dianzani
Keyword(s):  
Adenylate Cyclase ◽  
Rat Liver ◽  
Plasma Membranes ◽  
Liver Plasma Membranes ◽  
Rat Liver Plasma Membranes

The characteristics of lubrol-solubilized adenylate cyclase from rat liver plasma membranes

1978 ◽  
Vol 522 (2) ◽  
pp. 625-639 ◽  
Author(s):  
Ann F. Welton ◽  
Pramod M. Lad ◽  
Andrew C. Newby ◽  
Hirohei Yamamura ◽  
Simonetta Nicosta ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Rat Liver ◽  
Plasma Membranes ◽  
Liver Plasma Membranes ◽  
Rat Liver Plasma Membranes
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