Evidence for the presence of cyclic adenosine 3′,5′-monophosphate and its metabolism in loblolly pine (Pinustaeda L.) callus

1977 ◽  
Vol 7 (1) ◽  
pp. 68-75 ◽  
Author(s):  
Richard H. Smeltzer ◽  
Morris A. Johnson

Evidence is presented suggesting the occurrence of cyclic adenosine 3′,5′-monophosphate (cAMP) and adenyl cyclase activity in loblolly pine (Pinustaeda L.) callus cultures grown aseptically on a defined medium. The presence of enzymes in the callus capable of catalyzing cAMP hydrolysis also was detected. Adenosine was the most stable product resulting from cAMP hydrolysis. A direct relationship was found between apparent cAMP concentration and the rate of fresh weight increase of dark-grown callus during a 6-week passage.

Blood ◽  
1974 ◽  
Vol 43 (5) ◽  
pp. 743-748 ◽  
Author(s):  
Viktor Stolc

Abstract We observed that prostuglandins (PG) E1, E2, A1, A2, B1, and F2 alpha increase cAMP concentration in resting neutrophils. In phagocytosing cells, an additional enhancement was seen with PG E1 and PG A2. Such a stimulatory effect of Pg E1 was noted any time during phagocytosis of latex microparticles (3-18 min). Adrenergic inhibitors, phentolamine and propranolol, did not interfere with the stimulatory action of PG E1 on cAMP level in resting and phagocytosing leukocytes. Both aforementioned inhibitors enhanced cAMP level in resting and phagocytosing neutrophils at 1 mM concentration, and an additional increase was seen in PG E1stimulated leukocytes. Although phosphodiesterase activity was unchanged by phagocytosis and PG E1 action, adenylate cyclase (AC) activity was significantly higher in neutrophil homogenates after phagocytosis of latex particles. In contrary, contact of human lymphocytes with latex particles revealed a decrease in AC activity. These data indicate that AC-cAMP system is partly in a restrained state in resting neutrophils and can be relieved by phagocytosis.


1975 ◽  
Vol 34 (01) ◽  
pp. 042-049 ◽  
Author(s):  
Shuichi Hashimoto ◽  
Sachiko Shibata ◽  
Bokro Kobayashi

SummaryThe radioactive adenosine 3′,5′-monophosphate (cyclic AMP) level derived from 8-14C adenine in intact rabbit platelets decreased in the presence of mitochondrial inhibitor (potassium cyanide) or uncoupler (sodium azide), and markedly increased by the addition of NaF, monoiodoacetic acid (MIA), or 2-deoxy-D-glucose. The stimulative effect of the glycolytic inhibitors was distinctly enhanced by the simultaneous addition of sodium succinate. MIA did neither directly stimulate the adenyl cyclase activity nor inhibit the phosphodiesterase activity. These results suggest that cyclic AMP synthesis in platelets is closely linked to mitochondrial oxidative phosphorylation.


Reproduction ◽  
1974 ◽  
Vol 36 (2) ◽  
pp. 445-446
Author(s):  
C. Nugent ◽  
A Lopata ◽  
M. Gould

1972 ◽  
Vol 20 (11) ◽  
pp. 873-879 ◽  
Author(s):  
S. L. HOWELL ◽  
MARGARET WHITFIELD

A cytochemical method has been used to investigate the localization of adenyl cyclase activity in A and B cells of isolated rat islets of Langerhans. Adenosine triphosphate was initially utilized as substrate, the pyrophosphate liberated being precipitated by lead ions at its site of production. The specificity of the method was increased by the use of adenylyl-imidodiphosphate as an alternative substrate; this adenosine triphosphate analogue was not hydrolyzed by adenosine triphosphatase but provided an effective substrate for adenyl cyclase. Adenyl cyclase activity, which was found to retain its glucagon and fluoride sensitivity in glutaraldehyde-fixed tissue, was found exclusively and almost uniformly in the plasma membranes of A and B cells. Storage granule membrane, incorporated into the plasma membrane during secretion of the granule content by exocytosis, appeared to be devoid of adenyl cyclase activity.


Circulation ◽  
1971 ◽  
Vol 44 (4) ◽  
pp. 638-648 ◽  
Author(s):  
ROBERT E. GOLDSTEIN ◽  
C. LYNN SKELTON ◽  
GERALD S. LEVEY ◽  
D. LUKE GLANCY ◽  
G. DAVID BEISER ◽  
...  

1976 ◽  
Vol 256 (3) ◽  
pp. 319-325 ◽  
Author(s):  
Carla Cipriani ◽  
G. Moretti ◽  
E. Rampini ◽  
Carla Divano

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