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.

scholarly journals Tissue Distribution of Oleocanthal and Its Metabolites after Oral Ingestion in Rats

Antioxidants ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 688
Author(s):  
Anallely López-Yerena ◽  
Anna Vallverdú-Queralt ◽  
Olga Jáuregui ◽  
Xavier Garcia-Sala ◽  
Rosa M. Lamuela-Raventós ◽  
...  
Keyword(s):  
Olive Oil ◽  
Virgin Olive Oil ◽  
Extra Virgin Olive Oil ◽  
Rat Plasma ◽  
Molecular Structures ◽  
Rat Tissues ◽  
Potential Health ◽  
Regular Consumption ◽  
Acute Intake

Claims for the potential health benefits of oleocanthal (OLC), a dietary phenolic compound found in olive oil, are based mainly on in vitro studies. Little is known about the tissue availability of OLC, which is rapidly metabolized after ingestion. In this study, the distribution of OLC and its metabolites in rat plasma and tissues (stomach, intestine, liver, kidney, spleen, lungs, heart, brain, thyroid and skin) at 1, 2 and 4.5 h after the acute intake of a refined olive oil containing 0.3 mg/mL of OLC was examined by LC-ESI-LTQ-Orbitrap-MS. OLC was only detected in the stomach and intestine samples. Moreover, at 2 and 4.5 h, the concentration in the stomach decreased by 36% and 74%, respectively, and in the intestine by 16% and 33%, respectively. Ten OLC metabolites arising from phase I and phase II reactions were identified. The metabolites were widely distributed in rat tissues, and the most important metabolizing organs were the small intestine and liver. The two main circulating metabolites were the conjugates OLC + OH + CH3 and OLC + H2O + glucuronic acid, which may significantly contribute to the beneficial health effects associated with the regular consumption of extra virgin olive oil. However, more studies are necessary to determine the concentrations and molecular structures of OLC metabolites in human plasma and tissues when consumed with the presence of other phenolic compunds present in EVOO.

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.

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.

scholarly journals The regulation of phosphate-activated glutaminase activity and glutamine metabolism in the streptozotocin-diabetic rat

1984 ◽  
Vol 224 (1) ◽  
pp. 207-214 ◽  
Author(s):  
M Watford ◽  
E M Smith ◽  
E J Erbelding
Keyword(s):  
Drinking Water ◽  
Small Intestine ◽  
Glutamine Metabolism ◽  
Diabetic Rat ◽  
Complete Suppression ◽  
Chemically Induced ◽  
Phosphate Activated Glutaminase ◽  
Kidney Liver ◽  
Nh4cl Solution ◽  
Glutaminase Activity

The activity of phosphate-activated glutaminase was increased in the kidney, liver and small intestine of rats made diabetic for 6 days with injection of streptozotocin (75 mg/kg body wt.). Insulin prevented this increase in all three tissues. Treatment with NaHCO3, to correct the acidosis that accompanies diabetes, prevented the increase in renal glutaminase activity, but not that in liver or small intestine. Chemically induced acidosis (NH4Cl solution as drinking water) or alkalosis (NaHCO3 solution as drinking water) increased and decreased, respectively, glutaminase activity in the kidney, but were without significant effect on the activity in liver and small intestine. The increase in glutaminase activity in the small intestine during diabetes was due to an overall increase in the size of this organ, and was only detectable when activity was expressed in terms of whole organ, not mucosal scrapings or isolated enterocytes. Prolonged diabetes (40 days) resulted in an even greater increase in the size and glutaminase activity of the small intestine. Despite this marked increase in capacity for glutamine catabolism, arteriovenous-difference measurements showed a complete suppression of plasma glutamine utilization by the small intestine during diabetes, confirming the report by Brosnan, Man, Hall, Colbourne & Brosnan [(1983) Am. J. Physiol. 235, E261-E265].

Sequence, tissue distribution, and functional characterization of the rat fructose transporter GLUT5

1993 ◽  
Vol 264 (6) ◽  
pp. G1169-G1176 ◽  
Author(s):  
E. B. Rand ◽  
A. M. Depaoli ◽  
N. O. Davidson ◽  
G. I. Bell ◽  
C. F. Burant
Keyword(s):  
Small Intestine ◽  
Functional Characterization ◽  
Cdna Probe ◽  
Amino Acid Identity ◽  
Human Testis ◽  
Cdna Clones ◽  
Rat Tissues ◽  
Rat Small Intestine ◽  
Cross Hybridization ◽  
Distal Small Intestine

cDNA clones encoding rat GLUT5-small intestinal facilitative hexose transporter were isolated from a jejunum library by cross-hybridization with a human GLUT5 cDNA probe. The cDNA sequence indicates that rat GLUT5 is composed of 502 amino acids and has 81.5% amino acid identity and 87.3% similarity with the sequence of human GLUT5. Expression of synthetic rat GLUT5 mRNA in Xenopus oocytes showed that rat GLUT5 was able to mediate the uptake of fructose and, to a lesser extent, of glucose. RNA blotting studies showed that GLUT5 mRNA was present in rat small intestine, kidney, and brain. Although GLUT5 mRNA is expressed in human testis, adipose tissue, and skeletal muscle, it could not be detected by RNA blotting in these rat tissues. Developmental studies showed low levels of GLUT5 mRNA in rat small intestine and kidney during the prenatal period with a rapid induction of GLUT5 expression occurring postnatally. In situ hybridization studies of GLUT5 mRNA expression in the small intestine revealed differential expression along the crypt-villus axis with the highest levels of mRNA being in the midvillus region. In addition, there was quantitatively more GLUT5 mRNA detected in the proximal as opposed to the distal small intestine.

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.

Liver glyconeogenesis: a pathway to cope with postprandial amino acid excess in high-protein fed rats?

2007 ◽  
Vol 292 (4) ◽  
pp. R1400-R1407 ◽  
Author(s):  
Dalila Azzout-Marniche ◽  
Claire Gaudichon ◽  
Clémence Blouet ◽  
Cécile Bos ◽  
Véronique Mathé ◽  
...  
Keyword(s):  
Gene Expression ◽  
Small Intestine ◽  
Amino Acid ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Glycogen Synthesis ◽  
High Protein ◽  
Hepatic Glycogen ◽  
Molecular Evidence ◽  
Experimental Conditions ◽  
Fed State

This paper provides molecular evidence for a liver glyconeogenic pathway, that is, a concomitant activation of hepatic gluconeogenesis and glycogenesis, which could participate in the mechanisms that cope with amino acid excess in high-protein (HP) fed rats. This evidence is based on the concomitant upregulation of phosphoenolpyruvate carboxykinase (PEPCK) gene expression, downregulation of glucose 6-phosphatase catalytic subunit (G6PC1) gene expression, an absence of glucose release from isolated hepatocytes and restored hepatic glycogen stores in the fed state in HP fed rats. These effects are mainly due to the ability of high physiological concentrations of portal blood amino acids to counteract glucagon-induced liver G6PC1 but not PEPCK gene expression. These results agree with the idea that the metabolic pathway involved in glycogen synthesis is dependent upon the pattern of nutrient availability. This nonoxidative glyconeogenic disposal pathway of gluconeogenic substrates copes with amino excess and participates in adjusting both amino acid and glucose homeostasis. In addition, the pattern of PEPCK and G6PC1 gene expression provides evidence that neither the kidney nor the small intestine participated in gluconeogenic glucose production under our experimental conditions. Moreover, the main glucose-6-phosphatase (G6Pase) isoform expressed in the small intestine is the ubiquitous isoform of G6Pase (G6PC3) rather than the G6PC1 isoform expressed in gluconeogenic organs.

Thin Layer Chromatographic Screening Method for Sulfadiazine Residues in Calf Tissues, Plasma, and Urine

1978 ◽  
Vol 61 (3) ◽  
pp. 545-549
Author(s):  
Joseph L Woolley ◽  
Oliver Murch ◽  
Carl W Sigel
Keyword(s):  
Thin Layer ◽  
Screening Method ◽  
Target Tissue ◽  
Highly Sensitive ◽  
Tissue Homogenates ◽  
Specific Tissue ◽  
Sulfonamide Residues ◽  
Kidney Liver ◽  
Layer Chromatography ◽  
Endogenous Substances

Abstract Because of the lack of specificity of the Bratton-Marshall procedure for assaying sulfonamides, a sensitive, specific tissue residue assay for sulfadiazine (SDZ) was developed. The methodology has been extended to provide a highly sensitive screen for sulfonamide residues, which employs 2-dimensional thin layer chromatography in conjunction with fluorescamine derivatization. The procedure described, which has been developed for SDZ in calf tissues, involves direct ethyl acetate extraction of tissue homogenates. Following evaporation of the organic phase, a portion of the residue is spotted on a 20x20 cm silica gel 60 plate, which is then developed in 2 dimensions with solvent systems devised to separate SDZ from endogenous substances as well as from 12 other sulfonamides that might be present in calf tissues. The presence of SDZ at a concentration of 0.1 ppm or its absence is easily demonstrated in calf kidney, liver, muscle, plasma, and urine. The basic method can be modified for a particular sulfonamide in a target tissue and can be used as a quantitative assay for sulfonamide residues.

scholarly journals Sphenopalatine Ganglion Stimulation Upregulates Transport of Intra-Arterial Temozolomide Across the Blood–Brain Barrier

Neurosurgery ◽  
2019 ◽  
Vol 66 (Supplement_1) ◽  
Author(s):  
Thana N Theofanis ◽  
Ankit Rochani ◽  
Richard F Schmidt ◽  
Michael J Lang ◽  
Geoffrey Stricsek ◽  
...  
Keyword(s):  
Blood Brain Barrier ◽  
High Performance ◽  
Internal Standard ◽  
The United States ◽  
Rat Plasma ◽  
Brain Barrier ◽  
Target Tissue ◽  
Sphenopalatine Ganglion ◽  
Blood Brain ◽  
Treatment Paradigm

Abstract INTRODUCTION Sphenopalatine ganglion (SPG) stimulation has been shown to reversibly alter blood–brain barrier (BBB) permeability. At the present time, it is widely used for the treatment of cluster headaches in Europe and is well tolerated for this use in humans. METHODS In a rat model, we assessed the permeability of intra-arterial temozolomide with and without sphenopalatine ganglion stimulation. We developed a high-performance liquid chromatography and mass spectrometry method to measure temozolomide in rat plasma and brain tissue, with caffeine as the internal standard. RESULTS Here we show a statistically significant (P = .0006), 5-fold upregulation of TMZ crossing the BBB and reaching brain parenchyma in rats receiving low-frequency (LF, 10 Hz) SPG stimulation. CONCLUSION Glioblastoma multiforme (GBM) remains an extremely difficult disease to treat. Since 2004, the gold standard of treatment for GBM in the United States includes surgery + TMZ and radiation. Our treatment paradigm shows a mechanism in which we could more effectively and safely deliver TMZ in a targeted manner, to minimize systemic toxicity and maximize action at the target tissue. The SPG Stimulation treatment paradigm could be used in a broad spectrum of central nervous system (CNS) pathologies.

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