Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.4.1 (phosphodiesterase)
 18,767 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The intermediate lobe cells of pituitary gland synthesize and secrete bioactive peptides derived from proopiomelanocortin. In the present study, we investigated the effects of cholera toxin on the release of beta-endorphin (beta-Ep) from dispersed-intermediate lobe cells of rats. Cholera toxin added into culture medium, enhanced the intracellular accumulation of adenosine 3', 5'-monophosphate (cAMP) and the release of beta-endorphin like immunoreactive substance (beta-END-LIS). A positive dose-response relationship existed between the concentration of cholera toxin and the release of beta-END-LIS or the accumulation of cAMP. Maximal response was obtained with approximately 3 X 10(-10) M (in beta-END-LIS release) and 1 X 10(-9) M (in cAMP accumulation) concentration of cholera toxin. Incubation with cholera toxin (3 X 10(-8) M) resulted in a significant rise of cAMP accumulation after 20-30 min, and a 2-2.5 fold increase of beta-END-LIS release occurred after 60 min in comparison with nontreated cells. cAMP analog and phosphodiesterase inhibitor also increased the beta-END-LIS release). These results suggested the close relationship between cAMP accumulation and its biological effect (i.e. beta-END-LIS release).
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PMID:[The effects of cholera toxin in the release of beta-endorphin from the dispersed cells of the rat neurointermediate lobe]. 609 82

We have demonstrated the identity of calmodulin tightly bound to the particulate fractions of AH-66 hepatoma cells and normal liver with authentic soluble calmodulin and have compared the particulate calmodulin content of AH-66 cells with that of normal liver. Calmodulin bound to the particulate fractions of the hepatoma and normal liver cells was purified to electrophoretic homogeneity by a simple procedure which involves solubilization of the particulate fractions with LIS, extraction of the solubilized solution with 37.5% phenol, gel filtration, and affinity chromatography on Fluphenazine-Sepharose. There were no detectable differences between the particulate calmodulin thus purified and authentic soluble calmodulin of rat brain. The particulate calmodulin in the hepatoma and normal liver cells was assayed based on its ability to activate calmodulin-deficient phosphodiesterase after partial purification of calmodulin from the particulate fractions by solubilization with LIS and extraction with phenol as described above. In addition, the particulate calmodulin content in the hepatoma and normal liver cells was also measured after solubilization of the particulate fractions with Lubrol PX. The results obtained by these two different procedures indicate that calmodulin content in the particulate fraction as well as in the soluble fraction of the hepatoma is significantly higher than that in the corresponding fractions of normal liver.
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PMID:A simple procedure for the purification of calmodulin bound to membranes; calmodulin bound to the particulate fraction of AH-66 hepatoma ascites cells. 684 26