scholarly journals Amino Acids and the Early Mammalian Embryo: Origin, Fate, Function and Life-Long Legacy

2021 ◽  
Vol 18 (18) ◽  
pp. 9874
Author(s):  
Henry J. Leese ◽  
Paul McKeegan ◽  
Roger G Sturmey
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Culture Media ◽  
Early Embryo ◽  
Amino Acid Derivative ◽  
Cellular Functions ◽  
Traditional Role ◽  
Mammalian Embryo ◽  
Early Mammalian Embryo ◽  
And Function

Amino acids are now recognised as having multiple cellular functions in addition to their traditional role as constituents of proteins. This is well-illustrated in the early mammalian embryo where amino acids are now known to be involved in intermediary metabolism, as energy substrates, in signal transduction, osmoregulation and as intermediaries in numerous pathways which involve nitrogen metabolism, e.g., the biosynthesis of purines, pyrimidines, creatine and glutathione. The amino acid derivative S-adenosylmethionine has emerged as a universal methylating agent with a fundamental role in epigenetic regulation. Amino acids are now added routinely to preimplantation embryo culture media. This review examines the routes by which amino acids are supplied to the early embryo, focusing on the role of the oviduct epithelium, followed by an outline of their general fate and function within the embryo. Functions specific to individual amino acids are then considered. The importance of amino acids during the preimplantation period for maternal health and that of the conceptus long term, which has come from the developmental origins of health and disease concept of David Barker, is discussed and the review concludes by considering the potential utility of amino acid profiles as diagnostic of embryo health.

scholarly journals A Second and Unusual pucBA Operon of Rhodobacter sphaeroides 2.4.1: Genetics and Function of the Encoded Polypeptides

2003 ◽  
Vol 185 (20) ◽  
pp. 6171-6184 ◽  
Author(s):  
Xiaohua Zeng ◽  
Madhu Choudhary ◽  
Samuel Kaplan
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Complex Formation ◽  
Rhodobacter Sphaeroides ◽  
Sequence Data ◽  
Sole Source ◽  
Amino Acid Derivative ◽  
Dna Sequence Data ◽  
And Function ◽  
High Degree

ABSTRACT A new operon (designated the puc2BA operon) displaying a high degree of similarity to the original pucBA genes of Rhodobacter sphaeroides 2.4.1 (designated puc1) was identified and studied genetically and biochemically. The puc2B-encoded polypeptide is predicted to exhibit 94% identity with the original β-apoprotein. The puc2A-encoded polypeptide is predicted to be much larger (263 amino acids) than the 54-amino-acid puc1A-encoded polypeptide. In the first 48 amino acids of the puc2A-encoded polypeptide there is 58% amino acid sequence identity to the original puc1A-encoded polypeptide. We found that puc2BA is expressed, and DNA sequence data suggested that puc2BA is regulated by the PpsR/AppA repressor-antirepressor and FnrL. Employing genetic and biochemical approaches, we obtained evidence that the puc2B-encoded polypeptide is able to enter into LH2 complex formation, but neither the full-length puc2A-encoded polypeptide nor its N-terminal 48-amino-acid derivative is able to enter into LH2 complex formation. Thus, the sole source of α-polypeptides for the LH2 complex is puc1A. The role of the puc1C-encoded polypeptide was also determined. We found that the presence of this polypeptide is essential for normal levels of transcription and translation of the puc1 operon but not for transcription and translation of the puc2 operon. Thus, the puc1C gene product appears to have both transcriptional and posttranscriptional roles in LH2 formation. Finally, the absence of any LH2 complex when puc1B was deleted in frame was surprising since we know that in the presence of functional puc2BA, approximately 30% of the LH2 complexes normally observed contain a puc2B-encoded β-polypeptide.

scholarly journals Amino acid sequence of the encephalitogenic basic protein from human myelin

1971 ◽  
Vol 123 (1) ◽  
pp. 57-67 ◽  
Author(s):  
P. R. Carnegie
Keyword(s):  
Amino Acids ◽  
Central Nervous System ◽  
Nervous System ◽  
Amino Acid ◽  
Basic Protein ◽  
Structure And Function ◽  
Autoimmune Encephalomyelitis ◽  
The Central Nervous System ◽  
And Function ◽  
Experimental Autoimmune

Myelin from the central nervous system contains an unusual basic protein, which can induce experimental autoimmune encephalomyelitis. The basic protein from human brain was digested with trypsin and other enzymes and the sequence of the 170 amino acids was determined. The localization of the encephalitogenic determinants was described. Possible roles for the protein in the structure and function of myelin are discussed.

Source and function of urinary ammonia in the alligator

1959 ◽  
Vol 197 (4) ◽  
pp. 873-879 ◽  
Author(s):  
Roland A. Coulson ◽  
Thomas Hernandez
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Acid Level ◽  
Amino Acid Level ◽  
Plasma Amino Acid ◽  
Plasma Amino Acids ◽  
Renal Reabsorption ◽  
And Function ◽  
Phosphate Solutions

The rate of renal deamination of 18 amino acids was determined by injecting them into alligators and measuring the ammonia excreted. Not only did glycine, alanine, glutamine and leucine account for nearly half of the plasma amino acids, they were also deaminated more rapidly than any of the others. In view of this it was concluded that these four amino acids are the natural precursors of urinary NH3 in the alligator. Increased NH3 and CO2 excretion following glycine injections resulted in increased renal reabsorption of Na and Cl when NaCl was injected and increased Na reabsorption when NaHCO3 or Na phosphate solutions were injected. The fact that excess NH4HCO3 excretion enhances salt reabsorption independent of plasma pH makes it probable that the excretion of N is the chief function of the ammonia mechanism and that salt conservation is incidental. Insulin decreased the plasma amino acid level and drastically reduced the NH3 excretion. With the decrease in ammonia, NaCl and NaHCO3 were excreted in increased amounts.

Improved function with amino acids in the isolated perfused kidney

1982 ◽  
Vol 243 (3) ◽  
pp. F284-F292 ◽  
Author(s):  
F. H. Epstein ◽  
J. T. Brosnan ◽  
J. D. Tange ◽  
B. D. Ross
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Glutathione Depletion ◽  
Sodium Reabsorption ◽  
Thick Ascending Limb ◽  
Amino Acid Supplementation ◽  
Renal Structure ◽  
Improved Function ◽  
And Function ◽  
Renal Concentrating Capacity

When isolated rat kidneys are perfused with glucose as the only substrate, there is a progressive diminution in glomerular filtration rate and fractional reabsorption of sodium. This is most marked after 1 h. Renal glutathione content rapidly falls and is less than 30% of control levels after 1 h. Renal concentrating ability is markedly impaired and structural lesions are consistently observed in cells lining the thick ascending limb of Henle's loop. Addition of 20 physiologic amino acids including cysteine to the perfusate prevents the fall in renal glutathione, prevents the anatomical damage to ascending limb cells, permits GFR and fractional sodium reabsorption to remain high and close to their initial levels for as long as 4 h, and improves renal concentrating capacity. If amino acid supplementation is limited to three precursors of glutathione--cysteine, glycine, and glutamic acid--renal glutathione content is preserved and concentrating ability is improved, but GFR and fractional sodium reabsorption are not maintained as well as with comprehensive amino acid supplements. The results suggest that amino acid deficiency and glutathione depletion may contribute to disturbances in renal structure and function.

scholarly journals 60 YEARS OF POMC: Lipotropin and beta-endorphin: a perspective

2016 ◽  
Vol 56 (4) ◽  
pp. T13-T25 ◽  
Author(s):  
D G Smyth
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Analysis ◽  
Structure And Function ◽  
Biologically Active ◽  
Molecular Endocrinology ◽  
And Function ◽  
The Brain ◽  
Quantitative Amino Acid Analysis

Many important fields of research had a humble origin. In the distant past, A J P Martin’s discovery that amino acids could be separated by paper chromatography and Moore and Stein’s use of columns for quantitative amino acid analysis provided the first steps towards the determination of structure in complex biologically active molecules. They opened the door to reveal the essential relationship that exists between structure and function. In molecular endocrinology, for example, striking advances have been made by chemists with their expertise in the identification of structure working with biologists who contributed valuable knowledge and experience. Advantage was gained from the convergence of different background, and it is notable that the whole is greater than the sum. In the determination of structure, it may be recalled that four of the world’s great pioneers (Archibald Martin, Rodney Porter, Fred Sanger and Vincent du Vigneaud) were acknowledged for their fundamental contributions when individually they were awarded the Nobel Prize. They foresaw that the identification of structure would prove of outstanding importance in the future. Indeed, study of the structures of β-endorphin and enkephalin and the different forms of opiate activity they engender has led to a transformation in our understanding of chemical transmission in the brain.

scholarly journals Amino Acid Metabolism in Human Embryos

2016 ◽  
pp. 823-832 ◽  
Author(s):  
P. DRÁBKOVÁ ◽  
L. ANDRLOVÁ ◽  
R. HAMPL ◽  
R. KANĎÁR
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Metabolism ◽  
Culture Medium ◽  
Acid Metabolism ◽  
Culture Media ◽  
Time Lapse ◽  
Human Embryos ◽  
Strongly Correlated ◽  
Cell Stage

The aim of this study was to find some relationship between amino acid metabolism and the embryo morphokinetic parameters studied via time-lapse analysis. Study included 48 human embryo samples and their culture media. Two groups of embryos were identified: embryos reached the 8-cell stage on day 3 (n=34) and embryos failed to develop at any point during the incubation (n=14). Amino acids levels were measured on day 3 of embryo development; using time-lapse analysis, the precise timing of embryo cleavage, synchrony of division, grade of fragmentation etc. were established. No statistically significant differences between dividing and arresting embryos were observed in terms of amino acids production/consumption and turnover. Amino acids which were part of the culture medium did not exhibit any statistically significant correlation with kinetic parameters with the exception of the grade of fragmentation on day 3; there were negative correlation with glutamate, and positive with glutamine, glycine and taurine. In some dividing and in some arresting embryos appeared new amino acids which strongly correlated with each other, with methionine, but not with any other amino acid that is a regular part of the culture medium.

Utilization of amino acids by Trypanosoma brucei in culture: L-threonine as a precursor for acetate

Parasitology ◽  
1975 ◽  
Vol 71 (2) ◽  
pp. 311-326 ◽  
Author(s):  
G. A. M. Cross ◽  
R. A. Klein ◽  
D. J. Linstead
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Trypanosoma Brucei ◽  
Potent Inhibitor ◽  
Culture Media ◽  
Growth Cycle ◽  
Defined Medium ◽  
Amino Acid Compositions

The amino acid compositions of several culture media have been analysed and compared. The utilization and excretion of amino acids and other metabolites have been followed during growth of Trypanosoma brucei S42 in a defined medium. All of the added L-threonine was metabolized by the cells, even when it was present at elevated concentrations. Glucose was consumed throughout the growth cycle: glutamine was consumed more rapidly than glutamic acid, which was itself used at about the same rate as proline. Threonine was cleaved to form glycine and acetate, both of which accumulated in the medium. Alanine and succinate were excreted together with a small amount of pyruvate, but these three products accounted for less than half of the glucose used. CO2 production from glucose was not measured, but insignificant amounts of CO2 were produced from threonine. Tetraethylthiuram disulphide blocked the cleavage of threonine and was a potent inhibitor of trypanosome growth.

scholarly journals Cysteine in Broiler Poultry Nutrition

2021 ◽  
Author(s):  
Iyakutye Jacob Nte ◽  
Hollinshead Holly Gunn
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequences ◽  
Broiler Chicks ◽  
Feed Ingredients ◽  
Amino Acid Requirements ◽  
Protein Amino Acids ◽  
Poultry Diets ◽  
Soya Bean Meal ◽  
And Function

The SAAs are limiting in the major poultry feed ingredients, ranking first and fifth in soya bean meal and maize, respectively. Feed ingredients rich in protein, in particular and other nutrients, enhance Energy supply and protein accretion. Modern commercial broilers have reduced maintenance needs and high amino acid requirements, and are more responsive to protein (amino acids) than energy. Cysteine is a semi-essential amino acid belonging to the SAAs. It plays essential roles in protein synthesis, structure and function, causing growth depressing effects in broiler chicks when there is methionine:cysteine imbalance. Genetically predetermined amino acid sequences in proteins are essential for production of adequate quantities of meat, milk and eggs. Therefore, ideal amino acid ratios which conform to the requirements of broilers should be utilized. In nutrition, amino acids are equivalent to proteins, hence the shift in focus from proteins to individual amino acids, expressed as ideal ratios to lysine. The SAAs are practically relevant and have critical nutritional roles in animal nutrition with over 90% production being used to fortify animal (particularly poultry) diets. A balance in the methionine:cysteine ratio is necessary to ensure efficient utilization of the SAAs for proper growth and development in broiler poultry.

scholarly journals Membrane barrels are taller, fatter, inside-out soluble barrels

2021 ◽  
Author(s):  
Rik Dhar ◽  
Ryan Feehan ◽  
Joanna S.G. Slusky
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Outer Membrane ◽  
Acid Composition ◽  
Relative Size ◽  
And Function ◽  
Inside Out ◽  
Insight Into ◽  
Regular Alternation

AbstractUp-and-down β-barrel topology exists in both the membrane and soluble environment. However, β-barrels are virtually the only topology that exist in the outer membrane. By comparing features of these structurally similar proteins, we can determine what features are particular to the environment rather than the fold. Here we compare structures of membrane β-barrels to soluble β-barrels and evaluate their relative size, shape, amino acid composition, hydrophobicity, and periodicity. We find that membrane β-barrels are generally larger than soluble β-barrels in with more strands per barrel and more amino acids per strand, making them wider and taller. We also find that membrane β-barrels are inside-out soluble β-barrels. The inward region of membrane β-barrels have similar hydrophobicity to the outward region of soluble β-barrels, and the outward region of membrane β-barrels has similar hydrophobicity to the inward region of the soluble β-barrels. Moreover, even though both types of β-barrel have been assumed to have strands with amino acids that alternate in direction and hydrophobicity, we find that the membrane β-barrels have more regular alternation than soluble β-barrels. These features give insight into how membrane barrels maintain their fold and function in the membrane.

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