Effect of cyclic AMP on hexokinase and glucose-6-phosphate dehydrogenase isozymes in albino rat tissues

1981 ◽  
Vol 92 (1) ◽  
pp. 916-918
Author(s):  
L. E. Panin ◽  
G. S. Russkikh ◽  
E. �. Voitsekhovskaya
Keyword(s):  
Cyclic Amp ◽  
Rat Tissues ◽  
Albino Rat ◽  
Glucose 6 Phosphate Dehydrogenase

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

scholarly journals Effect of adrenaline and phorbol myristate acetate or bacterial lipopolysaccharide on stimulation of pathways of macrophage glucose, glutamine and O2 metabolism. Evidence for cyclic AMP-dependent protein kinase mediated inhibition of glucose-6-phosphate dehydrogenase and activation of NADP+-dependent ‘malic’ enzyme

1995 ◽  
Vol 310 (2) ◽  
pp. 709-714 ◽  
Author(s):  
L F B P Costa Rosa ◽  
R Curi ◽  
C Murphy ◽  
P Newsholme
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Pentose Phosphate Pathway ◽  
Malic Enzyme ◽  
Pentose Phosphate ◽  
Glutamine Metabolism ◽  
Dependent Protein Kinase ◽  
Macrophage Activity ◽  
Dependent Protein ◽  
Glucose 6 Phosphate Dehydrogenase

Adrenaline has recently been shown to stimulate both glucose metabolism and H2O2 release by macrophages but the activity of the key pentose phosphate pathway enzyme, glucose-6-phosphate dehydrogenase (which generates the NADPH crucial for the reduction of molecular oxygen), was reduced under these conditions [Costa Rosa, Safi, Cury and Curi (1992) Biochem. Pharmacol. 44, 2235-2241]. We report here that adrenaline activates another NADPH-producing enzyme, NADP(+)-dependent ‘malic’ enzyme, while also inhibiting glucose-6-phosphate dehydrogenase, via cyclic AMP-dependent protein kinase (PKA) activation. Regulation of glucose-6-phosphate dehydrogenase activity by PKA has not been reported elsewhere. The sparing of some glucose from pentose phosphate pathway consumption may be important in the provision of glycerol 3-phosphate which in the macrophage may be required for new phospholipid synthesis. Glutamine oxidation was also stimulated by adrenaline thus providing increased substrate (malate) for NADP(+)-dependent ‘malic’ enzyme and therefore shifting some of the burden of NADPH production from glucose to glutamine metabolism. We also report a novel synergistic effect of adrenaline and some bacterial products and/or gamma-interferon in stimulating secretory and metabolic pathways in macrophages which may be a part of a larger network of signals that lead to enhanced macrophage activity.

The effect of sarcolysin on the 24-hour periodicity of mitoses in some albino rat tissues

1964 ◽  
Vol 57 (3) ◽  
pp. 346-349
Author(s):  
V. N. Dobrokhotov ◽  
I. V. Markelova ◽  
L. V. Skolova ◽  
T. B. Timashkevich ◽  
R. I. Nikanorova ◽  
...  
Keyword(s):  
Rat Tissues ◽  
Albino Rat

scholarly journals A reappraisal of the effects of adenosine 3′:5′-cyclic monophosphate on the function and morphology of the rat prostate gland

1973 ◽  
Vol 134 (1) ◽  
pp. 129-142 ◽  
Author(s):  
F. R. Mangan ◽  
A. E. Pegg ◽  
W. I. P. Mainwaring
Keyword(s):  
Cyclic Amp ◽  
Prostate Gland ◽  
Hormonal Treatment ◽  
Supernatant Fraction ◽  
Metabolizing Enzymes ◽  
Biochemical Processes ◽  
Rat Prostate ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Stimulation Of

1. A comparison was made of the binding of 5α-dihydrotestosterone (17β-hydroxy-5α-androstan-3-one) and cyclic AMP in the rat prostate gland. Distinct binding mechanisms exist for these compounds, and cyclic AMP cannot serve as a competitor for the 5α-dihydrotestosterone-binding sites and vice versa. In contrast with the results obtained with 5α-dihydrotestosterone, very small amounts of cyclic AMP are retained in nuclear chromatin and the overall binding of this cyclic nucleotide is not markedly affected by castration. 2. Androgenic stimulation does not lead to major increases in the adenylate cyclase activities associated with any subcellular fraction of the prostate gland. Accordingly, changes in the concentration of cyclic AMP in the prostate gland after hormonal treatment are likely to be small, but these were not measured directly. 3. When administered to whole animals in vivo, small amounts of non-degraded cyclic AMP are found in the prostate gland but sufficient to promote an activation of certain carbohydrate-metabolizing enzymes in the cell supernatant fraction. The stimulatory effects of cyclic AMP were not evident with cytoplasmic enzymes engaged in polyamine synthesis or nuclear RNA polymerases. These latter enzymes were stimulated solely by the administration of testosterone. 4. By making use of antiandrogens, a distinction can be drawn between the biochemical responses attributable to the binding of 5α-dihydrotestosterone but not of cyclic AMP. Evidence is presented to suggest that the stimulation of RNA polymerase, ornithine decarboxylase and S-adenosyl-l-methionine decarboxylase is a consequence of the selective binding of 5α-dihydrotestosterone. Only the stimulation of glucose 6-phosphate dehydrogenase can be attributed to cyclic AMP or other metabolites of testosterone. 5. Overall, this study indicates that the formation of cyclic AMP is not a major feature of the androgenic response and affects only a restricted number of biochemical processes. Certainly, cyclic AMP cannot be considered as interchangeable with testosterone and its metabolites in the control of the function of the prostate gland. This difference is additionally emphasized by the failure of cyclic AMP to restore the morphology of the prostate gland in castrated animals; morphological restoration only follows the administration of androgens.

scholarly journals Extraction of Lipopeptide from Bacillus subtilis and Histological Study on Albino Rats Tissue

2021 ◽  
Vol 8 (5) ◽  
pp. 183-186
Author(s):  
Ghofran Filaih Abd AL-Hussan ◽  
Waleed Jaleel Abed AL-Kelaby ◽  
Ali Yas Khudhair AL-Ameri
Keyword(s):  
Bacillus Subtilis ◽  
Histological Study ◽  
Control Treatment ◽  
Albino Rats ◽  
Human Consumption ◽  
Rat Tissues ◽  
Albino Rat ◽  
Laboratory Rats ◽  
Nutrient Agar Medium ◽  
Kidney Liver

Introduction and Aim: An extract of the lipopeptides from Bacillus subtilis has been found to be extremely useful in antimicrobial applications. Specifically, the goal of this study is to manufacture lipopeptide and assess the safety of this substance on the tissues and organs of laboratory rats. Materials and Methods: Bacillus subtilis bacteria were isolated and identified at the postgraduate microbiology laboratory in the department of biology at Kufa University's College of Science. The bacteria became active after 24 hours of growth in the brain broth infusion broth medium. In order to determine the bacteria's capacity to produce lipopeptide. On nutrient agar medium, a quantity of lipopeptide was synthesized utilizing HCL for sediment, yielding an estimated amount of 1.5 gm during a two-month period, then the product was partially purified and lyophilized using a lyophilizer. For one week, the lipopeptide was administered on albino rat tissues such as the kidney, liver, spleen, and small intestine to determine its safety. Results: The results showed no damage or any changes on tested tissues compared with control treatment and all of the previously mentioned organ tissues were completely intact and this is evidence of the safety of the lipopeptide extract for use. Conclusions: It was discovered that lipopeptide had no effect on the organs that were utilized in the experiment and that it is safe for human consumption.

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