Isolated adrenal cortex cells: hypersensitivity to adrenocorticotropic hormone after hypophysectomy

Cells from the adrenals of hypophysectomized rats (up to 28 days after operation) require less adrenocorticotropic hormone to induce one-half maximal rate of production of 3',5'-adenosine monophosphate than do cells from the adrenals of intact rats. A corresponding increase in sensitivity is reflected in the steroidogenic response to adrenocorticotropic hormone up to 2 days after hypophysectomy.     

Cell communication, calcium ion, and cyclic adenosine monophosphate

The hypothesis advanced in this article requires further validation. Undoubtedly it will require modification as our knowledge of biochemical control increases. Nevertheless, it should prove useful in focusing attention on the apparent similarity in the response of a large number of specific cell types to particular stimuli. Emphasis has been placed on a few common and apparently key elements in these responses. It is recognized that other factors are undoubtedly involved. Specifically, the changes in membrane potentials indicate the likelihood of widespread changes in the properties of the cell membrane, for example, changes in Na(+) and K(+) transport and distribution. These aspects of cellular responses may eventually prove to be of equal or greater importance than those common aspects of the system already identified.     

Dibutyryl cyclic adenosine monophosphate stimulation of colcemid-inhibited axonal elongation

Adenosine 3',5'-monophosphate (cyclic AMP) and its dibutyryl derivative induce a variety of morphological changes, including those associated with in vitro axonal maturation. Established sensory ganglia treated with dibutyryl cyclic AMP show significant increases in average axonal length and number in comparison with controls; those treated with maintenance doses of Colcemid show no increases in either parameter; simultaneous treatment with both agents results in growth statistically similar to that produced by dibutyryl cyclic AMP alone. The data are consistent with our hypothesis that cyclic AMP promotes axonal elongation by stimulating microtubule assembly from a preexisting subunit pool.     

Pineal gland: dibutyryl cyclic adenosine monophosphate stimulation of labeled melatonin production

In organ cultures of intact rat pineal glands, N(6)O(2')-dibutyryl adenosine 3', 5'-monophosphate stimulates the conversion of tritiated trytophan to tritiated melatonin, as does L-norepinephrine. Potential sites of stimulation of melatonin production by dibutyryl cyclic adenosine monophosphate are discussed, based on observations that the dibutyryl analog also stimulates the conversion of serotonin labeled with carbon-14 to carbon-14-labeled melatonin without altering hydroxyin-dole-O-methyl transferase activity or intracellular accumulation of serotonin labeled with carbon-14.     

Phosphodiesterase in Dictyostelium discoideum and the chemotactic response to cyclic adenosine monophosphate

A phosphodiesterase with a low Michaelis constant for cyclic adenosine monophosphate was found in the membrane fraction of the cellular slime mold. This activity was highest during the aggregation stage. Enzyme with similar properties was also secreted by the cells. Dithiothreitol inhibited both enzymes and potentiated the cellular response to cyclic adenosine monophosphate.     

Oscillation of cyclic adenosine monophosphate concentration during the myocardial contraction cycle

The concentration of adenosine 3',5'-monophosphate (cyclic AMP) rises and falls during each myocardial contraction cycle. Peak concentrations of cyclic AMP precede peak development of systolic tension. Epinephrine alters the normal oscillation in myocardial cyclic AMP and increases both diastolic and systolic concentrations of the cyclic nucleotide. These transient changes in myocardial cyclic AMP indicate a potential role for cyclic AMP as a beat-to-beat regulator of myocardial contractility.     

Noradrenergic stimulation of cyclic adenosine monophosphate in rat Purkinje neurons: an immunocytochemical study

A specific immunofluorescent histochemical method for cyclic adenosine monophosphate was used to study rat cerebellum. After topical treatment with norepinephrine or stimulation of norepinephrine-containing afferents from locus coeruleus, there was a striking increase in the number of Purkinje cells with strong cyclic adenosine monophosphate reactivity. Other putative inhibitory transmitters had no significant effect on staining of Purkinje cells. The results provide the first histochemical support for the hypothesis that cyclic adenosine monophosphate can be generated postsynaptically in central neurons in response to noradrenergic stimuli.     

Cyclic adenosine monophosphate: function in photoreceptors

Inactivation of adenylate cyclase in outer segments of retinal photoreceptor cells is proportional to the bleaching of rhodopsin. Membranes of the outer segments also contain a particulate, light-insensitive phosphodiesterase of high specific activity. In electrophysiological experiments, application of cyclic adenosine monophosphate along with a methylxanthine mimics the effects of illumination on the photoreceptor cell of the compound eye of Limulus.     

Cyclic adenosine monophosphate and norepinephrine: effects on transmembrane properties of cerebellar Purkinje cells

Electrical properties of Purkinje cells were recorded by intracellular microelectrode during extracellular electrophoretic application of gamma aminobutyrate, norepinephrine, cyclic adenosine monophosphate, and dibutyryl cyclic adenosine monophosphate. All these substances hyperpolarized Purkinje cells. Transmembrane resistance decreased during gamma aminobutyrate hyperpolarization. In contrast, norepinephrine and the cyclic nucleotides generally elevated resistance. These results show that cyclic nucleotides mimic the unique effects of norepinephrine on the bioelectric properties of neuronal membranes.     

Cyclic adenosine monophosphate: possible mediator for norepinephrine effects on cerebellar Purkinje cells

Microelectrophoretic application of norepinephrine or cyclic adenosine monophosphate reduces the discharge frequency of Purkinje cells in the rat cerebellum. In contrast, other nucleotides accelerate the discharge rate of most units. Parenterally administered theophylline, which inhibits the hydrolysis of cyclic adenosine monophosphate enhances the effects of norepinephrine and cyclic adenosine monophosphate. Therefore, norepinephrine may be able to regulate Purkinje cells functionally by metabolic stimulation of cyclic adenosine monophosphate synthesis.     

Thyroid-stimulating hormone and prostaglandin E1 stimulation of cyclic 3',5'-adenosine monophosphate in thyroid slices

Thyroid-stimulating hormone increased the cyclic 3',5'-adenosine monophosphate concentration in dog thyroid slices during a 1-minute incubation period and produced a maximum effect soon thereafter. The elevation persisted for at least 30 minutes. The concentrations of the cyclic 3',5'-adenosine monophosphate increased as the TSH concentration was increased from 0.125 to 50 milliunits per milliliter. Prostaglandin E(1), which increases glucose oxidation in dog thyroid slices, also increased the concentration of cyclic 3',5'-adenosine monophosphate. Although sodium fluoride stimulates thyroid adenyl cyclase, it did not increase concentration of cyclic 3',5'-adenosine monophosphate. Carbamylcholine and menadiol sodium diphosphate augment glucose oxidation in dog thyroid slices but do not change concentrations of cyclic 3',5'-adenosine monophosphate.     

Cyclic adenosine monophosphate and hypertension in rats

Aortas from spontaneously hypertensive and stress hypertensive rats contained significantly lower intracellular concentrations of cyclic adenosine monophosphate than did their respective controls. Adenylate cyclase activity was normal but was less responsive to stimulation, while phosphodiesterase activity (especially the low Michaelis-Menten constant form) was significantly elevated. Human aortas contained two forms of phosphodiesterase that were similar to those in rat aortas.     

Pro-adrenocorticotropin/endorphin-derived peptides: coordinate action on adrenal steroidogenesis

A synthetic peptide, representing a portion of the 16K (16,000 dalton)-fragment sequence within the pro-adrenocorticotropin/endorphin precursor molecule, potentiates the steroidogenic action of the 1 to 24 portion of adrenocorticotropin [ACTH(1-24)] on the rat adrenal cortex. The peptide has 27 amino acid residues and consists of gamma-melanotropin with a carboxyl terminal extension. It affects both the inner and outer adrenocortical zones of hypophysectomized animals, as evidenced by a synergistic augmentation of corticosterone and aldosterone production, respectively. The peptide can be distinguished from adrenocorticotropin by its activation of cholesterol ester hydrolase and its failure to stimulate cholesterol side-chain cleavage.     

Gonadotropin-releasing hormone: regulation of adenosine 3',5'-monophosphate in ovarian granulosa cells

The antigonadal effects of gonadotropin-releasing hormone in ovarian granulosa cells are due to attenuation of the adenosine 3',5'-monophosphate (cyclic AMP) response to follicle-stimulating hormone. Agonists of gonadotropin-releasing hormone progressively inhibit adenylate cyclase and stimulate phosphodiesterase activities in cultured granulosa cells, indicating that blockade of gonadotropin action is attributable to the combined effects of decreased production and increased degradation of cyclic AMP.     

Cyclic adenosine monophosphate: andromimetic action on seminal vesicular enzymes

Administration of adenosine 3',5'-monophosphate with theophylline produced testosterone-like induction of hexokinase, phosphofructokinase, pyruvate kinase, and glucose-6-phosphate dehydrogenase in the seminal vesicles of both orchidectomized and immature rats. The N(6)-O(2)'-dibutyryl analog of this cyclic nucleotide produced greater increases in vesicular enzyme activities than those induced by the parent compound. The observed enhancement of the key glycolytic enzymes and of hexose monophosphate shunt dehydrogenase was significantly inhibited by actinomycin D and cycloheximide. The evidence indicates that cyclic adenosine monophosphate may be involved as an intermediary in the action of androgenic hormones on male accessory sex organs.     

Cyclic adenosine monophosphate phosphodiesterase in brain: effect on anxiety

Drugs that reduce anxiety may be mediated by cyclic adenosine monophosphate in the brain because (i) potent anxiety-reducing drugs are also potent inhibitors of brain phosphodiesterase activity; (ii) dibutyryl cyclic adenosine monophosphate has the ability to reduce anxiety; (iii) the methylxanthines show significant anxiety-reducing effects; (iv) theophylline and chlordiazepoxide produce additive anxiety-reducing activity; and (v) there is a significant correlation between the anxiety-reducing property of drugs and their ability to inhibit phosphodiesterase activity in the brain.     

Adenosine 3',5'-monophosphate, adrenocorticotropic hormone, and adrenocortical cytosol protein synthesis

In cultures of mouse adrenocortical tumor cells (Sato's minimal deviation Y-1 clonal strain), the acceleration of steroid biosynthesis after exposure to adrenocorticotropic hormone or cyclic adenosine 3',5'-monophosphate is maximum within 15 to 60 minutes and precedes any significant increase in labeling of protein with [4,5-(3)H]leucine. However, when cytosol proteins are separated by acrylamidegel electrophoresis, rapid changes in the amount and labeling of several protein fractions are evident in less than 30 minutes and are no longer evident within 60 minutes. This finding supports the proposal that the effects of tropic hormones and their intracellular mediators involve rapid selective effects on protein synthesis.     

Puromycin analogs: action of adrenocorticotropic hormone and the role of glycogen

The effect of the injection into rats of analogs of puromycin, 6-dimethylaminopurine, and the aminonucleoside of puromycin on the stimullation of steroidogenesis by adrenocorticotropic hormone was coin pared with that of puromycin and cycloheximide. This stimulation was blocked only by the antibiotics, which also inhibited adrenal protein synthesis. Glycogenolysis is not associated with the primary mechanism of the adrenocorticotropic hormone stimnulation of steroid hormone biosynthesis in rats.     

Isolated chromaffin cells from adrenal medulla contain primarily monoamine oxidase B

Cultured chromaffin cells from bovine adrenal medulla were found to contain primarily the B form of monoamine oxidase. This monoamine oxidase B enzyme was somewhat distinct from B enzymes from other sources, in that noradrenaline was a much poorer substrate than serotonin. Nonetheless, studies with selective inhibitors of the A form (clorgyline) and the B form [(-)-deprenyl] confirmed that chromaffin cell monoamine oxidase was the B form. The observation that chromaffin cell monoamine oxidase has poor affinity for catecholamines is consistent with physiological needs that require the cell to synthesize and store large amounts of catecholamines.