Effects of age-dependent or liposome-induced alterations in the phospholipid composition on sphingomyelin biosynthesis in rat liver microsomal and plasma membranes

1991 ◽  
Vol 23 (7-8) ◽  
pp. 689-693 ◽  
Author(s):  
Diana H. Petkova ◽  
Mariana N. Nikolova ◽  
Svetlana E. Kochlukova ◽  
Kamen S. Koumanov
Keyword(s):  
Rat Liver ◽  
Plasma Membranes ◽  
Phospholipid Composition ◽  
Age Dependent

Use of N-ethylmaleimide to identify the alanine carrier in plasma membranes from rat liver

1983 ◽  
Vol 11 (6) ◽  
pp. 754-755
Author(s):  
MICHAEL R. HAYES ◽  
JOHN D. McGIVAN
Keyword(s):  
Rat Liver ◽  
Plasma Membranes

scholarly journals The Glucagon-sensitive Adenylate Cyclase System in Plasma Membranes of Rat Liver

1972 ◽  
Vol 247 (7) ◽  
pp. 2038-2043 ◽  
Author(s):  
Lutz Birnbaumer ◽  
Stephen L. Pohl ◽  
Martin Rodbell ◽  
Finn Sundby
Keyword(s):  
Adenylate Cyclase ◽  
Rat Liver ◽  
Plasma Membranes ◽  
Adenylate Cyclase System

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.

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