Studies on Amino Acids in Embryonic Tissue. I. L-Lanthionine, a Naturally Occurring Amino Acid in the Chick Embryo*

Biochemistry ◽  
1966 ◽  
Vol 5 (8) ◽  
pp. 2658-2665 ◽  
Author(s):  
N. H. Sloane ◽  
Karl G. Untch
2000 ◽  
Vol 167 (2) ◽  
pp. 247-252 ◽  
Author(s):  
H Wang ◽  
H Wolosker ◽  
J Pevsner ◽  
SH Snyder ◽  
DJ Selkoe

Little evidence is available for the physiological function of D-amino acids in species other than bacteria. Here we demonstrate that naturally occurring freed -aspartate (D-Asp) is present in all magnocellular neurons of rat hypothalamus. The levels of this naturally occurring D-amino acid were elevated during lactation and returned to normal thereafter in the magnocellular neurosecretory system, which produces oxytocin, a hormone responsible for milk ejection during lactation. Intraperitoneal injections of D-Asp reproducibly increased oxytocin gene expression and decreased the concentration of circulating oxytocin in vivo. Similar changes were observed in the vasopressin system. These results provide evidence for the role(s) of naturally occurring free D-Asp in mammalian physiology. The findings argue against the conventional concept that only L-stereoisomers of amino acids are functional in higher species.


Development ◽  
1958 ◽  
Vol 6 (2) ◽  
pp. 365-372
Author(s):  
C. H. Waddington ◽  
Margaret Perry

Several authors have studied the effects on developing embryos of substances which are analogues of naturally occurring amino-acids and purines, and known to act, in other systems, as metabolic inhibitors. It was emphasized by Waddington, Feldman, & Perry (1955) that any particular substance may exhibit very different effects in embryos of different types. They found, for instance, that the purine analogue 8-azaguanine has a very strong action in the chick and a much lesser one in the newt embryo. It is therefore necessary to consider the various classes of embryos separately. In this communication we shall be concerned only with chick embryos. Substances under test can be administered to such embryos by injection through the shell, as was done in the paper cited above With this technique it is impossible to know how much diffusion takes place of the substance injected, and one cannot therefore be certain of the effective concentration which actually reaches the embryo.


Development ◽  
1958 ◽  
Vol 6 (2) ◽  
pp. 262-269
Author(s):  
Phyllis W. Schultz ◽  
Heinz Herrmann

Amino acid analogues have been observed to give rise to abnormal forms of development of chick and amphibian embryos (Herrmann, 1953; Rothfels, 1954; Waddington & Sirlin, 1954; Feldman & Waddington, 1955; Herrmann, Rothfels-Konigsberg, & Curry, 1955). Assuming that these disturbances may be due to interference with the utilization of amino acids for protein formation, we have attempted an analysis of this effect by comparison of the protein contents and of the uptake of glycine into the proteins of chick embryo explants in the presence and absence of amino acid analogues. The results of such experiments are reported in this paper. The chick embryos used for explanation, the explantation technique, and the determination of total protein glycine and of tracer glycine were essentially the same as described previously (Herrmann & Schultz, 1958). The embryos were explanted at the 11–13 somite stage on to the surface of an agar gel containing egg extract as nutrient medium following the procedure given by Spratt (1947) as modified by Rothfels (1954).


1969 ◽  
Vol 114 (1) ◽  
pp. 97-105 ◽  
Author(s):  
G. G. Guidotti ◽  
Britta Lüneburg ◽  
A. F. Borghetti

1. The preparation of cell suspensions by treatment of chick embryo hearts with collagenase at various stages of development is described. 2. Measurements of oxygen consumption, incorporation of labelled leucine into protein and accumulation of labelled α-aminoisobutyric acid against a concentration gradient indicated a long-lasting viability of the isolated heart cells in vitro; a satisfactory preservation of subcellular structures, including plasma membrane, was assessed by electron-microscopic examination. 3. The rate of α-aminoisobutyric acid accumulation by cardiac cells isolated from hearts at different stages of embryological development decreased with aging; insulin stimulated the intracellular accumulation of this amino acid analogue. 4. Insulin increased the uptake by isolated heart cells of several 14C-labelled naturally occurring amino acids; however, the fraction of amino acid taken up by the cells that was recovered free intracellularly, and therefore the concentration ratio (between intracellular water and medium), was enhanced by the hormone only with glycine, proline, serine, threonine, histidine and methionine. When isolated heart cells were incubated in the presence of a mixture of labelled amino acids, the addition of insulin increased the disappearance of radioactivity from the medium. 5. The general pattern of amino acid transport (in the absence and in the presence of insulin) in isolated cardiac cells was similar to that found in intact hearts, suggesting that the biological preparation described in this paper might be useful for studies of cell permeability and insulin action.


1983 ◽  
Vol 210 (1) ◽  
pp. 99-105 ◽  
Author(s):  
M J Carroll ◽  
M Young

The relationship between placental protein synthesis and transfer of amino acids from mother to foetus was studied in the guinea pig, by using [U-14C]-lysine, -leucine, -glycine, -aspartate and -alpha-aminoisobutyrate. The uptake of label by protein was 12-16% of total label transferred. Cycloheximide inhibited incorporation of all naturally occurring amino acids into protein by 81-96% and transfer by 62-75%; the concentration of label in the free pool was increased for each. These findings were confirmed when specific-radioactivity measurements were made with L-[U-14C]lysine. The transfer of the non-protein amino acid alpha-aminoisobutyrate was not significantly decreased by cycloheximide. A model, linking protein synthesis to the generation of a transfer pool of amino acids, is proposed whereby inhibition of protein synthesis decreases the amount of amino acid available for transfer.


2006 ◽  
Vol 55 (7) ◽  
pp. 879-886 ◽  
Author(s):  
Hesham M. Al-Younes ◽  
Joscha Gussmann ◽  
Peter R. Braun ◽  
Volker Brinkmann ◽  
Thomas F. Meyer

The differential influence of individual amino acids on the growth of Chlamydia trachomatis versus Chlamydia (Chlamydophila) pneumoniae was investigated. Certain essential amino acids added in excess at the middle of the infection course resulted in varying degrees of abnormality in the development of the two species. If amino acids were added as early as 2 h post-infection, these effects were even more pronounced. The most effective amino acids in terms of C. trachomatis growth inhibition were leucine, isoleucine, methionine and phenylalanine. These amino acids elicited similar effects against C. pneumoniae, except methionine, which, surprisingly, showed a lower inhibitory activity. Tryptophan and valine marginally inhibited C. trachomatis growth and, paradoxically, led to a considerable enhancement of C. pneumoniae growth. On the other hand, some non-essential amino acids administered at the middle of or throughout the infection course differentially affected the development of the two species. For example, C. trachomatis growth was efficiently inhibited by glycine and serine, whereas C. pneumoniae was relatively less sensitive to these agents. Another difference was apparent for glutamate, glutamine and aspartate, which stimulated C. pneumoniae growth more than that of C. trachomatis. Overall, several distinctive patterns of susceptibility to excess amino acid levels were revealed for two representative C. trachomatis and C. pneumoniae isolates. Perturbation of amino acid levels, e.g. of leucine and isoleucine, might form a basis for the development of novel treatment or preventive regimens for chlamydial diseases.


1960 ◽  
Vol 37 (3) ◽  
pp. 435-443
Author(s):  
W. L. NICHOLAS ◽  
ELLSWORTH C. DOUGHERTY ◽  
EDER LINDSAY HANSEN ◽  
OSMUND HOLM-HANSEN ◽  
VIVIAN MOSES

1. The nematode, Caenorhabditis briggsae was cultured axenicaily in a mixture of chick embryo extract, autoclaved liver extract and sodium acetate-2-14C. A protein hydrolysate was prepared from the worms and the eggs which were collected from the cultures. 2. Chromatography and radioautography were carried out in a study of the amino acid composition of the hydrolysate. The following amino acids were found labelled: aspartic acid, glutamic acid, alanine, proline, glycine, serine. Cystein and cystine were oxidized to cysteic acid which was also labelled. The following amino acids were not labelled: arginine, histidine, lysine, methionine, threonine, tyrosine, valine and the combined spot representing phenylalanine, leucine and isoleucine. Tryptophane would have been destroyed by our method of hydrolysis. 3. Since the labelled amino acids are synthesized by the worm, it is suggested, tentatively, that they are not required in an otherwise adequate diet. So far as the unlabelled amino acids are concerned, it is suggested, on the basis of the results of certain culture experiments (published separately) that, with the probable exception of tyrosine, they are essential in the diet of C. briggsae.


1981 ◽  
Vol 199 (3) ◽  
pp. 547-555 ◽  
Author(s):  
J Y Chang ◽  
R Knecht ◽  
D G Braun

Amino acids labelled with dimethylaminoazobenzenesulphonyl chloride can be separated by reversed-phase high-pressure liquid chromatography and detected in the visible region (436 nm). All 19 naturally occurring amino acids can be separated on a Zorbax ODS column by employing two different gradient systems consisting of an acetonitrile/aqueous buffer mixture. As little as 2--5 pmol of an individual dimethylaminoazobenzenesulphonyl-amino acid can be quantitatively analysed with reliability, and only 10--30 ng of the dimethylaminoazobenzenesulphonylated protein hydrolysate is needed for each complete amino acid analysis. This new technique is as sensitive as any of the current amino acid analysis methods involving ion-exchange separation plus fluorescence detection, and is technically much simpler. By the combination of this sensitive amino acid-analysing technique with carboxypeptidase, we have been able to determine the C-terminal sequence of polypeptides at the picomole level.


2020 ◽  
Vol 117 (32) ◽  
pp. 19159-19167
Author(s):  
Jian Wang ◽  
Chenyi Li ◽  
Yusong Zou ◽  
Yajun Yan

Amino acids are naturally occurring and structurally diverse metabolites in biological system, whose potentials for chemical expansion, however, have not been fully explored. Here, we devise a metabolic platform capable of producing industrially important C3-C5 diols from amino acids. The presented platform combines the natural catabolism of charged amino acids with a catalytically efficient and thermodynamically favorable diol formation pathway, created by expanding the substrate scope of the carboxylic acid reductase toward noncognate ω-hydroxylic acids. Using the established platform as gateways, seven different diol-convertible amino acids are converted to diols including 1,3-propanediol, 1,4-butanediol, and 1,5-pentanediol. Particularly, we afford to optimize the production of 1,4-butanediol and demonstrate the de novo production of 1,5-pentanediol from glucose, with titers reaching 1.41 and 0.97 g l−1, respectively. Our work presents a metabolic platform that enriches the pathway repertoire for nonnatural diols with feedstock flexibility to both sugar and protein hydrolysates.


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