Prostaglandylinositol cyclic phosphate, the natural antagonist of cyclic AMP

IUBMB Life ◽  
2020 ◽  
Vol 72 (11) ◽  
pp. 2282-2289
Author(s):  
Heinrich K. Wasner
Keyword(s):  
Cyclic Amp ◽  
Cyclic Phosphate

Degradation of the Cyclic AMP Antagonist Prostaglandylinositol Cyclic Phosphate (Cyclic PIP) by Dephosphorylation

1999 ◽  
Vol 380 (1) ◽  
Author(s):  
A. Kassner ◽  
M. Lessmann ◽  
H.K. Wasner
Keyword(s):  
Cyclic Amp ◽  
Inositol Phosphate ◽  
Prostaglandin E ◽  
Rat Tissues ◽  
Degrading Enzyme ◽  
Cyclic Phosphate ◽  
The Difference ◽  
Synthesis And Degradation

AbstractThe cAMP antagonist, prostaglandylinositol cyclic phosphate (cyclic PIP), is synthesized from prostaglandin E and activated inositol phosphate. From various tissues only that amount of cyclic PIP can be isolated that constitutes the difference between synthesis and degradation. In order to overcome this drawback, the cyclic PIP degrading enzyme or enzymes had to be characterized prior to searching for inhibitors. Cyclic PIP degrading activities have been found in all rat tissues tested, and are lowest in brain (380 pmol × min

Properties of an Adenosine Cyclic Phosphates Degrading Enzyme in Nicotiana tabacum L. var. Xanthi

1977 ◽  
Vol 32 (3-4) ◽  
pp. 297-300 ◽  
Author(s):  
Axel Brennicke ◽  
Hans Dieter Frey
Keyword(s):  
Nicotiana Tabacum ◽  
Cyclic Amp ◽  
Inorganic Phosphate ◽  
Strong Inhibitor ◽  
Degrading Enzyme ◽  
Nicotiana Tabacum L ◽  
Messenger System ◽  
Cyclic Phosphate ◽  
Act Up ◽  
Cyclic Phosphates

Abstract This work describes an enzyme which degrades adenosine 3′:5′-cyclic phosphate (3′ :5′-cyclic-AMP) and adenosine 2′:3′-cyclic phosphate (2′:3′-cyclic-AMP). The reaction pro­ ducts are 3′-AMP and 5′-AMP in case of 3′:5′-cyclic-AMP, 2′-AMP and 3′-AMP when 2′:3′-cyclic-AMP is given as substrate. Inorganic phosphate acts as a strong inhibitor, whereas theophyllin does not act up to a concentration of 10-3 m . Probably the adenosine cyclic phosphates degrading enzyme has no function in a ‘second messenger’ system with 3′:5′-cyclic-AMP.

scholarly journals rac-Glycerol 1:2-cyclic phosphate 2-phosphodiesterase, a new soluble phosphodiesterase of mammalian tissues

1978 ◽  
Vol 173 (2) ◽  
pp. 579-589 ◽  
Author(s):  
N Clarke ◽  
R M C Dawson
Keyword(s):  
Molecular Weight ◽  
Cyclic Amp ◽  
Gel Filtration ◽  
Reducing Agents ◽  
Ph Optimum ◽  
Acetone Precipitation ◽  
Nitrophenyl Phosphate ◽  
Mammalian Tissues ◽  
Cyclic Phosphate

1. A soluble phosphodiesterase is present in mammalian tissues which rapidly hydrolyses enantiomorphs of rac-glycerol 1:2-cyclic phosphate, producing rac-glycerol 1-phosphate. 2. The enzyme has been purified up to 1700-fold by a combination of acetone precipitation and chromatography on DEAE-Sephadex A-50, Sephadex G-150 and hydroxyapatite. 3. The Km with glycerol cyclic phosphate as substrate is 7.2 mM, and the pH optimum broad (6.9–7.5). The molecular weight (by gel filtration) of the enzyme is approx. 35500. 4. The phosphodiesterase has no requirement for Ca2+ or Mg2+, but is stimulated by reducing agents (cysteine, dithiothreitol) and Fe2+. 5. The purified phosphodiesterase preparation also hydrolysed 3′:5′-cyclic AMP, producing 5′-AMP exclusively, and 2′:3′-cyclic AMP, forming 3′-AMP and 2′-AMP in the ratio 7:3. Bis-(p-nitrophenyl) phosphate was slowly hydrolysed, but other phosphodiesters tested were not attacked. 6. The phosphodiesterase is inhibited by theophylline and o-phenanthroline. It is inhibited by Pi and by a variety of phosphomonoesters, of which certain aromatic primary phosphates are particularly effective.

Prostaglandin Deficiency Promotes Sensitization of Adenylyl Cyclase

2000 ◽  
Vol 381 (5-6) ◽  
pp. 525-529 ◽  
Author(s):  
S. Weber ◽  
H. Lemoine ◽  
H.K. Wasner
Keyword(s):  
Cyclic Amp ◽  
Adenylyl Cyclase ◽  
Adrenergic Receptors ◽  
Type Ii Diabetes ◽  
Plasma Membranes ◽  
Male Rats ◽  
Inhibition Of Prostaglandin Synthesis ◽  
Cyclic Phosphate ◽  
Stimulation Of ◽  
Cyclic Amp Synthesis

Abstract Inhibition of prostaglandin synthesis by the drug indomethacin suppresses the synthesis of the cyclic AMP antagonist, prostaglandylinositol cyclic phosphate (cyclic PIP), and leads to a metabolic state comparable to type II diabetes. It was of interest whether prostaglandindeficiency likewise causes sensitization of adenylyl cyclase, as this has been reported for the diabetic state. In liver plasma membranes of indomethacintreated male rats, basal and forskolinstimulated cyclic AMP synthesis remained unchanged when compared to untreated control rats. In control rats, stimulation of cyclic AMP synthesis by fluoride (2.2-fold) or glucagon (3.5-fold) was much lower than stimulation by forskolin (6.6-fold). In contrast, in indomethacin treated rats, stimulation of cAMP synthesis by fluoride (4.6-fold) or glucagon (5.2-fold) nearly matched the stimulation by forskolin (6.4-fold). The level of α[1]adrenergic receptors was slightly reduced, from 450 to 320 fmol/mg protein, by the indomethacin treatment. Independent of the treatment by indomethacin, stimulation of cyclic AMP synthesis by adrenaline failed, in agreement with the low density of adrenergic βreceptors. In conclusion, PGE deficiency sensitizes adenylyl cyclase in rat liver for G proteincoupled receptors (glucagon) and also for fluoride.

Method for the Selective 2′-O-Substitution of Nucleosides

1980 ◽  
Vol 35 (1-2) ◽  
pp. 163-167 ◽  
Author(s):  
C. Sauer ◽  
U. Schwabe
Keyword(s):  
Cyclic Amp ◽  
Phosphate Group ◽  
New Method ◽  
Protecting Groups ◽  
Step Procedure ◽  
One Step ◽  
Cyclic Phosphate ◽  
Neutral Conditions

Abstract This paper presents a new method for selective reactions of predetermined sugar hydroxyls of nucleosides. Suc-cinylated nucleosides were investigated as examples for the use of the cyclic phosphate group for protecting purposes. Starting from cyclic AMP the 2′-O-group was selectively succinylated yielding 93% 2′-O-succinyl cyclic AMP. The cyclic phosphate was enzymatically dephosphorylated in a one step procedure under neutral conditions and 2′-O -succinyl adenosine containing a small amount of the 3′-O-isomer was produced in 91% yield. When establishment of equilibrium of the 2′-O-and 3′-O-isomers was allowed, 54% yield of crystallized 3′-O-succinyl adenosine was prod­ uced. The results suggest that the easily accessible cyclic monophosphates are good protecting groups for the pro­ duction of nucleoside derivatives, especially at the 2′-O-position under neutral conditions.

Effects of Angiotensin II on Adenylcyclase Activity, Phosphodiesterase Activity and on the Level of Cyclic AMP in Rat Uterus

1973 ◽  
Vol 45 (s1) ◽  
pp. 247s-250s
Author(s):  
G. Anglès D'Auriac ◽  
P. Meyer
Keyword(s):  
Angiotensin Ii ◽  
Cyclic Amp ◽  
Enzyme Activities ◽  
Phosphodiesterase Activity ◽  
Rat Uterus ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Cyclic Phosphate ◽  
Intracellular Concentrations

1. Intracellular concentrations of adenosine 3′: 5′-cyclic phosphate (cyclic AMP) and activities of adenylcyclase and phosphodiesterase were determined in oestrogen-pretreated rat uteri during exposure to different concentrations of angiotensin II. 2. No significant variations in cyclic AMP or in the enzyme activities were observed at concentrations of angiotensin inducing significant contractions. 3. It is concluded that in rat uterus, the process of excitation-contraction coupling triggered by angiotensin is not mediated by variations in intracellular levels of cyclic AMP.

Cytochemical Evidence for Presynatic β-Adrenergic Regulation of Secretion in the Developing Rat Submandibular Gland

1977 ◽  
Vol 35 ◽  
pp. 430-431
Author(s):  
L.S. Cutler
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Submandibular Gland ◽  
Neonatal Rat ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Parotid Glands ◽  
Adrenergic Agonist ◽  
Rat Submandibular Gland

Many studies previously have shown that the B-adrenergic agonist isoproterenol and the a-adrenergic agonist norepinephrine will stimulate secretion by the adult rat submandibular (SMG) and parotid glands. Recent data from several laboratories indicates that adrenergic agonists bind to specific receptors on the secretory cell surface and stimulate membrane associated adenylate cyclase activity which generates cyclic AMP. The production of cyclic AMP apparently initiates a cascade of events which culminates in exocytosis. During recent studies in our laboratory it was observed that the adenylate cyclase activity in plasma membrane fractions derived from the prenatal and early neonatal rat submandibular gland was retractile to stimulation by isoproterenol but was stimulated by norepinephrine. In addition, in vitro secretion studies indicated that these prenatal and neonatal glands would not secrete peroxidase in response to isoproterenol but would secrete in response to norepinephrine. In contrast to these in vitro observations, it has been shown that the injection of isoproterenol into the living newborn rat results in secretion of peroxidase by the SMG (1).

Elucidating cyclic AMP signaling in subcellular domains with optogenetic tools and fluorescent biosensors

2019 ◽  
Vol 47 (6) ◽  
pp. 1733-1747 ◽  
Author(s):  
Christina Klausen ◽  
Fabian Kaiser ◽  
Birthe Stüven ◽  
Jan N. Hansen ◽  
Dagmar Wachten
Keyword(s):  
Cyclic Amp ◽  
Adenosine Monophosphate ◽  
Adenylyl Cyclases ◽  
Temporal Precision ◽  
Fluorescent Biosensors ◽  
Subcellular Domains ◽  
Spatio Temporal ◽  
Hydrolysis Of ◽  
Shed Light ◽  
Cyclic Amp Signaling

The second messenger 3′,5′-cyclic nucleoside adenosine monophosphate (cAMP) plays a key role in signal transduction across prokaryotes and eukaryotes. Cyclic AMP signaling is compartmentalized into microdomains to fulfil specific functions. To define the function of cAMP within these microdomains, signaling needs to be analyzed with spatio-temporal precision. To this end, optogenetic approaches and genetically encoded fluorescent biosensors are particularly well suited. Synthesis and hydrolysis of cAMP can be directly manipulated by photoactivated adenylyl cyclases (PACs) and light-regulated phosphodiesterases (PDEs), respectively. In addition, many biosensors have been designed to spatially and temporarily resolve cAMP dynamics in the cell. This review provides an overview about optogenetic tools and biosensors to shed light on the subcellular organization of cAMP signaling.

Decreased cyclic AMP in the epidermis of lesions of psoriasis

1972 ◽  
Vol 105 (5) ◽  
pp. 695-701 ◽  
Author(s):  
J. J. Voorhees
Keyword(s):  
Cyclic Amp
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