Stimulation of pancreatic growth by intraduodenal amino acids and HCl

1980 ◽  
Vol 239 (5) ◽  
pp. G400-G405
Author(s):  
L. R. Johnson ◽  
S. J. Dudrick ◽  
P. D. Guthrie
Keyword(s):  
Amino Acids ◽  
Dna Synthesis ◽  
Protein Content ◽  
Infusion Rate ◽  
Exocrine Pancreas ◽  
The Other ◽  
Physiological Conditions ◽  
Pancreatic Growth ◽  
Set Up ◽  
Stimulation Of

Exogenous secretin and cholecystokinin (CCK) have been shown to stimulate the growth of the exocrine pancreas. To conclude that a hormone produces an effect under normal physiological conditions, one must demonstrate that the endogenous hormone also produces the action in question. To release endogenous secretin 0.01 N HCl was continuously infused into the duodenums of eight rats for 5 days. Sixteen animals were prepared with catheters inserted 1 cm below the pylorus. The other eight animals were infused with PO4 buffer, pH 7.5. The infusion rate for both groups was 2 ml/h. Animals were killed at the end of 5 days, and the oxyntic gland mucosa and pancreas were examined. Pancreatic weights, DNA synthesis, DNa, RNA, and protein content were significantly increased in rats receiving acid. An identical experiment was set up to release endogenous CCK. In this experiment eight rats received a solution containing 50 mM phenylalanine and 50 mM tryptophan. The controls received the caloric equivalent in glucose. At the end of 1 wk the pancreases of the rats infused with amino acids averaged 405 (P < 0.001) heavier than the controls. Similar increases occurred in DNA, RNA, and protein content. These studies suggest that endogenous secretin and CCK can be released in amounts sufficient to stimulate growth.

Effects of nitrogen rate and genotype on seed protein and amino acid content in canola

2015 ◽  
Vol 154 (3) ◽  
pp. 438-455 ◽  
Author(s):  
Q. S. ZUO ◽  
G. S. ZHOU ◽  
S. F. YANG ◽  
Y. YANG ◽  
L. R. WU ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Content ◽  
Seed Protein ◽  
Amino Acid Content ◽  
The Other ◽  
Seed Protein Content ◽  
Canola Seed ◽  
N Application ◽  
N Rates

SUMMARYCanola (Brassica napusL.) meal is widely used in animal feed as a protein source, and its quality relies on protein and amino acid content. However, little information is available regarding amino acid regulation in canola seed with nitrogen (N) application. The present study is aimed to evaluate the effect of N rate and genotype on canola seed amino acid concentrations under field conditions. A split-plot design comprising four N rates (0, 120, 240 and 360 kg N/ha) and three genotypes differing in seed protein content were used in 2010/11 and 2011/12. The results showed that increasing N rate decreased seed oil content linearly but increased seed protein content in all of the genotypes. The total amino acid concentration and absolute concentrations of individual amino acids in canola seed also improved significantly with the N rates in all of the genotypes. Regarding the proportions of amino acids, a group that included glutamic acid (Glu), proline (Pro) and arginine (Arg) dominated and occupied > 0·30 compared with other amino acids. The ratio of amino acids in this group increased by 8·3% with 360 kg N/ha compared with the control. However, the proportions of the other amino acids showed negative responses to the N rates. The results of regression analysis of the responses of individual amino acids to N rate indicated that Glu, Pro and Arg had a greater improvement potential with application of N fertilizer, as revealed by higher slopes in the linear equations compared with the other amino acids. Additionally, the concentrations of sulphur-containing amino acids, methionine and cysteine, were also a potential target for improving with N application because these are always deficient in major crops. In conclusion, N application cannot only improve seed protein content but also enhance deposition of amino acids such as Glu, Pro and Arg.

scholarly journals CCK-independent mTORC1 activation during dietary protein-induced exocrine pancreas growth

2010 ◽  
Vol 299 (5) ◽  
pp. G1154-G1163 ◽  
Author(s):  
Stephen J. Crozier ◽  
M. Dolors Sans ◽  
Jackie Y. Wang ◽  
Stephen I. Lentz ◽  
Stephen A. Ernst ◽  
...  
Keyword(s):  
Dna Synthesis ◽  
Dna Content ◽  
Dietary Protein ◽  
Exocrine Pancreas ◽  
Mammalian Target Of Rapamycin ◽  
High Protein ◽  
Pancreatic Growth ◽  
Total Dna ◽  
Mtorc1 Activation ◽  
Cck Release

Dietary protein can stimulate pancreatic growth in the absence of CCK release, but there is little data on the regulation of CCK-independent growth. To identify mechanisms whereby protein stimulates pancreatic growth in the absence of CCK release, C57BL/6 control and CCK-null male mice were fed normal-protein (14% casein) or high-protein (75% casein) chow for 7 days. The weight of the pancreas increased by 32% in C57BL/6 mice and 26% in CCK-null mice fed high-protein chow. Changes in pancreatic weight in control mice were due to both cell hypertrophy and hyperplasia since there was an increase in protein-to-DNA ratio, total DNA content, and DNA synthesis. In CCK-null mice pancreatic growth was almost entirely due to hypertrophy with both protein-to-DNA ratio and cell size increasing without significant increases in DNA content or DNA synthesis. ERK, calcineurin, and mammalian target of rapamycin complex 1 (mTORC1) are activated in models of CCK-induced growth, but there were no differences in ERK or calcineurin activation between fasted and fed CCK-null mice. In contrast, mTORC1 activation was increased after feeding and the duration of activation was prolonged in mice fed high-protein chow compared with normal-protein chow. Changes in pancreatic weight and RNA content were completely inhibited, and changes in protein content were partially abated, when the mTORC1 inhibitor rapamycin was administered during high-protein chow feeding. Prolonged mTORC1 activation is thus required for dietary protein-induced pancreatic growth in the absence of CCK.

Quine on Meaning and Translation

Philosophy ◽  
1979 ◽  
Vol 54 (209) ◽  
pp. 329-346
Author(s):  
D. E. Bolton
Keyword(s):  
The Other ◽  
Set Up ◽  
The One ◽  
Verbal Stimulation ◽  
Stimulation Of

In Word and Object Professor Quine formulated his Principle of Indeterminacy of Translation as follows:Manuals for translating one language into another can be set up in divergent ways, all compatible with the totality of speech dispositions, yet incompatible with one another. In countless places they will diverge in giving, as their respective translations of a sentence of the one language, sentences of the other language which stand to each other in no plausible sort of equivalence however loose. The firmer the direct links of a sentence with non-verbal stimulation, of course, the less drastically its translations can diverge from one another from manual to manual.

Studies on the responses of the female Aedes Mosquito. X.—Comparison of oestrogens and amino acids as attractants

1964 ◽  
Vol 55 (3) ◽  
pp. 395-403 ◽  
Author(s):  
P. Roessler ◽  
A. W. A. Brown
Keyword(s):  
Amino Acids ◽  
Aedes Aegypti ◽  
The Other ◽  
Aedes Mosquito ◽  
Free Flight ◽  
Flight Cage ◽  
Stimulation Of

The attractiveness of oestriol and of a sample L-lysine to females of Aedes aegypti (L.) was tested (a) in an olfactometer of the Wieting-Hoskins type, and (b) in a free-flight cage enclosed in glass. Similar results were given by both methods, L-lysine being the more attractive at higher concentrations, but oestriol retaining its attractiveness down to much lower concentrations. When 27 L-amino acids were tested in the free-flight cage, 16 showed significantly positive stimulation. Of these lysine was the most attractive, representing a group of 11 which carried CO2 in carbaminoyl or adsorbed form or in both; the other five, of which tyrosine was the most attractive, carried no CO2.

scholarly journals CELL DIVISION AND DNA SYNTHESIS IN TETRAHYMENA PYRIFORMIS DEPRIVED OF ESSENTIAL AMINO ACIDS

1964 ◽  
Vol 21 (2) ◽  
pp. 275-281 ◽  
Author(s):  
G. E. Stone ◽  
D. M. Prescott
Keyword(s):  
Amino Acids ◽  
Cell Division ◽  
Amino Acid ◽  
Dna Synthesis ◽  
Tetrahymena Pyriformis ◽  
Essential Amino Acids ◽  
The Other ◽  
Cent Increase ◽  
Amino Acid Requirements

The question of amino acid requirements for DNA synthesis and cell division has been studied in Tetrahymena pyriformis by depriving cells of histidine and tryptophan at defined stages in the interdivision interval. Deprivation any time before DNA synthesis does not prevent the initiation of such synthesis but completely inhibits the following division and limits the increase in DNA, as measured microspectrophotometrically, to 20 per cent. H3-thymidine added to the medium is not incorporated during the 20 per cent increase. Deprivation after DNA synthesis is initiated does not prevent the continuation (to completion) of DNA synthesis, and cell division ensues. H3-thymidine added to the medium under these conditions is incorporated into macronuclear DNA. The data indicate that some amino acid-dependent event occurs, about the time of the beginning of the DNA synthesis period, which is not essential for initiation of DNA synthesis but which is essential for the maintenance of synthesis once it has begun. These results are further discussed in terms of enzymes required to convert thymidine (and possibly the other three deoxyribonucleosides) to the immediate precursor of DNA synthesis.

The effect of ioxynil on the free amino acid and protein content of the leaves of tartary buckwheat and spring wheat

1968 ◽  
Vol 46 (1) ◽  
pp. 89-92
Author(s):  
David Paton ◽  
Saul Zalik
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Content ◽  
Free Amino Acid ◽  
Spring Wheat ◽  
Free Amino ◽  
The Other ◽  
Tartary Buckwheat ◽  
Other Hand ◽  
Protein Amino Acids

The effects of ioxynil on the free amino acid and protein content of the leaves of tartary buckwheat and wheat were compared 2 days after the seedlings were sprayed. Spring wheat showed little change in the overall concentration of either the soluble or protein amino acids. Tartary buck wheat, on the other hand, showed marked changes in the balance between soluble and protein amino acids.

Baclofen: effects on amino acid release

1978 ◽  
Vol 56 (1) ◽  
pp. 150-154 ◽  
Author(s):  
S. J. Potashner
Keyword(s):  
Amino Acids ◽  
Excitatory Amino Acids ◽  
The Other ◽  
Aminobutyric Acid ◽  
Nerve Terminals ◽  
Amino Butyric Acid ◽  
Acid Release ◽  
Afferent Terminals ◽  
Excitatory Transmitter ◽  
Stimulation Of

This study investigated the effects of the antispastic drug β-(p-chlorophenyl)-γ-amino-butyric acid (Baclofen) on the release of amino acids from slices of guinea pig cerebral cortex. Electrical stimulation of slices evoked the release of endogenous14C-labelled glutamate, aspartate, γ-aminobutyric acid (GABA), alanine, and threonine–serine–glutamine (labelled via metabolism of D-[U-14C]glucose), and of exogenous glutamate, aspartate, GABA, and α-aminoisobutyrate. The releases of endogenous14C-labelled glutamate, aspartate, and GABA were three to seven times larger than those of other amino acids. Baclofen (4 μM) inhibited the evoked release of endogenous 14C-labelled glutamate and aspartate by nearly 60%, that of endogenous14C-labelled threonine–serine–glutamine and alanine by 14–19%, but had no effect on that of endogenous14C-labelled GABA. The drug inhibited the evoked release of the exogenous amino acids by 25–32%. Baclofen doubled the incorporation of 14C from D-[U-14C]glucose into endogenous alanine but was without effect on either the incorporation of 14C into the other endogenous amino acids or the turnover of any of the endogenous14C-labelled amino acids. Because endogenous14C-labelled glutamate, aspartate, and GABA are probably released from nerve terminals, Baclofen selectively suppresses the release of excitatory amino acids from nerve terminals. Similarly, depression of the release of excitatory transmitter (presumably glutamate) from primary afferent terminals in the spinal cord may at least partly explain the antispastic action of Baclofen.

scholarly journals The Group I Strain of Streptococcus mutans, UA140, Produces Both the Lantibiotic Mutacin I and a Nonlantibiotic Bacteriocin, Mutacin IV

2001 ◽  
Vol 67 (1) ◽  
pp. 15-21 ◽  
Author(s):  
Fengxia Qi ◽  
Ping Chen ◽  
Page W. Caufield
Keyword(s):  
Amino Acids ◽  
Oral Cavity ◽  
Molecular Mass ◽  
Streptococcus Mutans ◽  
The Other ◽  
Physiological Conditions ◽  
Appl Environ ◽  
Gram Positive Bacteria ◽  
Group I ◽  
Processing Site

ABSTRACT Strains of Streptococcus mutans produce at least three mutacins, I, II, and III. Mutacin II is a member of subgroup AII in the lantibiotic family of bacteriocins, and mutacins I and III belong to subgroup AI in the lantibiotic family. In this report, we characterize two mutacins produced by UA140, a group I strain of S. mutans. One is identical to the lantibiotic mutacin I produced by strain CH43 (F. Qi et al., Appl. Environ. Microbiol. 66:3221–3229, 2000); the other is a nonlantibiotic bacteriocin, which we named mutacin IV. Mutacin IV belongs to the two-peptide, nonlantibiotic family of bacteriocins produced by gram-positive bacteria. Peptide A, encoded by gene nlmA, is 44 amino acids (aa) in size and has a molecular mass of 4,169 Da; peptide B, encoded bynlmB, is 49 aa in size and has a molecular mass of 4,826 Da. Both peptides derive from prepeptides with glycines at positions −2 and −1 relative to the processing site. Production of mutacins I and IV by UA140 appears to be regulated by different mechanisms under different physiological conditions. The significance of producing two mutacins by one strain under different conditions and the implication of this property in terms of the ecology of S. mutans in the oral cavity are discussed.

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