scholarly journals The effects of added purines on urate and purine synthesis de novo by isolated chick liver, kidney and lymphoid cells

1976 ◽  
Vol 158 (3) ◽  
pp. 549-556 ◽  
Author(s):  
P Badenoch-Jones ◽  
P J Buttery
Keyword(s):  
De Novo ◽  
Cell Types ◽  
Liver Cells ◽  
Lymphoid Cells ◽  
Kidney Cells ◽  
Purine Synthesis ◽  
Liver And Kidney ◽  
Stimulation Of

1. Isolated chick lymphoid cells, together with isolated chick liver and kidney cells, incorporate [1-14C]glycine or [14C]formate into urate. 2. Of the cell types used, bursal cells incorporate 14C into urate at the fastest rate, although the output of total urate by bursal cells is only 10% that of liver cells. 3. When suspended in Eagle's medium the incorporation of 14C into urate is inhibited by adenine and guanine up to 1 mM. In contrast, the addition of 1 mM-AMP or -GMP results in a relatively large stimulation of this incorporation. 4. Added adenine is rapidly taken up by liver cells and then released in an unmetabolized form; AMP is taken up more slowly and is rapidly metabolized. The metabolites (possibly including adenine) are then released. 5. Intracellular liver 5-phosphoribosyl 1-pyrophosphate is approx. 0.7mM and remains constant or falls slightly during a 3 h incubation of the cells. 6. The addition of adenine or guanine, AMP or GMP, does not alter liver intracellular 5-phosphoribosyl 1-pyrophosphate concentrations. Added 5-phosphoribosyl 1-pyrophosphate is not taken up by liver cells. 7. The results are discussed in the context of the control of urate and purine synthesis de novo in the chick.

scholarly journals The effects of adenine nucleotides and guanine nucleotides on urate synthesis de novo by isolated chick liver and kidney cells

1975 ◽  
Vol 148 (3) ◽  
pp. 599-601 ◽  
Author(s):  
P Badenoch-Jones ◽  
P J Buttery
Keyword(s):  
De Novo ◽  
Adenine Nucleotides ◽  
Liver Cells ◽  
Guanine Nucleotides ◽  
Kidney Cells ◽  
Liver And Kidney

Isolated chick liver and kidney cells produce urate de novo from glycine, and this is partially inhibited by 1 mm-AMP and by 1 mm-GMP in liver cells but not in kidney cells. Azaserine fully inhibits this synthesis de novo, but attempts to isolate formylglycine amide ribonucleotide from azaserine-blocked cells were unsuccessful.

Effects of glycerol and fructose on purine synthesis de novo and on PP-ribose-P availability in rat liver cells

1982 ◽  
Vol 60 (12) ◽  
pp. 1109-1115
Author(s):  
Christine Des Rosiers ◽  
Marcel Lalanne ◽  
Joan Willemot
Keyword(s):  
Rat Liver ◽  
De Novo ◽  
Normal Values ◽  
Initial Period ◽  
Liver Cells ◽  
P Availability ◽  
Isolated Rat Liver ◽  
Purine Synthesis ◽  
Initial Decrease ◽  
Rat Liver Cells

Incubation of freshly isolated rat liver cells with glycerol resulted in an initial decrease, followed by an increase in purine synthesis de novo and in PP-ribose-P availability. The magnitude of these effects was dependent on the concentration of glycerol; as it increased, the initial period of latency or inhibition was prolonged, and the extent of the subsequent stimulation was greater. The intracellular Pi concentration and the [14C]ATP/[14C]ADP ratio were also initially decreased in these cells, and they too returned subsequently to normal values. All these changes were similar to those induced by fructose under the same conditions. The increase in PP-ribose-P availability always preceded that in purine synthesis de novo, indicating that, under most circumstances, PP-ribose-P availability is limiting for purine synthesis de novo. Finally, PP-ribose-P synthesis in these cells varied in parallel with the intracellular Pi concentration and with the ATP/ADP and ATP/AMP ratios.

scholarly journals Prostaglandin D2 mediates the stimulation of glycogenolysis in the liver by phorbol ester

1988 ◽  
Vol 250 (1) ◽  
pp. 77-80 ◽  
Author(s):  
E Casteleijn ◽  
J Kuiper ◽  
H C J Van Rooij ◽  
J A A M Kamps ◽  
J F Koster ◽  
...  
Keyword(s):  
Phorbol Ester ◽  
Cell Types ◽  
Liver Cells ◽  
Prostaglandin D2 ◽  
Perfused Liver ◽  
Glucose Homoeostasis ◽  
Parenchymal Liver Cell ◽  
Parenchymal Liver ◽  
Complex Regulation ◽  
Stimulation Of

The tumour-promoting phorbol ester, phorbol 12-myristate 13-acetate (PMA), when added to the perfused liver, stimulates glycogenolysis 2-fold. This stimulation is not seen when aspirin is present in the perfusion medium. In isolated parenchymal liver cells. PMA is not able to stimulate glycogenolysis, suggesting that its effect on glycogenolysis might be indirect and depends on the presence of the non-parenchymal liver cell types. To test the possible operation of an indirect mechanism, we measured the amount of prostaglandin (PG) D2 in liver perfusates. After addition of PMA, the amount of PGD2 is doubled, in parallel with the increase in glycogenolysis. Glycogenolysis in both isolated parenchymal liver cells and perfused liver could be stimulated by the addition of PGD2. Our data indicate that stimulation of glycogenolysis in the liver by PMA may be mediated by non-parenchymal liver cells, which produce PGD2 in response to PMA. Subsequently PGD2 activates glycogenolysis in the parenchymal liver cells. The intercellular communication inside the liver in response to PMA adds a new mechanism to the complex regulation of glucose homoeostasis by the liver.

Stimulation of human purine synthesis de novo by fructose infusion

Metabolism ◽  
1975 ◽  
Vol 24 (7) ◽  
pp. 861-869 ◽  
Author(s):  
Kari O. Raivio ◽  
Michael A. Becker ◽  
Laurence J. Meyer ◽  
Martin L. Greene ◽  
George Nuki ◽  
...  
Keyword(s):  
De Novo ◽  
Purine Synthesis ◽  
Stimulation Of

scholarly journals DNA Damage and Glutathione Peroxidase Activity in Liver and Kidney Cells in Wistar Rats Exposed to Terbuthylazine (TERB) for 28 Consecutive Days

2020 ◽  
Author(s):  
Vilena Kašuba ◽  
Vedran Micek ◽  
Alica Pizent ◽  
Blanka Tariba Lovaković ◽  
Davor Želježić ◽  
...  
Keyword(s):  
Dna Damage ◽  
Glutathione Peroxidase ◽  
Tail Length ◽  
Liver Cells ◽  
Male Rats ◽  
Kidney Cells ◽  
Low Doses ◽  
Parenchymal Liver ◽  
Liver And Kidney ◽  
Parenchymal Cells

The potential of low doses of the chloro-triazine herbicide terbuthylazine to induce DNA damage and impair activity of glutathione peroxidase (GPx) was evaluated in kidney and parenchymal and non-parenchymal liver cells of adult male rats. In a 28-day study, terbuthylazine was applied daily by oral gavage at doses: 0.004, 0.4 and 2.29 mg/kg bw/day. Tail Intensity (T Int) and Tail Length (TL) were used as descriptors of DNA damage. In the kidney, Tail Int was significantly different in all treated groups, while TL was different in 0.4 and 2.29 mg/kg bw/day groups, compared to controls. Significant differences in TL were recorded in parenchymal and non-parenchymal liver cells of all treated groups. Tail Int was significantly different from controls in non-parenchymal liver cells at all applied doses and in parenchymal cells at terbuthylazine doses of 0.004 and 2.29 mg/kg bw/day. A significant increase in GPx activity was observed only in the kidney at doses 0.4 and 2.29 mg/kg bw/day compared to the controls indicating its possible role in the protection of kidney from free radicals. It appears that repeated exposure to low doses of terbuthylazine could cause DNA instability in kidney cells and in parenchymal and non-parenchymal liver cells in rats.

Purine synthesis de novo and its regulation in rat hepatocytes

1980 ◽  
Vol 58 (8) ◽  
pp. 599-606 ◽  
Author(s):  
Christine Des Rosiers ◽  
Marcel Lalanne ◽  
Joan Willemot
Keyword(s):  
Pentose Phosphate Pathway ◽  
De Novo ◽  
Rat Hepatocytes ◽  
Isolated Hepatocytes ◽  
Pentose Phosphate ◽  
Male Rats ◽  
P Availability ◽  
Prolonged Incubation ◽  
Purine Synthesis ◽  
Stimulation Of

Purine synthesis de novo and its regulation were studied in freshly isolated hepatocytes from fed adult male rats. These cells incorporated [14C]formate mainly into purine ribonucleotides. The immediate effect of increasing the concentration of inorganic phosphate in the incubation medium was an increase in 5-phosphoribosyl 1-pyrophosphate (PP-ribose-P) availability and a stimulation of purine synthesis de novo. However, prolonged incubation of cells in 25 mM phosphate resulted in a decreased PP-ribose-P availability and purine synthesis de novo. Methylene blue and phenazine methosulfate decreased PP-ribose-P availability and purine synthesis de novo although they stimulated considerably the pentose phosphate pathway. In contrast, epinephrine and glucagon increased significantly PP-ribose-P availability and purine synthesis de novo, but they did not change the activity of the pentose phosphate pathway. These results show a relationship between PP-ribose-P availability and purine synthesis de novo in rat hepatocytes. They emphasize the complexity of the regulation of PP-ribose-P availability.

Antiparasitic Treatment of Patients with P. falciparum Malaria Reduces the Ability of Patient Serum to Induce Tissue Factor by Decreasing NF-κB Activation

1995 ◽  
Vol 73 (01) ◽  
pp. 039-048 ◽  
Author(s):  
A Bierhaus ◽  
Ch J Hemmer ◽  
N Mackman ◽  
R Kutob ◽  
R Ziegler ◽  
...  
Keyword(s):  
Tissue Factor ◽  
Falciparum Malaria ◽  
De Novo ◽  
Neutralizing Antibody ◽  
Mobility Shift ◽  
Before And After ◽  
Tf Gene ◽  
Electrophoretic Mobility Shift Assays ◽  
Antiparasitic Treatment ◽  
Stimulation Of

SummarySerum from patients with P. falciparum malaria at day 1 (pretherapy) induces tissue factor (TF) in cultured endothelial cells. TF induction depends on de novo transcription as shown in Nuclear Run On assays. Electrophoretic mobility shift assays demonstrated binding of AP-1 and NF- κB/Rel proteins to their recognition sites in the TF promotor. After therapy (day 28), stimulation of TF antigen by patient serum is reduced by 70%. When serum obtained before and after therapy was compared, a decrease of NF-κB activation was evident. Activation of NF-κB-like proteins was in part dependent on TNFα in patient serum, since a TNFα neutralizing antibody reduced induction of TF transcription and translation and induction of NF-κB-like proteins. Induction of TF activity was suppressed by pDTC, an inhibitor of NF-κB activation. When different promotor constructs of the TF gene were tested, induction was dependent upon the presence of the intact NF-κB-like binding site in the TF promotor. A mutant with deleted NF-κB, but intact AP-1 sites was not inducible. Mutation of the AP-1 sites did not prevent induction, but reduced inducibility by pretherapy serum. Therefore, NF-κB/Rel proteins are responsible for induction of TF transcription by pretherapy serum, but AP-1 is needed for highest inducibility. The effect of antiparasitic therapy on the induction of TF by serum from patients with complicated P. falciparum malaria is dependent on a therapy-mediated loss of activation of NF-κB-like proteins in post-treatment patient serum.

Preparation, spectral properties and biological activities of 5-bromo-6-methyl-2'-deoxyuridine and 5-iodo-6-methyl-2'-deoxyuridine

1980 ◽  
Vol 45 (8) ◽  
pp. 2364-2370 ◽  
Author(s):  
Antonín Holý ◽  
Erik De Clercq
Keyword(s):  
Antiviral Activity ◽  
Spectral Properties ◽  
De Novo ◽  
Biological Activities ◽  
Rabbit Kidney ◽  
Kidney Cells ◽  
Cd Spectra ◽  
Methyl Derivatives ◽  
Primary Rabbit

Reaction of 3',5'-di-O-benzoyl-6-methyl-2'-deoxyuridine (IIa) with elementary bromine or iodine afforded 5-halogeno derivatives IIc and IId which on methanolysis gave 5-bromo-6-methyl-2'-deoxyurine (Ic) and 5-iodo-6-methyl-2'-deoxyurine (Id), respectively. The CD spectra of Ic, Id and 6-methyl-2'-deoxyuridine (Ia) are compared and discussed with regard to determination of the nucleoside conformation. Unlike 5-bromo- and 5-iodo-2'-deoxyuridine, the 6-methyl derivatives Ic and Id exhibit neither antibacterial nor antiviral activity. Nor do they exert any antimetabolic effect on the de novo DNA synthesis in primary rabbit kidney cells.

scholarly journals Selective deletion of SHIP-1 in hematopoietic cells in mice leads to severe lung inflammation involving ILC2 cells

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Xujun Ye ◽  
Fengrui Zhang ◽  
Li Zhou ◽  
Yadong Wei ◽  
Li Zhang ◽  
...  
Keyword(s):  
Lung Inflammation ◽  
Airway Remodeling ◽  
Pulmonary Inflammation ◽  
Hematopoietic Cells ◽  
Cell Lineage ◽  
Allergic Inflammation ◽  
Cell Types ◽  
Lymphoid Cells ◽  
Whole Body

AbstractSrc homology 2 domain–containing inositol 5-phosphatase 1 (SHIP-1) regulates the intracellular levels of phosphotidylinositol-3, 4, 5-trisphosphate, a phosphoinositide 3–kinase (PI3K) product. Emerging evidence suggests that the PI3K pathway is involved in allergic inflammation in the lung. Germline or induced whole-body deletion of SHIP-1 in mice led to spontaneous type 2-dominated pulmonary inflammation, demonstrating that SHIP-1 is essential for lung homeostasis. However, the mechanisms by which SHIP-1 regulates lung inflammation and the responsible cell types are still unclear. Deletion of SHIP-1 selectively in B cells, T cells, dendritic cells (DC) or macrophages did not lead to spontaneous allergic inflammation in mice, suggesting that innate immune cells, particularly group 2 innate lymphoid cells (ILC2 cells) may play an important role in this process. We tested this idea using mice with deletion of SHIP-1 in the hematopoietic cell lineage and examined the changes in ILC2 cells. Conditional deletion of SHIP-1 in hematopoietic cells in Tek-Cre/SHIP-1 mice resulted in spontaneous pulmonary inflammation with features of type 2 immune responses and airway remodeling like those seen in mice with global deletion of SHIP-1. Furthermore, when compared to wild-type control mice, Tek-Cre/SHIP-1 mice displayed a significant increase in the number of IL-5/IL-13 producing ILC2 cells in the lung at baseline and after stimulation by allergen Papain. These findings provide some hints that PI3K signaling may play a role in ILC2 cell development at baseline and in response to allergen stimulation. SHIP-1 is required for maintaining lung homeostasis potentially by restraining ILC2 cells and type 2 inflammation.

Sign in / Sign up

Export Citation Format

Share Document