Effects of changes in the concentration of systemic progesterone on ions, amino acids and energy substrates in cattle oviduct and uterine fluid and blood

2010 ◽  
Vol 22 (4) ◽  
pp. 684 ◽  
Author(s):  
S. A. Hugentobler ◽  
J. M. Sreenan ◽  
P. G. Humpherson ◽  
H. J. Leese ◽  
M. G. Diskin ◽  
...  
Keyword(s):  
Amino Acid ◽  
Marked Effect ◽  
Fluid Secretion ◽  
Early Embryo ◽  
Secretion Rate ◽  
Maternal Environment ◽  
Uterine Fluid ◽  
Oviduct Fluid ◽  
Amino Acid Concentrations

Early embryo loss is a major factor affecting the conception rate in cattle. Up to 40% of cattle embryos die within 3 weeks of fertilisation while they are nutritionally dependent on oviduct and uterine fluids for their survival. Inadequate systemic progesterone is one of the factors contributing to this loss. We have characterised the effects of changes in systemic progesterone on amino acid, ion and energy substrate composition of oviduct and uterine fluids on Days 3 and 6, respectively, of the oestrus cycle in cattle. Oviduct and uterine fluids were collected in situ following infusion of progesterone. There was no effect of progesterone on oviduct fluid secretion rate; however, uterine fluid secretion rate was lowered. Progesterone increased uterine glucose, decreased oviduct sulfate and, to a lesser degree, oviduct sodium, but had no effect on any of the ions in the uterus. The most marked effect of progesterone was on oviducal amino acid concentrations, with a twofold increase in glycine, whereas in the uterus only valine was increased. These results provide novel information on the maternal environment of the early cattle embryo and provide further evidence of progesterone regulation of oviduct amino acid concentrations in cattle.

Uptake and metabolism of amino acids by the dog liver perfused in situ

1962 ◽  
Vol 202 (3) ◽  
pp. 407-414 ◽  
Author(s):  
Rapier H. McMenamy ◽  
William C. Shoemaker ◽  
Jonas E. Richmond ◽  
David Elwyn
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Mixture ◽  
Acid Mixture ◽  
Sharp Rise ◽  
Dog Blood ◽  
Dog Liver ◽  
Amino Acid Concentrations ◽  
Uptake And Metabolism

Dog livers were perfused in situ for periods up to 6 hr with dog blood recycled through a pump-oxygenator. An amino acid mixture was administered for 90 min. Concentrations of amino acids were determined at intervals of 30 min or more. Rates of uptake and metabolism were calculated. After the start of perfusion, there is a fall in most plasma amino acid concentrations and a reciprocal rise in liver amino acids. Addition of amino acids causes a sharp rise in plasma amino acids. There is a rapid uptake of most of the amino acids by liver, although the concentrations of amino acids in liver fail to rise appreciably. Notable exceptions are valine, leucine, and isoleucine. Uptake of amino acids stimulates: a) an increase in the rate of synthesis of urea which ultimately accounts for 90% of the metabolized amino acids; b) a net synthesis of ornithine; and c) net noncatabolic metabolism of amino acids which may in part be protein synthesis. The results support the view that the liver temporarily stores a part of ingested amino acids as proteins, and subsequently makes them available to other organs.

Regulation of protein synthesis in lung by amino acids and insulin

1983 ◽  
Vol 245 (5) ◽  
pp. E508-E514
Author(s):  
J. M. Besterman ◽  
C. A. Watkins ◽  
D. E. Rannels
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Rat Plasma ◽  
Colloid Osmotic Pressure ◽  
Atp Depletion ◽  
Concentration Addition ◽  
Amino Acid Availability ◽  
Amino Acid Concentrations

Acute effects of amino acid availability and insulin on protein synthesis were investigated in rat lungs perfused in situ with buffer containing either 4.5% fraction V bovine serum albumin (FrV BSA), 4.5% essentially fatty acid-free (FAF) BSA, or 4.5% dextran to maintain colloid osmotic pressure. In the presence of FrV BSA, protein synthesis was unaffected by perfusion for 1 or 3 h with buffer containing no added amino acids (0X), as compared with amino acids at concentrations one (1X) or five (5X) times those in rat plasma. Regardless of the amino acid concentration, addition of insulin was without effect. Likewise, in lungs perfused for 1 h with either FAF BSA or dextran, protein synthesis was insensitive to amino acid availability or to insulin. After 3 h, however, protein synthesis decreased 34 and 37%, respectively, when these lungs were perfused in the absence of both amino acids and insulin. In both cases, the inhibition was prevented by addition of insulin to the perfusate; addition of the hormone to perfusate containing 1X amino acids or elevating perfusate amino acids to 5X did not affect protein synthesis. The deficit in protein synthesis observed in the absence of both amino acids and insulin was not accompanied by ATP depletion or by lower intracellular concentrations of amino acids. Similarly, the effect of insulin was not associated with a general elevation in intracellular amino acid concentrations.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Overexpression of ornithine aminotransferase: consequences on amino acid homeostasis

2008 ◽  
Vol 101 (6) ◽  
pp. 843-851 ◽  
Author(s):  
Gabrielle Ventura ◽  
Jean-Pascal De Bandt ◽  
Frédéric Segaud ◽  
Christine Perret ◽  
Daniel Robic ◽  
...  
Keyword(s):  
Amino Acid ◽  
Transgene Expression ◽  
Transgenic Animals ◽  
Metabolic Effects ◽  
Ornithine Aminotransferase ◽  
Wild Type ◽  
Rate Of Reaction ◽  
Amino Acid Concentrations ◽  
Transgenic Male

Ornithine aminotransferase (OAT) is a reversible enzyme expressed mainly in the liver, kidney and intestine. OAT controls the interconversion of ornithine into glutamate semi-aldehyde, and is therefore involved in the metabolism of arginine and glutamine which play a major role in N homeostasis. We hypothesised that OAT could be a limiting step in glutamine–arginine interconversion. To study the contribution of the OAT enzyme in amino acid metabolism, transgenic mice that specifically overexpress human OAT in the liver, kidneys and intestine were generated. The transgene expression was analysed by in situ hybridisation and real-time PCR. Tissue (liver, jejunum and kidney) OAT activity, and plasma and tissue (liver and jejunum) amino acid concentrations were measured. Transgenic male mice exhibited higher OAT activity in the liver (25 (sem 4) v. 11 (sem 1) nmol/min per μg protein for wild-type (WT) mice; P < 0·05) but there were no differences in kinetic parameters (i.e. Km and maximum rate of reaction (Vmax)) between WT and transgenic animals. OAT overexpression decreased plasma and liver ornithine concentrations but did not affect glutamine or arginine homeostasis. There was an inverse relationship between ornithine levels and OAT activity. We conclude that OAT overexpression has only limited metabolic effects, probably due to the reversible nature of the enzyme. Moreover, these metabolic modifications had no effect on phenotype.

scholarly journals Amino acid concentrations in uterine fluid during early pregnancy differ in fertile and subfertile dairy cow strains

2014 ◽  
Vol 97 (3) ◽  
pp. 1364-1376 ◽  
Author(s):  
S. Meier ◽  
M.D. Mitchell ◽  
C.G. Walker ◽  
J.R. Roche ◽  
G.A. Verkerk
Keyword(s):  
Amino Acid ◽  
Early Pregnancy ◽  
Dairy Cow ◽  
Uterine Fluid ◽  
Amino Acid Concentrations

scholarly journals Spatial and Pregnancy-Related Changes in the Protein, Amino Acid, and Carbohydrate Composition of Bovine Oviduct Fluid

2020 ◽  
Vol 21 (5) ◽  
pp. 1681 ◽  
Author(s):  
Beatriz Rodríguez-Alonso ◽  
Veronica Maillo ◽  
Omar Salvador Acuña ◽  
Rebeca López-Úbeda ◽  
Alejandro Torrecillas ◽  
...  
Keyword(s):  
Amino Acid ◽  
High Performance ◽  
Amino Acid Content ◽  
Phosphoglycerate Kinase ◽  
Cell System ◽  
Early Embryo ◽  
Carbohydrate Composition ◽  
Protein Amino Acid ◽  
Oviduct Fluid ◽  
Post Hoc

Knowledge of how the biochemical composition of the bovine oviduct is altered due to the oviduct anatomy or the presence of an embryo is lacking. Thus, the aim of this study was to assess the effect of (І) oviduct anatomy and (ІІ) embryo presence on oviductal fluid (OF) protein, amino acid, and carbohydrate composition. Cross-bred beef heifers (n = 19) were synchronized and those in standing estrus were randomly allocated to a cyclic (non-bred) or pregnant (artificially inseminated) group. All heifers were slaughtered on Day 3 after estrus. The oviducts ipsilateral to the corpus luteum from each animal were isolated, straightened and cut, separating ampulla and isthmus. Each portion was flushed with 500 µl of PBS enabling recovery of the oocyte/embryo. Recovered unfertilized oocytes (cyclic group) and embryos (8-cell embryos; pregnant group) were located in the isthmus of the oviduct. Samples of flushing medium from the isthmus and ampulla were used for proteomic (n = 2 per group), amino acid (n = 5), and carbohydrate (n = 5) analysis. For proteomic analysis, total protein from cyclic and pregnant samples were labelled with different cyanine fluorescent probes and separated according to the isoelectric point using immobilized pH gradient strips (pH 3–10, 17 cm, Protean® IEF cell system, Bio Rad). Second dimension was performed in a polyacrylamide gel (12%) in the presence of SDS using a Protean II XL system (Bio Rad). Images were obtained with a Typhoon 9410 scanner and analyzed with Progenesis SameSpots software v 4.0. Amino acid content in the OF was determined by high performance liquid chromatography (HPLC). Glucose, lactate, and pyruvate were quantified using microfluorometric enzyme-linked assays. For the proteomic assessment, the results of the image analysis were compared by ANOVA. For both amino acid and carbohydrate analyses, statistical analysis was carried out by 2-way ANOVA with the Holm-Sidak nonparametric post hoc analysis. On Day 3 post-estrus, OF composition varied based on (І) anatomical region, where isthmic metabolites were present in lower (i.e., lactate, glycine, and alanine) or higher (i.e., arginine) concentrations compared to the ampulla; and (ІІ) embryo presence, which was correlated with greater, arginine, phosphoglycerate kinase 1, serum albumin, α-1-antiproteinase and IGL@ protein concentrations. In conclusion, data indicate that the composition of bovine OF is anatomically dynamic and influenced by the presence of an early embryo.

Isolation and embryonic expression of an abdominal-A-like gene from the lepidopteran, Manduca sexta

Development ◽  
1991 ◽  
Vol 112 (1) ◽  
pp. 119-129 ◽  
Author(s):  
L.M. Nagy ◽  
R. Booker ◽  
L.M. Riddiford
Keyword(s):  
Amino Acid ◽  
Manduca Sexta ◽  
Abdominal Segment ◽  
Early Embryo ◽  
Predicted Amino Acid Sequence ◽  
Posterior Half ◽  
Larval Stages ◽  
Amino Acid Region ◽  
In Situ Hybridizations

Using sequence homology to the Drosophila Antennapedia gene, we isolated a homeobox-containing gene from the lepidopteran, Manduca sexta. Sequence analysis and in situ hybridizations to tissue sections suggest that the Manduca gene encodes a lepidopteran homologue of the Drosophila Bithorax complex gene abdominal-A. The predicted amino acid sequence of a 76 amino acid region that includes the homeobox and the regions immediately flanking it are identical between the Manduca and Drosophila genes. Northern blots reveal that the manduca abd-A gene is expressed first in the early embryo and continues to be expressed throughout later embryonic and larval stages. In situ hybridizations show that the posterior half of the first abdominal segment marks the anterior border of the Manduca abd-A expression. This expression pattern demonstrates the conservation of parasegments as domains of gene activity in the lepidopteran embryo. The Manduca abd-A expression extends from the posterior half of the first abdominal segment through the tenth abdominal segment, a domain that is greater than that of the Drosophila abd-A expression, and reflects the difference in visible segment number between the two insects.

scholarly journals Foetal glutamate as a possible precursor of placental glutamine in the guinea pig

1981 ◽  
Vol 198 (2) ◽  
pp. 397-401 ◽  
Author(s):  
D L Bloxam ◽  
C F Tyler ◽  
M Young
Keyword(s):  
Amino Acid ◽  
Guinea Pig ◽  
Foetal Circulation ◽  
Guinea Pig Placenta ◽  
Near Term ◽  
Pig Placenta ◽  
Amino Acid Concentrations ◽  
Net Release

The role of foetal glutamate as a source of placental glutamine was investigated in the near-term pregnant guinea-pig placenta perfused in situ through the umbilical vessels. With normal foetal amino acid concentrations there was a significant two-way exchange of glutamate between the placenta and foetal perfusate, but a net release of the amino acid from the placenta. Radioactively labelled glutamate carbon entering the placenta by this exchange was freely incorporated into intracellular glutamine, but only 1.5% of it was found in glutamine transported out into the foetal circulation. In the guinea pig, therefore, foetal glutamate does not appear to be a precursor of glutamine released from the placenta on the foetal side.

Effect of maternal diet on the amino acid composition of human uterine fluid

2014 ◽  
Author(s):  
Alexandra Jayne Kermack ◽  
Ying Cheong ◽  
Nick Brook ◽  
Nick Macklon ◽  
Franchesca D Houghton
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Maternal Diet ◽  
Uterine Fluid
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