Glutathione metabolism in heart and liver of the aging rat

1994 ◽  
Vol 72 (1-2) ◽  
pp. 58-61 ◽  
Author(s):  
M. Stio ◽  
T. Iantomasi ◽  
F. Favilli ◽  
P. Marraccini ◽  
B. Lunghi ◽  
...  
Keyword(s):  
Rat Heart ◽  
Reduced Glutathione ◽  
Age Groups ◽  
Glutathione Metabolism ◽  
Oxidized Glutathione ◽  
Glutathione S Transferase ◽  
Age Related ◽  
Glutamylcysteine Synthetase ◽  
Old Rats ◽  
Glucose 6 Phosphate Dehydrogenase

A comprehensive study on glutathione metabolism in rat heart and liver as a function of age was performed. In the heart, reduced glutathione, total glutathione, and the glutathione redox index showed a decrease during aging, while oxidized glutathione levels increased in 5-month-old rats with respect to the young animals and remained quite constant in 14- and 27-month-old rats. In the liver, the highest levels of reduced glutathione were found in the 2-month-old rats, while oxidized glutathione reached a peak at 5 months. Glutathione-associated enzymes showed age-related changes. Glutathione peroxidase, unaffected by aging in the heart, decreased in the liver of the 27-month-old rats. In the heart and the liver, the highest values of glutathione S-transferase were found at 5 months and 27 months, respectively. Glucose-6-phosphate dehydrogenase followed a similar trend in both heart and liver. Glutathione reductase also showed the same behaviour in heart and in liver, increasing in old rats with respect to the other age groups. A decrease in γ-glutamylcysteine synthetase was found in the heart and liver of 27-month-old rats in comparison with the 2-month-old ones. In conclusion, a decreased antioxidant capability has been demonstrated in both heart and liver of old rats.Key words: glutathione metabolism, age, rat heart, rat liver.

Longitudinal force and stress of rat's esophagus: age-related changes.

1977 ◽  
Vol 232 (6) ◽  
pp. E580
Author(s):  
M P Zabinski ◽  
P Biancani
Keyword(s):  
Age Groups ◽  
Longitudinal Direction ◽  
Longitudinal Force ◽  
Active Stress ◽  
Length Relationship ◽  
Age Related ◽  
Old Rats ◽  
The Difference

Longitudinal force-length relationship of the rat esophagus was studied in vitro in three age groups: 1 mo, 3 mo, and 12 mo. The length of maximum force development (MFD) occurs at 1.4-1.5 times the in vivo length for all age groups. The active force developed at MFD increases markedly with age. The difference in the active forces in the 3-mo and 12-mo age groups is due to differences in cross section because the active stress of the esophagus in the longitudinal direction is approximately equal for the two age groups. The active stress in the 1-mo-old rats is lower than in the 3-mo-old rats, suggesting an increased contractility of the esophagus with age in this period of development.

Angiotensin II enhances β-adrenergic receptor-mediated vasorelaxation in aortas from young but not old rats

2000 ◽  
Vol 279 (6) ◽  
pp. H2807-H2814 ◽  
Author(s):  
William E. Schutzer ◽  
Hong Xue ◽  
John F. Reed ◽  
Jean-Baptiste Roullet ◽  
Sharon Anderson ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Adrenergic Receptor ◽  
Age Groups ◽  
Ang Ii ◽  
Camp Production ◽  
Fischer 344 ◽  
Age Related ◽  
Old Rats ◽  
Potent Vasoconstrictor ◽  
Direct Activator

β-Adrenergic receptor (β-AR)-mediated (cAMP-dependent) vasorelaxation declines with advancing age. It has been shown that angiotensin II (ANG II), a potent vasoconstrictor, enhances cAMP-mediated vasorelaxation. Therefore, we questioned whether ANG II could reverse age-related, impaired β-AR-mediated vasorelaxation and cAMP production. Pretreatment of aortic rings from 6-wk-old or 6-mo-old male Fischer 344 rats with ANG II significantly enhanced vasorelaxation induced by isoproterenol (Iso), a β-AR agonist, and forskolin, a direct activator of adenylyl cyclase, but not dibutyryl-cAMP or isobutylmethylxanthine. The ANG II effect was blocked by losartan but not PD-123319 and was not observed in the aortas from 12- and 24-mo-old animals. Iso-stimulated cAMP production in the aorta was enhanced in the presence of ANG II in the 6-wk-old and 6-mo-old age groups only. Results suggest ANG II cannot reverse the age-related impairment in β-AR-dependent vasorelaxation. We conclude aging may affect a factor common to both ANG II-receptors and β-AR signaling pathways or aging may impair cross-talk between these two receptor pathways.

Differences in lung glutathione metabolism may account for rodent susceptibility in elastase-induced emphysema development

2009 ◽  
Vol 296 (4) ◽  
pp. R1113-R1123 ◽  
Author(s):  
Gisella R. Borzone ◽  
Leonel F. Liberona ◽  
Andrea P. Bustamante ◽  
Claudia G. Saez ◽  
Pablo R. Olmos ◽  
...  
Keyword(s):  
Glutathione Peroxidase ◽  
Glutathione Reductase ◽  
Diffuse Alveolar Damage ◽  
Intratracheal Instillation ◽  
Glutathione Metabolism ◽  
Oxidized Glutathione ◽  
Sprague Dawley ◽  
Sprague Dawley Rats ◽  
Glutamylcysteine Synthetase ◽  
Gsh Metabolism

Syrian Golden hamsters develop more severe emphysema than Sprague-Dawley rats after intratracheal instillation of the same dose of elastase/body weight. Although species variations in antielastase defenses may largely explain these results, other variables, such as differences in lung antioxidants, cannot be overlooked since oxidative stress modulates antiprotease activity. We propose that elastase instillation might affect lung glutathione (GSH) metabolism differently in these species. Our aim was to study in hamsters and rats, lung glutathione metabolism at different times, from the stage of diffuse alveolar damage to advanced emphysema. We measured total and oxidized glutathione content as well as activity and expression of enzymes related to GSH synthesis and redox cycling: γ-glutamylcysteine synthetase, glutathione peroxidase, and glutathione reductase. Whereas rats showed no significant changes in these measurements, hamsters showed significant derangement in GSH metabolism early after elastase instillation: 25% fall in total GSH ( P < 0.05) with no increase in oxidized glutathione associated with reduced enzyme activities 24 h after elastase [60% for γ-glutamylcysteine synthetase ( P < 0.01), 30% for glutathione peroxidase ( P < 0.01), and 75% for glutathione reductase ( P < 0.001)]. GSH homeostasis was restored at the end of the first week, involving transient increased expression of these enzymes. We conclude that elastase induces significant alterations in GSH metabolism of hamster lungs and no overall change in rat lungs. Although differences in disease severity may account for our findings, the hamster becomes vulnerable to functional inhibition of α1-antitrypsin by oxidants and thus, even more susceptible to injury than it would be, considering only its low α1-antitrypsin level.

Effect of age on renal conservation of phosphate in the rat

1986 ◽  
Vol 251 (3) ◽  
pp. F399-F407 ◽  
Author(s):  
G. M. Kiebzak ◽  
B. Sacktor
Keyword(s):  
Age Groups ◽  
Membrane Vesicles ◽  
Fractional Excretion ◽  
Renal Handling ◽  
Pi Transport ◽  
Age Related ◽  
Renal Brush Border Membrane ◽  
Low Phosphorus ◽  
Old Rats ◽  
Effect Of Age

Renal handling of phosphate (Pi) was examined in male Wistar-derived rats, 2-3, 6, 12, 18, and 24 mo of age. We observed a significant age-related phosphaturia [i.e., elevated urinary excretion (UPi V) and fractional excretion (FEPi)] in rats fed a normal phosphorus diet (NPD; 0.5% Pi). Concomitantly, plasma Pi decreased significantly and progressively with age. The mechanism of this age-related decrement in Pi conservation was examined by determining the initial (5 s) rate of Na+ gradient-dependent uptake of Pi in renal brush-border membrane vesicles (BBMV). Pi uptake significantly declined with increasing age. No consistent age-related decrease was seen in the Na+ gradient-dependent uptakes of glucose and proline by the same BBMV preparations, demonstrating the specificity of the Pi transport decrement. Pi transport kinetics revealed a significant age-related decrease in Vmax. No difference in Km of Pi was seen between age groups. These kinetic findings suggest either a decreased number of Pi carriers or decreased turnover of Pi carriers. Elevated parathyroid hormone did not explain the alteration in Pi conservation since urinary cAMP was not elevated in the intact senescent rat, and Pi uptake was not normalized in 24-mo-old rats 3 days after parathyroidectomy. The senescent 24-mo-old rat as well as the young adult 6-mo-old animal adapted to a low-phosphorus diet (LPD; 0.1% Pi) with a striking (greater than 100%) increase in Pi uptake by BBMV compared with NPD. thus the senescent kidney retained the capacity to respond appropriately to a LPD.(ABSTRACT TRUNCATED AT 250 WORDS)

IGFBP mRNA expression in small intestine of rat during postnatal development

2001 ◽  
Vol 281 (6) ◽  
pp. G1378-G1384 ◽  
Author(s):  
C. A. Shoubridge ◽  
C.-B. Steeb ◽  
L. C. Read
Keyword(s):  
Mrna Expression ◽  
Postnatal Development ◽  
Age Groups ◽  
Rat Intestine ◽  
Age Related ◽  
Igf I ◽  
Igf Binding ◽  
Old Rats ◽  
Igf Binding Protein ◽  
Igfbp 3

In contrast to the adult gut, the immature intestine is refractory to subcutaneously infused insulin-like growth factor I (IGF-I). IGF binding protein (IGFBP) mRNA expression was characterized in intestinal tissues from 6-, 19-, and 90-day-old rats to determine if changes in local expression could account for this age-related change in IGF-I potency. For all age groups, IGFBP-3 to -6, but not IGFBP-1 or -2, were detected by Northern blot analysis. IGFBP-3, -4, and -5 were more intensely expressed in the 6-day-old rat intestine compared with weanling or adult tissue. In contrast, IGFBP-6 expression peaked at the time of weaning. In situ hybridization showed IGFBP-3 to -6 expression was confined to cells of the lamina propria and submucosa and also in the muscularis layer for IGFBP-5. Furthermore, the pattern of IGFBP-5 localization in the intestine changed with development. The findings indicate that the expression of IGFBP-3 to -6 is higher in the immature intestine compared with the adult intestine, suggesting locally produced IGFBPs may inhibit systemically derived IGF-I action in the intestine. Therefore, changes to local IGFBP expression may contribute to the varying response of the rat intestine to IGF-I peptides during postnatal development.

scholarly journals Age-related profile of beta-N-acetylhexosaminidase glycosylation in rat liver.

1998 ◽  
Vol 45 (3) ◽  
pp. 791-797 ◽  
Author(s):  
A Lityńska ◽  
M Przybyło
Keyword(s):  
Detection System ◽  
Age Groups ◽  
Glycosylation Pattern ◽  
Lysosomal Fraction ◽  
Age Related ◽  
Group I ◽  
Chain Analysis ◽  
Glycan Chain ◽  
Old Rats ◽  
Galanthus Nivalis

Beta-N-acetylhexosaminidase was prepared from a liver lysosomal fraction obtained from rats between 18 days of gestation (group I) and 72 weeks of age (groups II-VI). A glycan chain analysis was performed after an electrophoresis and blotting, followed by a very sensitive detection system with highly specific digoxigenin-labelled lectins. The presence of high-mannose/hybrid type glycans, as well as their fucosylated forms was shown in all the experimental groups. Complex-type glycans with terminal sialic acid or galactose were present in all the groups except for 1-week-old rats in which only a positive reaction with lectins from Galanthus nivalis and Aleuria aurantia was observed. Thus it may be assumed that age-related changes in the glycosylation pattern occur on the first days after birth.

scholarly journals Comparative transcriptome and metabolome analysis reveal glutathione metabolic network and functional genes underlying blue and red-light mediation in maize seedling leaf

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Tiedong Liu ◽  
Xiwen Zhang
Keyword(s):  
Gene Family ◽  
Red Light ◽  
Maize Seedling ◽  
Glutathione Metabolism ◽  
Glutathione S Transferase ◽  
Metabolome Analysis ◽  
Reductase Gene ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Seedling Leaf ◽  
Differently Expressed Genes

Abstract Background Light quality severely affects biosynthesis and metabolism-associated process of glutathione. However, the role of specific light is still unclear on the glutathione metabolism. In this article, comparatively transcriptome and metabolome methods are used to fully understand the blue and red-light conditions working on the glutathione metabolism in maize seedling leaf. Results There are 20 differently expressed genes and 4 differently expressed metabolites in KEGG pathway of glutathione metabolism. Among them, 12 genes belong to the glutathione S-transferase family, 3 genes belong to the ascorbate peroxidase gene family and 2 genes belong to the ribonucleoside-diphosphate reductase gene family. Three genes, G6PD, SPDS1, and GPX1 belong to the gene family of glucose 6-phosphate dehydrogenase, spermidine synthase, and glutathione peroxidase, respectively. Four differently expressed metabolites are identified. Three of them, Glutathione disulfide, Glutathione, and l-γ-Glutamyl-L-amino acid are decreased while L-Glutamate is increased. In addition, Through PPI analysis, two annotated genes gst16 and DAAT, and 3 unidentified genes 100381533, pco105094 and umc2770, identified as RPP13-like3, BCAT-like1and GMPS, were obtained. By the analysis of protein sequence and PPI network, we predict that pco105094 and umc2770 were involved in the GSSG-GSH and AsA-GSH cycle in the network of glutathione metabolism. Conclusions Compared to red light, blue light remarkably changed the transcription signal transduction and metabolism of glutathione metabolism. Differently expressed genes and metabolic mapped to the glutathione metabolism signaling pathways. In total, we obtained three unidentified genes, and two of them were predicted in current glutathione metabolism network. This result will contribute to the research of glutathione metabolism of maize.

Changes in glutathione status and 3,5,3'-triiodothyronine action in livers of rats given cysteine-deficient diets

1989 ◽  
Vol 61 (2) ◽  
pp. 301-307 ◽  
Author(s):  
H. Garcin ◽  
C. Suberville ◽  
P. Higueret ◽  
D. Higueret
Keyword(s):  
Malate Dehydrogenase ◽  
Nuclear Protein ◽  
Protein Complexes ◽  
Reduced Glutathione ◽  
Scatchard Analysis ◽  
Oxidized Glutathione ◽  
Deficient Diet ◽  
Young Rats ◽  
Glutathione Status ◽  
Glucose 6 Phosphate Dehydrogenase

1. For a period of 32 d young rats were given a diet containing (g/kg) 220 casein, 120 casein +1.93 L-cysteine (Cys), or 120 casein.2. The formation of 3,5,3'-triiodothyronine (T3)-nuclear protein complexes was reduced in rats fed on the Cys-deficient diet.3. Scatchard analysis showed that decreased formation of T3 -nuclear protein complexes was due to a decreased affinity of T3 receptors; this decrease was induced, at least in part, by a reduced glutathione content.4. In rats fed on the Cys-deficient diet there was an expected decrease in growth but an unexpected increase in the activities of glucose-6-phosphate dehydrogenase (EC 1.1.1.49) and malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) (EC 1.1.1.40). It is suggested that this increase is related to an increased oxidized glutathione: reduced glutathione ratio.

scholarly journals Do Connexin Mutants Cause Cataracts by Perturbing Glutathione Levels and Redox Metabolism in the Lens?

Biomolecules ◽  
2020 ◽  
Vol 10 (10) ◽  
pp. 1418
Author(s):  
Oscar Jara ◽  
Peter J. Minogue ◽  
Viviana M. Berthoud ◽  
Eric C. Beyer
Keyword(s):  
Oxidative Damage ◽  
Reduced Glutathione ◽  
Oxidative Modification ◽  
Glutathione Metabolism ◽  
Early Event ◽  
Oxidized Glutathione ◽  
Cataract Formation ◽  
Redox Metabolism ◽  
Gap Junction Channels ◽  
Mouse Lines

Cataracts of many different etiologies are associated with oxidation of lens components. The lens is protected by maintenance of a pool of reduced glutathione (GSH) and other antioxidants. Because gap junction channels made of the lens connexins, Cx46 and Cx50, are permeable to GSH, we tested whether mice expressing two different mutants, Cx46fs380 and Cx50D47A, cause cataracts by impairing lens glutathione metabolism and facilitating oxidative damage. Levels of GSH were not reduced in homogenates of whole mutant lenses. Oxidized glutathione (GSSG) and the GSSG/GSH ratio were increased in whole lenses of Cx50D47A, but not Cx46fs380 mice. The GSSG/GSH ratio was increased in the lens nucleus (but not cortex) of Cx46fs380 mice at 4.5 months of age, but it was not altered in younger animals. Carbonylated proteins were increased in Cx50D47A, but not Cx46fs380 lenses. Thus, both mouse lines have oxidizing lens environments, but oxidative modification is greater in Cx50D47A than in Cx46fs380 mice. The results suggest that GSH permeation through lens connexin channels is not a critical early event in cataract formation in these mice. Moreover, because oxidative damage was only detected in animals with significant cataracts, it cannot be an early event in their cataractogenesis.

Age-related changes in the diurnal rhythm of CRH gene expression in the paraventricular nuclei

1996 ◽  
Vol 270 (2) ◽  
pp. E238-E243 ◽  
Author(s):  
A. Cai ◽  
P. M. Wise
Keyword(s):  
Diurnal Rhythm ◽  
Adrenocorticotropic Hormone ◽  
Age Groups ◽  
Aged Rats ◽  
Middle Aged ◽  
Paraventricular Nuclei ◽  
Age Related ◽  
Old Rats ◽  
Two Age Groups

A circadian rhythm secretion of corticotropin-releasing hormone (CRH) is thought to regulate the circadian pattern of secretion of adrenocorticotropic hormone and corticosterone. We have previously reported that the amplitude of the diurnal rhythm of serum corticosterone concentrations decreases in 17- to 20-mo-old rats. In the present experiment, we tested whether an age-related alteration in the daily rhythm and/or level of CRH mRNA in the paraventricular nuclei (PVN) occurs during middle age. Groups of young and middle-aged animals were killed at several times of day. We assessed the level of CRH mRNA in the PVN and dorsal medial subdivision of the PVN using in situ hybridization. In young rats, CRH mRNA expression exhibited a diurnal rhythm in the dorsal medial PVN. The same trend was observed in the entire medial PVN. In middle-aged rats, no rhythm was detected in either region. The overall average level of CRH mRNA was not different between these two age groups. These findings suggest that changes in the suprachiasmatic nucleus or in its ability to entrain neuroendocrine outputs occur relatively early during the aging process.

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