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.

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 Purine salvage networks in Giardia lamblia.

1983 ◽  
Vol 158 (5) ◽  
pp. 1703-1712 ◽  
Author(s):  
C C Wang ◽  
S Aldritt
Keyword(s):  
Giardia Lamblia ◽  
De Novo ◽  
Adenine Nucleotides ◽  
Guanine Nucleotides ◽  
Rational Approach ◽  
Purine Nucleotides ◽  
Purine Salvage ◽  
Nucleotide Synthesis ◽  
Guanine Base

Purine metabolism in Giardia lamblia was investigated by monitoring incorporation of radiolabeled precursors into purine nucleotides in the log-phase trophozoites cultivated in vitro in axenic media and incubated in buffered saline glucose. The lack of incorporation of formate, glycine, hypoxanthine, inosine, and xanthine into the nucleotide pool suggests the absence of de novo purine nucleotide synthesis and the inability to form IMP as the precursor of AMP and GMP in G. lamblia. Only adenine, adenosine, guanine, and guanosine were incorporated. Further analysis of the labeled nucleotides by HPLC indicated that adenine and adenosine are converted only to adenine nucleotides whereas guanine and guanosine are only incorporated into guanine nucleotides. There is no competition of incorporation between adenine/adenosine and guanine/guanosine, and there is no interconversion between adenine and guanine nucleotides. Results from analyzing [5'-3H]guanosine incorporation indicate that the ribose moiety is not incorporated with the guanine base. Assays of purine salvage enzymic activities in the crude extracts of G. lamblia revealed the presence of only four major enzymes; adenosine and guanosine hydrolases and adenine and guanine phosphoribosyl transferases. Apparently, G. lamblia has an exceedingly simple purine salvage system; it converts adenosine and guanosine to corresponding purine bases and then forms AMP and GMP by the actions of corresponding purine phosphoribosyl transferases. The guanine phosphoribosyl transferase in G. lamblia is interesting because it does not recognize either hypoxanthine or xanthine as substrate. It thus must have a unique substrate specificity and may be regarded as a potential target to attack as a rational approach to chemotherapeutic control of giardiasis.

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 metabolism in Saccharomyces cerevisiae

1977 ◽  
Vol 55 (9) ◽  
pp. 935-941 ◽  
Author(s):  
Philip W. Burridge ◽  
Robin A. Woods ◽  
J. Frank Henderson
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Nucleic Acid ◽  
De Novo ◽  
Adenine Nucleotides ◽  
Purine Metabolism ◽  
Guanine Nucleotides ◽  
Wild Type ◽  
Purine Bases

The synthesis, interconversion, and catabolism of purine bases, ribonucleosides, and ribonucleotides in wild-type Saccharomyces cerevisiae were studied by measuring the conversion of radioactive adenine, hypoxanthine, guanine, and glycine into acid-soluble purine bases, ribonucleosides, and ribonucleotides, and into nucleic acid adenine and guanine. The pathway(s) by which adenine is converted to inosinate is (are) uncertain. Guanine is extensively deaminated to xanthine. In addition, some guanine is converted to inosinate and adenine nucleotides. Inosinate formed either from hypoxanthine or de novo is readily converted to adenine and guanine nucleotides.

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 De novo colorectal cancer after liver and kidney transplantation–Microenvironment disturbance

2020 ◽  
Vol 5 (3) ◽  
pp. 100057
Author(s):  
Rui Caetano Oliveira ◽  
Edgar Tavares-Silva ◽  
Ana Margarida Abrantes ◽  
Hugo Antunes ◽  
Paulo Teixeira ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Kidney Transplantation ◽  
De Novo ◽  
Liver And Kidney

Metabolism of adenine nucleotides in the cultured fetal mouse heart

1977 ◽  
Vol 233 (2) ◽  
pp. H282-H288
Author(s):  
I. A. Kaufman ◽  
N. F. Hall ◽  
M. A. DeLuca ◽  
J. S. Ingwall ◽  
S. E. Mayer
Keyword(s):  
Organ Culture ◽  
Adenosine Deaminase ◽  
De Novo ◽  
Adenine Nucleotide ◽  
Adenine Nucleotides ◽  
Energy Charge ◽  
Mouse Heart ◽  
Nucleotide Synthesis ◽  
Fetal Mouse ◽  
Deprivation Period

Intact beating fetal mouse hearts in organ culture were deprived of oxygen and glucose for up to 4 h, resulting in loss of beating, an 80% fall in ATP, reduction of energy charge from 0.85 to 0.48, and doubling of total nucleoside concentration. Radiolabeled adenine nucleotides were degraded to hypoxanthine and inosine, which were lost from the hearts into the medium during the deprivation period. Adenosine and adenine also appeared in the medium when adenosine deaminase was inhibited. After 24 h of O2 and glucose resupply, ATP returned to 60% of control, and energy charge rose to 0.76. Labeled nucleosides and bases remaining in the heart or exogenous labeled adenine were utilized to resynthesize ATP. [14C]glycine was rapidly taken up by recovering hearts but was not used for de novo adenine nucleotide synthesis. Ability to recover ATP and spontaneous contraction appear related to residual nucleotide and nucleoside content rather than to energy charge.

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