Stimulation of the insulin-sensitive cAMP phosphodiesterase by an ATP-dependent soluble factor from insulin-treated rat adipocytes

1990 ◽  
Vol 167 (2) ◽  
pp. 614-620 ◽  
Author(s):  
Hiroshi Shibata ◽  
Tetsuro Kono
Keyword(s):  
Soluble Factor ◽  
Camp Phosphodiesterase ◽  
Rat Adipocytes ◽  
Stimulation Of

scholarly journals Cyclic GMP-dependent Stimulation of the Membrane-bound Insulin-sensitive cAMP Phosphodiesterase from Rat Adipocytes

1989 ◽  
Vol 264 (28) ◽  
pp. 16458-16464
Author(s):  
F W Robinson ◽  
C J Smith ◽  
J E Flanagan ◽  
H Shibata ◽  
T Kono
Keyword(s):  
Cyclic Gmp ◽  
Camp Phosphodiesterase ◽  
Rat Adipocytes ◽  
Membrane Bound ◽  
Stimulation Of

Stimulation of Ca(2+)-dependent exocytosis of the sperm acrosome by cAMP acting downstream of phospholipase A2

Reproduction ◽  
2000 ◽  
pp. 57-68 ◽  
Author(s):  
J Garde ◽  
ER Roldan
Keyword(s):  
Arachidonic Acid ◽  
Phospholipase A2 ◽  
Phospholipase C ◽  
Phosphodiesterase Inhibitors ◽  
Dibutyryl Camp ◽  
Camp Phosphodiesterase ◽  
Ram Sperm ◽  
Camp Formation ◽  
Stimulation Of

Spermatozoa undergo exocytosis in response to agonists that induce Ca2+ influx and, in turn, activation of phosphoinositidase C, phospholipase C, phospholipase A2, and cAMP formation. Since the role of cAMP downstream of Ca2+ influx is unknown, this study investigated whether cAMP modulates phospholipase C or phospholipase A2 using a ram sperm model stimulated with A23187 and Ca2+. Exposure to dibutyryl-cAMP, phosphodiesterase inhibitors or forskolin resulted in enhancement of exocytosis. However, the effect was not due to stimulation of phospholipase C or phospholipase A2: in spermatozoa prelabelled with [3H]palmitic acid or [14C]arachidonic acid, these reagents did not enhance [3H]diacylglycerol formation or [14C]arachidonic acid release. Spermatozoa were treated with the phospholipase A2 inhibitor aristolochic acid, and dibutyryl-cAMP to test whether cAMP acts downstream of phospholipase A2. Under these conditions, exocytosis did not occur in response to A23187 and Ca2+. However, inclusion of dibutyryl-cAMP and the phospholipase A2 metabolite lysophosphatidylcholine did result in exocytosis (at an extent similar to that seen when cells were treated with A23187/Ca2+ and without the inhibitor). Inclusion of lysophosphatidylcholine alone, without dibutyryl-cAMP, enhanced exocytosis to a lesser extent, demonstrating that cAMP requires a phospholipase A2 metabolite to stimulate the final stages of exocytosis. These results indicate that cAMP may act downstream of phospholipase A2, exerting a regulatory role in the exocytosis triggered by physiological agonists.

Stimulation of Leptin Release by Actinomycin D in Rat Adipocytes

1998 ◽  
Vol 55 (8) ◽  
pp. 1309-1314 ◽  
Author(s):  
John N. Fain ◽  
Suleiman W. Bahouth
Keyword(s):  
Actinomycin D ◽  
Rat Adipocytes ◽  
Stimulation Of

Mechanism for Dual Regulation of the Particulate cGMP-Inhibited cAMP Phosphodiesterase in Rat Adipocytes by Isoproterenol and Insulin

1990 ◽  
pp. 309-314
Author(s):  
C. J. Smith ◽  
E. Degerman ◽  
V. Vasta ◽  
H. Tornqvist ◽  
P. Belfrage ◽  
...  
Keyword(s):  
Camp Phosphodiesterase ◽  
Rat Adipocytes
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