The effect of the source and dosage of dietary Cu on redox status in rat tissues

2019 ◽  
Vol 104 (1) ◽  
pp. 352-361
Author(s):  
Katarzyna Ognik ◽  
Ewelina Cholewińska ◽  
Krzysztof Tutaj ◽  
Monika Cendrowska‐Pinkosz ◽  
Wojciech Dworzański ◽  
...  
Keyword(s):  
Redox Status ◽  
Rat Tissues

Ciprofloxacin‐Induced Glutathione Redox Status Alterations in Rat Tissues

2004 ◽  
Vol 27 (3) ◽  
pp. 233-242 ◽  
Author(s):  
Aylin Gürbay ◽  
Filiz Hıncal
Keyword(s):  
Redox Status ◽  
Rat Tissues ◽  
Glutathione Redox

High-resolution scanning electron microscopy (HRSEM) of mitochondria from various rat tissues

1988 ◽  
Vol 46 ◽  
pp. 14-15
Author(s):  
P.J. Lea ◽  
M.J. Hollenberg
Keyword(s):  
Electron Microscopy ◽  
Pigment Epithelium ◽  
Retinal Pigment ◽  
Rat Hepatocytes ◽  
Three Dimensions ◽  
Objective Lens ◽  
Rat Tissues ◽  
Thin Sections ◽  
Reconstruction Methods ◽  
Scanning Electron

Our current understanding of mitochondrial ultrastructure has been derived primarily from thin sections using transmission electron microscopy (TEM). This information has been extrapolated into three dimensions by artist's impressions (1) or serial sectioning techniques in combination with computer processing (2). The resolution of serial reconstruction methods is limited by section thickness whereas artist's impressions have obvious disadvantages.In contrast, the new techniques of HRSEM used in this study (3) offer the opportunity to view simultaneously both the internal and external structure of mitochondria directly in three dimensions and in detail.The tridimensional ultrastructure of mitochondria from rat hepatocytes, retinal (retinal pigment epithelium), renal (proximal convoluted tubule) and adrenal cortex cells were studied by HRSEM. The specimens were prepared by aldehyde-osmium fixation in combination with freeze cleavage followed by partial extraction of cytosol with a weak solution of osmium tetroxide (4). The specimens were examined with a Hitachi S-570 scanning electron microscope, resolution better than 30 nm, where the secondary electron detector is located in the column directly above the specimen inserted within the objective lens.

The Demonstration of Human Prostatic Acid Phosphatase (Pap) With Phosphorylcholine

1976 ◽  
Vol 34 ◽  
pp. 88-89
Author(s):  
José A. Serrano ◽  
Hannah L. Wasserkrug ◽  
Anna A. Serrano ◽  
Arnold M. Seligman
Keyword(s):  
Acid Phosphatase ◽  
Prostate Gland ◽  
Prostatic Acid Phosphatase ◽  
Human Prostate ◽  
Rat Tissues ◽  
Specific Substrate ◽  
Acid Phosphatases ◽  
Lysosomal Acid ◽  
Cacodylate Buffer

As previously reported (1, 2) phosphorylcholine (PC) is a specific substrate for prostatatic acid phosphatase (PAP) as opposed to other acid phosphatases, e.g., lysosomal acid phosphatase. The specificity of PC for PAP is due to the pentavalent nitrogen in PC, a feature that renders PC resistant to hydrolysis by all other acid phosphatases. Detailed comparative cytochemical results in rat tissues are in press. This report deals with ultracytochemical results applying the method to normal and pathological human prostate gland.Fresh human prostate was obtained from 7 patients having transurethral resections or radical prostatectomies. The tissue was fixed in 3% glutaraldehyde- 0.1 M cacodylate buffer (pH 7.4) for 15 min, sectioned at 50 μm on a Sorvall TC-2 tissue sectioner, refixed for a total of 2 hr, and rinsed overnight in 0.1 M cacodylate buffer (pH 7.4)-7.5% sucrose.

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.

Melatonin actions in the heart; more than a hormone

2018 ◽  
Vol 1 (1) ◽  
pp. 21-26 ◽  
Author(s):  
Darío Acuña-Castroviejo ◽  
Maria T Noguiera-Navarro ◽  
Russel J Reiter ◽  
Germaine Escames
Keyword(s):  
Cell Membranes ◽  
Myocardial Cell ◽  
Rat Tissues ◽  
Dependent Manner ◽  
Broad Distribution ◽  
Multiple Organs ◽  
High Doses ◽  
Extrapineal Melatonin ◽  
Dose Dependent ◽  
Different Doses

Due to the broad distribution of extrapineal melatonin in multiple organs and tissues, we analyzed the presence and subcellular distribution of the indoleamine in the heart of rats. Groups of sham-operated and pinealectomized rats were sacrificed at different times along the day, and the melatonin content in myocardial cell membranes, cytosol, nuclei and mitochondria, were measured. Other groups of control animals were treated with different doses of melatonin to monitor its intracellular distribution. The results show that melatonin levels in the cell membrane, cytosol, nucleus, and mitochondria vary along the day, without showing a circadian rhythm. Pinealectomized animals trend to show higher values than sham-operated rats. Exogenous administration of melatonin yields its accumulation in a dose-dependent manner in all subcellular compartments analyzed, with maximal concentrations found in cell membranes at doses of 200 mg/kg bw melatonin. Interestingly, at dose of 40 mg/kg b.w, maximal concentration of melatonin was reached in the nucleus and mitochondrion. The results confirm previous data in other rat tissues including liver and brain, and support that melatonin is not uniformly distributed in the cell, whereas high doses of melatonin may be required for therapeutic purposes.

Regulation of insulin receptor mRNA splicing in rat tissues. Effect of fasting, aging, and diabetes

Diabetes ◽  
1995 ◽  
Vol 44 (10) ◽  
pp. 1196-1201 ◽  
Author(s):  
H. Vidal ◽  
D. Auboeuf ◽  
M. Beylot ◽  
J. P. Riou
Keyword(s):  
Insulin Receptor ◽  
Mrna Splicing ◽  
Rat Tissues ◽  
Receptor Mrna

Intestinal digestibility of selected minerals, growth performance and meat quality in turkeys fed diets supplemented with different sources and levels of zinc

2020 ◽  
Vol 0 (0) ◽  
Author(s):  
Kamil Otowski ◽  
Aleksandra Drażbo ◽  
Katarzyna Ognik ◽  
Krzysztof Kozłowski
Keyword(s):  
Growth Performance ◽  
Meat Quality ◽  
Redox Status ◽  
Bursa Of Fabricius ◽  
Breast Meat ◽  
Zn Addition ◽  
Inclusion Level ◽  
Dietary Treatments ◽  
Different Sources ◽  
Intestinal Digestibility

AbstractThe aim of this study was to determine whether dietary supplementation with zinc oxide nanoparticales (NP-ZnO) as a substitute for the conventional ZnO affects the intestinal digestibility of selected minerals, growth performance and meat quality in turkeys. The replacement of ZnO with NP-ZnO had no effect on the intestinal digestibility of Zn, Cu, Fe and Ca, whereas the lowest dose of supplemental Zn reduced Zn digestibility. The applied inclusion levels and sources of Zn had no effect on the growth performance (except the feed intake) of turkeys, including liveability. No differences in the relative weights of the heart, spleen and bursa of Fabricius (except the liver), or the weights of the femur and tibia were found between the dietary treatments. Neither the dose nor the source of supplemental Zn influenced carcass dressing percentage or the share of breast, thigh and drumstick muscles in the carcass. In comparison with the highest and moderate doses of Zn, the lowest inclusion level of Zn contributed to increased yellowness of breast meat (P=0.005). The analyzed doses and sources of supplemental Zn exerted varied effects on the redox status of fresh and frozen breast meat. In conclusion, the growth performance of turkeys, carcass yield and composition as well as the redox status of fresh and frozen breast meat were generally similar, regardless of the dietary source and level of Zn. The beneficial effect of Zn addition at 100 mg/kg was improved Zn and Ca digestibility, and increased redness of breast meat.

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