Phosphodiesterase activity and cyclic AMP content during early germination of Mucor rouxii spores

C TOMES AND S MORENO

FUNGAL GENETICS AND BIOLOGY

Elsevier

Lugar: Amsterdam, Holanda; Año: 1990 vol. 14 p. 78 - 83

1087-1845

Phosphodiesterase activity and cyclic AMP content during early germination of Mucor rouxii spores. Experimental Mycology 13, 78-83. Incubation ofMucor rouxii spores. Experimental Mycology 13, 78-83. Incubation of Mucor rouxii spores in complex medium under aerobic conditions resulted in a very rapid transient increase in the level of soluble, low-K, CAMP phosphodiesterase. Maximum activity was reached after 2-4 min. Simultaneously, the CAMP content increased quickly, reproducing the profile exhibited by phosphodiesterase. Activation of the enzyme in vitro by a CAMP-dependent phosphorylation process showed that its stimulation was minimal at those times when its activity was highest. The correlation between cellular CAMP content, phosphodiesterase activity, and sensitivity of the enzyme to activation by phosphorylation suggests that the in vivo regulation of phosphodiesterase activity by CAMP-dependent phosphorylation may be the mechanism for shutoff of the CAMP signal elicited by glucose. activity by CAMP-dependent phosphorylation may be the mechanism for shutoff of the CAMP signal elicited by glucose. process showed that its stimulation was minimal at those times when its activity was highest. The correlation between cellular CAMP content, phosphodiesterase activity, and sensitivity of the enzyme to activation by phosphorylation suggests that the in vivo regulation of phosphodiesterase activity by CAMP-dependent phosphorylation may be the mechanism for shutoff of the CAMP signal elicited by glucose. activity by CAMP-dependent phosphorylation may be the mechanism for shutoff of the CAMP signal elicited by glucose. increase in the level of soluble, low-K, CAMP phosphodiesterase. Maximum activity was reached after 2-4 min. Simultaneously, the CAMP content increased quickly, reproducing the profile exhibited by phosphodiesterase. Activation of the enzyme in vitro by a CAMP-dependent phosphorylation process showed that its stimulation was minimal at those times when its activity was highest. The correlation between cellular CAMP content, phosphodiesterase activity, and sensitivity of the enzyme to activation by phosphorylation suggests that the in vivo regulation of phosphodiesterase activity by CAMP-dependent phosphorylation may be the mechanism for shutoff of the CAMP signal elicited by glucose. activity by CAMP-dependent phosphorylation may be the mechanism for shutoff of the CAMP signal elicited by glucose. process showed that its stimulation was minimal at those times when its activity was highest. The correlation between cellular CAMP content, phosphodiesterase activity, and sensitivity of the enzyme to activation by phosphorylation suggests that the in vivo regulation of phosphodiesterase activity by CAMP-dependent phosphorylation may be the mechanism for shutoff of the CAMP signal elicited by glucose. activity by CAMP-dependent phosphorylation may be the mechanism for shutoff of the CAMP signal elicited by glucose. spores in complex medium under aerobic conditions resulted in a very rapid transient increase in the level of soluble, low-K, CAMP phosphodiesterase. Maximum activity was reached after 2-4 min. Simultaneously, the CAMP content increased quickly, reproducing the profile exhibited by phosphodiesterase. Activation of the enzyme in vitro by a CAMP-dependent phosphorylation process showed that its stimulation was minimal at those times when its activity was highest. The correlation between cellular CAMP content, phosphodiesterase activity, and sensitivity of the enzyme to activation by phosphorylation suggests that the in vivo regulation of phosphodiesterase activity by CAMP-dependent phosphorylation may be the mechanism for shutoff of the CAMP signal elicited by glucose. activity by CAMP-dependent phosphorylation may be the mechanism for shutoff of the CAMP signal elicited by glucose. process showed that its stimulation was minimal at those times when its activity was highest. The correlation between cellular CAMP content, phosphodiesterase activity, and sensitivity of the enzyme to activation by phosphorylation suggests that the in vivo regulation of phosphodiesterase activity by CAMP-dependent phosphorylation may be the mechanism for shutoff of the CAMP signal elicited by glucose. activity by CAMP-dependent phosphorylation may be the mechanism for shutoff of the CAMP signal elicited by glucose. in vitro by a CAMP-dependent phosphorylation process showed that its stimulation was minimal at those times when its activity was highest. The correlation between cellular CAMP content, phosphodiesterase activity, and sensitivity of the enzyme to activation by phosphorylation suggests that the in vivo regulation of phosphodiesterase activity by CAMP-dependent phosphorylation may be the mechanism for shutoff of the CAMP signal elicited by glucose. activity by CAMP-dependent phosphorylation may be the mechanism for shutoff of the CAMP signal elicited by glucose. in vivo regulation of phosphodiesterase activity by CAMP-dependent phosphorylation may be the mechanism for shutoff of the CAMP signal elicited by glucose.