scholarly journals Differences in deoxycytidine metabolism in mouse and rat

1983 ◽  
Vol 210 (2) ◽  
pp. 367-371 ◽  
Author(s):  
T S Chan ◽  
B D Lakhchaura ◽  
T F Hsu
Keyword(s):  
Rat Plasma ◽  
Lymphoid Cells ◽  
Enzyme Assays ◽  
Rat Tissues ◽  
Rat Serum ◽  
Cytotoxic Effects ◽  
Tissue Extracts ◽  
Pharmacological Response ◽  
Deoxycytidine Deaminase ◽  
Kidney Liver

Bone-marrow macrophages from both rat and mouse release deoxycytidine derived from phagocytosed nuclei. Mouse plasma contains no detectable deoxycytidine (less than 0.1 microM), whereas the concentration in rat plasma is 18 microM. Enzyme assays of tissue extracts show that both mouse and rat spleen contain high deoxycytidine kinase activity. Mouse organs, including kidney, liver and lung, also have deoxycytidine deaminase activity. In contrast, rat tissues have virtually no deoxycytidine deaminase activity. Lack of deaminase provides an explanation for the presence of deoxycytidine in rat plasma. Cytotoxicity assays show that cultured mouse lymphoid cells grown in undialysed rat serum are more resistant to cytotoxic effects of deoxyadenosine than are those cells grown in dialysed rat serum. The results suggest that a major difference in deoxycytidine metabolism between mouse and rat may account for discrepancies in the pharmacological response of the two animals to certain nucleoside compounds.

scholarly journals LC-ESI-LTQ-Orbitrap-MS for Profiling the Distribution of Oleacein and Its Metabolites in Rat Tissues

Antioxidants ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 1083
Author(s):  
Anallely López-Yerena ◽  
Anna Vallverdú-Queralt ◽  
Rosa M. Lamuela-Raventós ◽  
Elvira Escribano-Ferrer
Keyword(s):  
Small Intestine ◽  
Rat Plasma ◽  
Rat Tissues ◽  
Target Tissue ◽  
Experimental Conditions ◽  
Distribution Kinetics ◽  
New Applications ◽  
Kidney Liver ◽  
Acute Intake ◽  
Orbitrap Ms

The purpose of this work was to study the distribution of oleacein (OLEA) and its metabolites in rat plasma and different tissues, namely brain, heart, kidney, liver, lung, small intestine, spleen, stomach, skin, and thyroid, following the acute intake of a refined olive oil containing 0.3 mg/mL of OLEA. For this purpose, a distribution kinetics study was carried out. The plasma and tissues were collected at 1, 2, and 4.5 h after the intervention, and analyzed by LC-ESI-LTQ-Orbitrap-MS. Unmetabolized OLEA was detected in the stomach, small intestine, liver, plasma and, most notably, the heart. This finding may be useful for the development of new applications of OLEA for cardiovascular disease prevention. Noteworthy are also the high levels of hydroxytyrosol (OH-TY) and OLEA + CH3 found in the small intestine, liver, and plasma, and the detection of nine OLEA metabolites, five of them arising from conjugation reactions. Liver, heart, spleen, and lungs were the target tissues where the metabolites were most distributed. However, it is important to note that OH-TY, in our experimental conditions, was not detected in any target tissue (heart, spleen, thyroids, lungs, brain, and skin). These results shed further light on the metabolism and tissue distribution of OLEA and contribute to understanding the mechanisms underlying its effect in human health.

Fibrinolytic Activity of Lung and Spleen Extracts Observed in Conventional but not in Germ-Free Rats

1979 ◽  
Vol 42 (02) ◽  
pp. 726-733 ◽  
Author(s):  
Utako Okamoto ◽  
Jun-ichiro Yamamoto ◽  
Yoko Nagamatsu ◽  
Noboru Horie
Keyword(s):  
Serine Protease ◽  
Plasminogen Activator ◽  
Fibrinolytic Activity ◽  
Iodoacetic Acid ◽  
Thrombin Inhibitor ◽  
Rat Tissues ◽  
Germ Free ◽  
Neutral Ph ◽  
Tissue Extracts

SummaryProtease-like activity which split plasminogen-free fibrin was demonstrated in 2 M KSCN extracts of the lung and spleen of conventional rats. The activity was virtually undetectable in tissue extracts from germ-free rats. The extracts from the conventional rat tissues split fibrin and fibrinogen remarkably at neutral pH, but not casein, when examined using fibrin, fibrinogen-agar and casein-agar plates. The fibrinolytic activity was inhibited by STI and DFP, indicating a serine protease nature. The activity was not inhibited by TLCK, t-AMCHA or dansyl-L-arginine-methylpiperidine amide (a selective synthetic thrombin inhibitor, OM189). It was neither activated nor inhibited by cysteine, KCN or iodoacetic acid. The results obtained indicate that the protease-like activity of the lung and spleen extracted with 2 M KSCN from conventional rats has properties which differ from those of trypsin, plasmin, plasminogen-activator, thrombin, and cathepsin A, B and C.

Uptake, distribution, and excretion of 31silicon in normal rats

1986 ◽  
Vol 251 (6) ◽  
pp. E670-E673 ◽  
Author(s):  
A. J. Adler ◽  
Z. Etzion ◽  
G. M. Berlyne
Keyword(s):  
Blood Brain Barrier ◽  
Silicic Acid ◽  
Plasma Levels ◽  
Brain Barrier ◽  
Major Portion ◽  
Rat Tissues ◽  
Blood Brain ◽  
Intracardiac Injection ◽  
Wet Weight ◽  
Kidney Liver

This study examines the uptake, distribution, and excretion of 31-labeled silicic acid in rat tissues at 1, 2, and 4 h after intracardiac injection of 31Si(OH)4. Plasma levels of 31Si decrease rapidly from 0.71 +/- 0.04% at 1 h to 0.07 +/- 0.06% of the dose administered per milliliter at 4 h. 31Si in plasma was found to be virtually entirely nonprotein bound. Kidney, liver, and lung accumulated the greatest amounts of 31Si per gram of wet weight, with concentrations at 4 h suggesting both relatively avid uptake and retention. Bone, skin, spleen, muscle, and testes also accumulated 31Si, but the levels were considerably lower than the aforementioned organs. Brain, however, contained negligible concentrations of 31Si throughout the study, indicating active exclusion by the blood-brain barrier. The major portion of the administered 31Si, 77 +/- 12%, was recovered in the urine within 4 h.

Characteristics of a somatostatin-binding protein

1978 ◽  
Vol 56 (1) ◽  
pp. 48-53 ◽  
Author(s):  
N. Ogawa ◽  
T. Thompson ◽  
H. G. Friesen
Keyword(s):  
Diabetes Mellitus ◽  
Binding Protein ◽  
Gel Filtration ◽  
The Other ◽  
Rat Tissues ◽  
Cytoplasmic Protein ◽  
Disulfide Bridges ◽  
Thiol Groups ◽  
Tissue Extracts ◽  
Streptozotocin Induced Diabetes

The concentrations of a somatostatin-binding protein, found in the cytosol of a number of rat tissues, are similar in both sexes, and hypophysectomy has little or no effect on the level of binding protein in tissue extracts. On the other hand, streptozotocin-induced diabetes mellitus causes a modest decrease. The somatostatin-binding proteins obtained from extracts of several rat tissues are not only similar in molecular weight but also exhibit a similar isoelectric point and electrophoretic mobility. Agents that block thiol groups or prevent the formation of disulfide bridges markedly decrease the binding of somatostatin to the cytoplasmic protein. Studies using thiol reagents and gel filtration suggest that free thiol groups in somatostatin-binding protein are important for the binding of somatostatin.

Urinary excretion of the TRH-like peptide pyroglutamyl-glutamyl-prolineamide in rats

1997 ◽  
Vol 153 (3) ◽  
pp. 411-421 ◽  
Author(s):  
W Klootwijk ◽  
R D H de Boer ◽  
E Sleddens-Linkels ◽  
S M Cockle ◽  
W W de Herder ◽  
...  
Keyword(s):  
Urinary Excretion ◽  
Anterior Pituitary ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Female Rats ◽  
Male Rats ◽  
Rat Tissues ◽  
Rat Serum ◽  
Methanolic Extracts ◽  
Gonadotrophin Secretion

Abstract TRH-like immunoreactivity (TRH-LI) was estimated in methanolic extracts of rat tissues and blood by RIA using antiserum 4319, which binds most peptides with the structure pGlu-X-ProNH2, or antiserum 8880, which is specific for TRH (pGlu-His-ProNH2). TRH-LI (determined with antiserum 4319) and TRH (determined with antiserum 8880) contents were 8 and 8 ng/g in brain, 216 and 222 ng/g in hypothalamus, 6·5 and 6 ng/g in pancreas, 163 and 116 ng/g in male pituitary, 105 and 77 ng/g in female pituitary, 1 and 0·1 ng/g in salivary gland, 61 and 42 ng/g in thyroid, 12 and 3 ng/g in adrenal, 3 and 0·3 ng/g in prostate, and 11 and 0·8 ng/g in ovary respectively. Blood TRH-LI (antiserum 4319) and TRH (antiserum 8880) levels were 31 and 18 pg/ml in male rats, and 23 and 10 pg/ml in female rats respectively. Unextracted serum obtained from blood kept for at least 1 h at room temperature no longer contained authentic TRH but still contained TRH-LI (males 20·3 ± 3·1, females 15·9 ± 3·0 pg/ml; means ± s.e.m.). Isocratic reverse-phase HPLC showed that TRH-LI in serum is largely pGlu-Glu-ProNH2 (<EEP-NH2), a peptide previously found in prostate and anterior pituitary. In urine, TRH-LI (antiserum 4319) and TRH (antiserum 8880) levels were 3·21 ± 0·35 and 0·32 ± 0·04 ng/ml in male rats and 3·75 ± 0·22 and 0·37 ± 0·04 ng/ml in female rats respectively (means ± s.e.m.). Anion-exchange chromatography on QAE-Sephadex showed that urine of normally fed rats contains both basic/neutral TRH-LI (b/nTRH-LI) and acidic TRH-LI (aTRH-LI) in a ratio of ≈ 40:60, and further analysis by HPLC indicated that aTRH-LI represents <EEP-NH2. Analysis of food extracts and urine from fasted rats demonstrated that b/nTRH-LI is derived from food particles spilled by the rats during urine collection, while aTRH-LI is endogenously produced. While urinary aTRH-LI levels were higher in female than in male rats (2·99 ± 0·41 vs 2·04 ± 0·20 ng/ml), the daily urinary excretion was similar in both sexes (females 15·6 ± 1·4, males 19·5 ± 2·0 ng/day). Intravenously injected <EEP-NH2 disappeared from serum with a half-life of ≈ 1 h, and was recovered unchanged and quantitatively in urine. In contrast, when <EEP-NH2 was administered with food, only ≈ 0·5% was recovered in urine. The urinary clearance rate of serum TRH-LI amounted to 0·52 ± 0·10 ml/min in males and 0·34 ± 0·05 ml/min in females. In view of the presence of <EEP-NH2 in the anterior pituitary gland, and the regulation of its content in parallel with gonadotrophins, we examined the possibility that serum <EEP-NH2 is of pituitary origin and correlates with gonadotrophin secretion. However, treatments that alter pituitary <EEP-NH2 content and gonadotrophin release had no effect on serum TRH-LI or urinary aTRH-LI. In conclusion, the TRH-like peptide <EEP-NH2 is present in rat serum and is excreted into the urine. Moreover, <EEP-NH2 in serum and urine is not derived from rat food and is probably not of pituitary origin. Journal of Endocrinology (1997) 153, 411–421

scholarly journals Primary structure of rat plasma membrane Ca2+-ATPase isoform 4 and analysis of alternative splicing patterns at splice site A

1995 ◽  
Vol 306 (3) ◽  
pp. 779-785 ◽  
Author(s):  
T P Keeton ◽  
G E Shull
Keyword(s):  
Plasma Membrane ◽  
Alternative Splicing ◽  
Splice Site ◽  
Primary Structure ◽  
Sequence Divergence ◽  
Rat Plasma ◽  
Pcr Analysis ◽  
Rat Tissues ◽  
Mrna Tissue Distribution ◽  
Splicing Patterns

We have determined the primary structure of the rat plasma membrane Ca(2+)-ATPase isoform 4 (PMCA4), and have analysed its mRNA tissue distribution and alternative splicing patterns at splice site A. Rat PMCA4 (rPMCA4) genomic clones were isolated and used to determine the coding sequences and intron/exon organization of the 5′-end of the gene, and the remaining coding sequence was determined from PCR-amplified cDNA fragments. Pairwise comparisons reveal that the amino acid sequence of rPMCA4 has diverged substantially from those of rPMCA isoforms 1, 2 and 3 (73-76% identity) and from that of human PMCA4 (87%). Despite the high degree of sequence divergence between the two species, comparisons of intron and untranslated mRNA sequences with the corresponding human sequences confirm the identity of this rat isoform as PMCA4. Northern blot studies demonstrate that the PMCA4 mRNA is expressed in all rat tissues examined except liver, with the highest levels in uterus and stomach. A combination of PCR analysis of alternative splicing patterns and sequence analysis of the gene demonstrate that a 36 nt exon at site A is included in PMCA4 mRNAs of most tissues but is largely excluded in heart and testis. Alternative splicing of both the 36 nt exon and a previously characterized 175 nt exon at splice site C, each of which can be either included or excluded in a highly tissue-specific manner, leads to the production of four different PMCA4 variants ranging in size from 1157 to 1203 amino acids.

Changes in the alkaline phosphatase (EC 3.1.3.1) and inorganic pyrophosphatase (EC 3.6.1.1) activities of rat tissues during magnesium deficiency. The importance of controlling feeding pattern

1976 ◽  
Vol 36 (3) ◽  
pp. 487-495 ◽  
Author(s):  
B. W. Loveless ◽  
F. W. Heaton
Keyword(s):  
Alkaline Phosphatase ◽  
Magnesium Deficiency ◽  
Protein Molecule ◽  
Feeding Pattern ◽  
Inorganic Pyrophosphatase ◽  
Rat Tissues ◽  
Eating Pattern ◽  
Adequate Diet ◽  
Tissue Extracts ◽  
And Control

1. The adoption of a meal-eating pattern of feeding by rats altered the alkaline phosphatase (EC 3.1.3.1) activity in serum and liver. It was therefore necessary to regulate the feeding pattern of both magnesium-deficient rats and control animals receiving a Mg-adequate diet in order to study the effect of the deficiency.2. Mg deficiency decreased the activities of alkaline phosphatase and inorganic pyro-phosphatase (EC 3.6.1.1) in serum, kidney and tibia, but increased them in spleen.3. Addition of a standard concentration of exogenous Mg to tissue extracts usually increased the activity of corresponding enzymes from Mg-deficient and control rats by the same proportion, indicating that the main effect of the deficiency was on the amount of enzyme present rather than on the efficiency of its operation.4. Certain quantitative differences in the response to exogenous Mg and the activity ratio, alkaline phosphatase: inorganic pyrophosphatase were found between tissues from Mg-deficient and control rats. The significance of these are discussed in relation to the association of the two enzymic activities with the same protein molecule, and the possible occurrence of isoenzymes.

Distribution of α1-adrenoceptor subtype proteins in different tissues of neonatal and adult rats

2000 ◽  
Vol 78 (3) ◽  
pp. 237-243 ◽  
Author(s):  
Hao Shen ◽  
Krishna G Peri ◽  
Xing-Fei Deng ◽  
Sylvain Chemtob ◽  
Daya R Varma
Keyword(s):  
Vas Deferens ◽  
Polyclonal Antibodies ◽  
Receptor Subtype ◽  
Receptor Subtypes ◽  
Rat Tissues ◽  
Adult Rats ◽  
Adult Rat ◽  
Old Rats ◽  
Kidney Liver ◽  
The Brain

Distribution of α1-adrenoceptor (α1AR) subtype (α1A, α1B, α1D) proteins in brain, heart, kidney, and liver of 1-week-old rats and in brain, heart, aorta, kidney, liver, vas deferens, prostate, and adrenal glands of adult rats was investigated by Western analysis, using receptor subtype specific polyclonal antibodies. High levels of immunoreactive α1AAR and α1DAR in brain and heart and of α1BAR in liver and heart of neonatal rats were detected. In adult rat tissues, the abundance of α1AAR protein was most marked in the brain, intermediate in heart, aorta, liver, vas deferens, and adrenals, and minimal in the kidney and prostate; relative to other tissues, the expression of α1BAR was higher in brain and heart and that of α1DAR in brain. All the three receptor subtypes increased with age in the brain cortex, whereas the abundance of α1BAR increased in the heart but decreased in the liver; α1AAR and α1DAR in liver, kidney, and heart were not affected by age. It is concluded that α1AR subtypes are widely expressed in different neonatal and adult rat tissues.Key words: α1A-adrenoceptors, α1B-adrenoceptors, α1D-adrenoceptors, α1-adrenoceptor proteins.

scholarly journals Forms of lipoprotein lipase in rat tissues: in adipose tissue the proportion of inactive lipase increases on fasting

1996 ◽  
Vol 313 (3) ◽  
pp. 893-898 ◽  
Author(s):  
Martin BERGÖ ◽  
Gunilla OLIVECRONA ◽  
Thomas OLIVECRONA
Keyword(s):  
Adipose Tissue ◽  
Lipoprotein Lipase ◽  
Translational Regulation ◽  
Specific Activity ◽  
Catalytic Efficiency ◽  
Rat Tissues ◽  
Tissue Extracts ◽  
Significant Difference ◽  
Lpl Mass ◽  
Fasted Rats

Previous studies have shown that the ratio of lipoprotein lipase (LPL) catalytic activity to LPL mass in tissues differs in different conditions, but it is not clear whether this occurs by a change in the catalytic efficiency of the LPL molecules, or because of a shift in the relation between active and inactive forms of the enzyme. To explore this, we have measured LPL activity and mass in detergent extracts of rat tissues. LPL specific activity was high and similar in heart, skeletal muscle, lung and brain. The liver had significantly lower specific activity, which is in accord with previous findings that the liver takes up and catabolizes LPL. The specific activity was also low in adipose tissue from fasted rats. When tissue extracts were applied to columns of heparin–agarose and eluted by a gradient of NaCl, a peak of active LPL was eluted at 1.0 M NaCl, but there was also a peak of inactive LPL protein, which was eluted at 0.6 M NaCl. In adipose tissue, LPL activity decreased by 70–80% during an overnight fast, whereas LPL mass decreased by only 20–40%. The mass ratio between inactive and active LPL, as separated by heparin–agarose chromatography, increased from 0.5 to over 2 during the fast. In hearts there was no significant difference between fed and fasted rats in total LPL activity, LPL mass or in the distribution between inactive and active forms. The results indicate that the relation between inactive (probably monomeric) and active (dimeric) forms of LPL is a target for post-translational regulation in adipose tissue.

Sign in / Sign up

Export Citation Format

Share Document