scholarly journals INCREASED PEROXIDATIVE DAMAGE AND DECREASED PROTEIN SYNTHESIS ARE FEATURES OF AGING POTATO SEED-TUBERS.

HortScience ◽  
1992 ◽  
Vol 27 (6) ◽  
pp. 623g-624
Author(s):  
G.N.M Kumar ◽  
N.R. Knowles
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Free Amino Acids ◽  
Free Amino ◽  
Seed Tuber ◽  
Growth Potential ◽  
Potato Seed ◽  
Root Growth Potential ◽  
Peroxidative Damage ◽  
Seed Tubers

The physiological mechanisms leading to a decline in sprout-vigor, root growth potential and apical dominance during long-term aging of potato seed tubers are currently under investigation. Malondialdehyde (MDA) and ethane, products of peroxidative degradation of PUFA increase in seed-tuber tissues with advancing age (from 2 to 32 months of storage). MDA is known to react with free amino acids to produce lipofuscin-like fluorescent compounds (FC), which build-up in aging/senescent tissues of plants and animals. With advancing seed-tuber age, an increase in free amino acids, MDA and FC concentrations was evident. Moreover, high levels of MDA have been shown to reduce protein synthesis in both plant and animal cells. We therefore examined the extent to which seed-tuber age affects protein synthesizing capacity of tuber tissues during sprouting. Tissue disks from 6- and 18-mo-old seed-tubers at various stages of sprouting, were compared for their protein synthesizing ability by monitoring the incorporation of radiolabelled amino acids into TCA precipitable products. The rate of incorporation (dpm mg protein-1 min-1) was 1.8 to 5.4-fold higher in tissue from 6-mo-old, as compared to that from 18-mo-old seed tubers, at similar stages of sprout development. Loss in protein synthesizing ability (possibly due to direct peroxidative damage) may be an important factor contributing to loss of sprout-vigor from aged potato seed-tubers.

scholarly journals Amino acid regulation of synthesis of ribonucleic acid and protein in the liver of rats

1971 ◽  
Vol 124 (2) ◽  
pp. 385-392 ◽  
Author(s):  
R. W. Wannemacher ◽  
C. F. Wannemacher ◽  
M. B. Yatvin
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Free Amino Acids ◽  
Free Amino ◽  
Cellular Protein ◽  
Deficient Diet ◽  
Cellular Protein Content ◽  
Regulate Protein

Weanling (23-day-old) rats were fed on either a low-protein diet (6% casein) or a diet containing an adequate amount of protein (18% casein) for 28 days. Hepatic cells from animals fed on the deficient diet were characterized by markedly lower concentrations of protein and RNA in all cellular fractions as compared with cells from control rats. The bound rRNA fraction was decreased to the greatest degree, whereas the free ribosomal concentrations were only slightly less than in control animals. A good correlation was observed between the rate of hepatic protein synthesis in vivo and the cellular protein content of the liver. Rates of protein synthesis both in vivo and in vitro were directly correlated with the hepatic concentration of individual free amino acids that are essential for protein synthesis. The decreased protein-synthetic ability of the ribosomes from the liver of protein-deprived rats was related to a decrease in the number of active ribosomes and heavy polyribosomes. The lower ribosomal content of the hepatocytes was correlated with the decreased concentration of essential free amino acids. In the protein-deprived rats, the rate of accumulation of newly synthesized cytoplasmic rRNA was markedly decreased compared with control animals. From these results it was concluded that amino acids regulate protein synthesis (1) by affecting the number of ribosomes that actively synthesize protein and (2) by inhibiting the rate of synthesis of new ribosomes. Both of these processes may involve the synthesis of proteins with a rapid rate of turnover.

scholarly journals Pinocytosis and intracellular degradation of exogenous protein: modulation by amino acids.

1983 ◽  
Vol 96 (6) ◽  
pp. 1586-1591 ◽  
Author(s):  
J M Besterman ◽  
J A Airhart ◽  
R B Low ◽  
D E Rannels
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Free Amino Acids ◽  
Free Amino ◽  
De Novo ◽  
Serum Proteins ◽  
Fluid Phase ◽  
Cellular Protein ◽  
Intracellular Degradation ◽  
Exogenous Protein

Intracellular degradation of exogenous (serum) proteins provides a source of amino acids for cellular protein synthesis. Pinocytosis serves as the mechanism for delivering exogenous protein to the lysosomes, the major site of intracellular degradation of exogenous protein. To determine whether the availability of extracellular free amino acids altered pinocytic function, we incubated monolayers of pulmonary alveolar macrophages with the fluid-phase marker, [14C]sucrose, and we dissected the pinocytic process by kinetic analysis. Additionally, intracellular degradation of endogenous and exogenous protein was monitored by measuring phenylalanine released from the cell monolayers in the presence of cycloheximide. Results revealed that in response to a subphysiological level of essential amino acids or to amino acid deprivation, (a) the rate of fluid-phase pinocytosis increased in such a manner as to preferentially increase both delivery to and size of an intracellular compartment believed to be the lysosomes, (b) the degradation of exogenously supplied albumin increased, and (c) the fraction of phenylalanine derived from degradation of exogenous albumin and reutilized for de novo protein synthesis increased. Thus, modulation of the pinosome-lysosome pathway may represent a homeostatic mechanism sensitive to the availability of extracellular free amino acids.

scholarly journals The specific radioactivity of the precursor pool for estimates of the rate of protein synthesis (Short Communication)

1973 ◽  
Vol 134 (4) ◽  
pp. 1127-1130 ◽  
Author(s):  
Edward B. Fern ◽  
Peter J. Garlick
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Free Amino Acids ◽  
Free Amino ◽  
Short Communication ◽  
Specific Radioactivity ◽  
Precursor Pool

Infusion of rats with [U-14C]glycine resulted in labelling of glycine and serine in tissue proteins. The pattern of labelling in protein more nearly resembled that of the free amino acids in the tissue than in the plasma.

Autoradiographische Untersuchungen zur Proteinsynthese während der Frühentwicklung von Dermestes frischi (Coleoptera) / Autoradiographic Investigations on Protein Synthesis During Early Development of Dermestes frischi (Coleoptera)

1972 ◽  
Vol 27 (2) ◽  
pp. 193-195 ◽  
Author(s):  
H. W. Küthe
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Early Development ◽  
Free Amino Acids ◽  
Free Amino ◽  
Protein Fractions ◽  
Cleavage Stages ◽  
Cortical Regions

Injection of tritiated phenylalanine or leucine in eggs shortly after deposition shows the importance and use of free amino acids during cleavage stages. First the activity is found homogeneously distributed in the yolk system and ooplasm. In late cleavage stages the amino acids are incorporated into the periplasm of the egg. These results lead to the conclusions, that there is a continuous transfer of material out of the yolk system into cortical regions during cleavage. Secondly the first new synthetized protein fractions are located in the cortical ooplasm.

scholarly journals Ingestion of Free Amino Acids as Opposed to Intact Protein Increases Amino Acid Absorption but Does Not Further Augment Postprandial Muscle Protein Synthesis Rates

2020 ◽  
Vol 4 (Supplement_2) ◽  
pp. 673-673
Author(s):  
Michelle E G Weijzen ◽  
Rob JJ van Gassel ◽  
Imre W K Kouw ◽  
Stefan H M Gorissen ◽  
Marcel CG van de Poll ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Protein Digestion ◽  
Acid Absorption ◽  
Amino Acid Absorption

Abstract Objectives The rate of protein digestion and amino acid absorption determines the postprandial rise in circulating amino acids and, as such, modulates postprandial muscle protein synthesis rates. This study compares protein digestion and amino acid absorption kinetics and the subsequent muscle protein synthetic response following ingestion of intact protein versus an equivalent amount of free, crystalline amino acids. Methods Twenty-four healthy, young subjects (age: 22 ± 3 y, BMI: 23 ± 2 kg·m−2, sex: 12 M/12F) ingested 30 g intrinsically L-[1–13C]-phenylalanine and L-[1–13C]-leucine labeled milk protein (PROT; n = 12) or an equivalent amount of free amino acids (AA; n = 12). In addition, subjects received primed continuous L-[ring-2H5]-phenylalanine, L-[ring-3,5–2H2]-tyrosine, and L-[1–13C]-leucine infusions. Blood samples and muscle biopsies were obtained frequently to assess protein digestion and amino acid absorption kinetics and subsequent muscle protein synthesis rates over a 6 h postprandial period. An unpaired t-test was used to compare overall exogenous phenylalanine release in plasma. For other parameters repeated measures ANOVA were applied to determine differences between groups over time (time as within, and group as between-subjects factor). Data are expressed as mean ± SD. Results Postprandial plasma amino acid concentrations and exogenous phenylalanine appearance rates increased after ingestion of PROT and AA (both, P < 0.001), with a greater increase following ingestion of AA when compared to PROT (time*group interaction P < 0.001). Exogenous phenylalanine release in plasma assessed over the 6 h postprandial period, was greater in AA (76 ± 9%) compared with PROT (59 ± 10%; P < 0.001). Ingestion of AA and PROT strongly increased muscle protein synthesis rates based upon L-[ring-2H5]-phenylalanine (time effect P < 0.001), with no differences between groups (from 0.037 ± 0.015 to 0.053 ± 0.014%·h−1 and from 0.039 ± 0.016 to 0.051 ± 0.010%·h−1, respectively; time*group interaction P = 0.629). Conclusions Ingestion of free amino acids as opposed to intact milk protein is followed by more rapid amino acid absorption and greater postprandial plasma amino acid availability, but this does not further augment postprandial muscle protein synthesis rates. Funding Sources This research did not receive external funding.

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