Effect of acute hypoxia in the antenatal period on uptake of labeled amino acids into rat brain proteins and tissue homogenates

1976 ◽  
Vol 82 (3) ◽  
pp. 1327-1329
Author(s):  
M. Ya. Maizelis ◽  
A. L. Zabludovskii
Keyword(s):  
Amino Acids ◽  
Rat Brain ◽  
Acute Hypoxia ◽  
Brain Proteins ◽  
Antenatal Period ◽  
Tissue Homogenates

Regulation of the post-translational conjugation of amino acids to rat brain proteins

Neuroscience ◽  
1990 ◽  
Vol 37 (1) ◽  
pp. 215-221 ◽  
Author(s):  
G. Chakraborty ◽  
J.A. Sturman ◽  
N.A. Ingoglia
Keyword(s):  
Amino Acids ◽  
Rat Brain ◽  
Brain Proteins

Movement of [U-14C]glucose Carbon into and Subsequent Release from lipids and High-Molecular-Weight Constituents of Rat Brain, Liver, and Heart In Vivo

1972 ◽  
Vol 50 (1) ◽  
pp. 91-105 ◽  
Author(s):  
R. Vrba ◽  
Anna Winter
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Rat Brain ◽  
High Molecular Weight ◽  
High Speed ◽  
Time Course ◽  
Specific Radioactivity ◽  
Brain Proteins ◽  
Glucose Carbon

After subcutaneous injection of [U-14C]glucose into rats the amount of 14C incorporated in vivo into proteins was always higher than into lipids in brain, liver, and heart. The specific radioactivity of brain proteins was higher than those of liver and heart. Blood-brain comparisons show that protein carbon is derived continuously from glucose in the brain in situ and not as a result of deposition of amino acids or proteins from the circulation. Seventy-two percent of 14C in purified brain protein fractions was found in the amino acids of the hydrolysates of these fractions, mainly in alanine, glutamic, and aspartic acids. Maximum labelling was reached about 4 h after injection of [U-14C]glucose. Elimination of 14C from three classes of brain proteins (high-speed supernatant, particulate deoxycholate extractable, and residual) followed a biphasic time-course. The extent of labelling of, and the rate of elimination of 14C from, the three classes of rat brain proteins were very similar. The fate of 14C in the other investigated tissue fractions of brain, liver, and heart was compared with the fate of 14C in brain proteins.The results lend further support to the previously published suggestion that: (a) brain does not contain appreciable amounts of metabolically inert proteins or of proteins with turnover rates significantly higher than the mean for the bulk of brain proteins; (b) glucose carbon participates at a different rate and to a different extent in the metabolism of high-molecular-weight constituents of brain as compared to liver, heart, and plasma proteins; (c) the continuous conversion of glucose carbon into protein is an important part of the maintenance of the homeostasis of tissue proteins in vivo.

Atypical amino acids inhibit histidine, valine, or lysine transport into rat brain

1983 ◽  
Vol 245 (4) ◽  
pp. R556-R563 ◽  
Author(s):  
J. K. Tews ◽  
A. E. Harper
Keyword(s):  
Amino Acids ◽  
Rat Brain ◽  
Blood Brain Barrier ◽  
Brain Slices ◽  
Aromatic Amino Acids ◽  
Brain Barrier ◽  
Basic Amino Acids ◽  
Large Neutral Amino Acids ◽  
Neutral Amino Acids ◽  
Single Meal

Transport of histidine, valine, or lysine into rat brain slices and across the blood-brain barrier (BBB) was determined in the presence of atypical nonprotein amino acids. Competitors of histidine and valine transport in slices were large neutral amino acids including norleucine, norvaline, alpha-aminooctanoate, beta-methylphenylalanine, and alpha-aminophenylacetate. Less effective were aromatic amino acids with ring substituents; ineffective were basic amino acids and omega-amino isomers of norleucine and aminooctanoate. Lysine transport was moderately depressed by homoarginine or ornithine plus arginine; large neutral amino acids were also similarly inhibitory. Histidine or valine transport across the BBB was also strongly inhibited by large neutral amino acids that were the most effective competitors in the slices (norvaline, norleucine, alpha-aminooctanoate, and alpha-aminophenylacetate); homoarginine and 8-aminooctanoate were ineffective. Homoarginine, ornithine, and arginine almost completely blocked lysine transport, but the large neutral amino acids were barely inhibitory. When rats were fed a single meal containing individual atypical large neutral amino acids or homoarginine, brain pools of certain large neutral amino acids or of arginine and lysine, respectively, were depleted.

Acute effects of aspartame on large neutral amino acids and monoamines in rat brain

Life Sciences ◽  
1983 ◽  
Vol 32 (14) ◽  
pp. 1651-1658 ◽  
Author(s):  
John D. Fernstrom ◽  
Madelyn H. Fernstrom ◽  
Marcia A. Gillis
Keyword(s):  
Amino Acids ◽  
Rat Brain ◽  
Acute Effects ◽  
Large Neutral Amino Acids ◽  
Neutral Amino Acids

scholarly journals Manganese Alters Rat Brain Amino Acids Levels

2012 ◽  
Vol 150 (1-3) ◽  
pp. 337-341 ◽  
Author(s):  
Dinamene Santos ◽  
M. Camila Batoreu ◽  
Isabel Almeida ◽  
Ruben Ramos ◽  
M. Sidoryk-Wegrzynowicz ◽  
...  
Keyword(s):  
Amino Acids ◽  
Rat Brain

Determination of amino acids in different regions of the rat brain application to the acute effects of tetrahydrocannabinol (THC) and trimethyltin (TMT)

Life Sciences ◽  
1988 ◽  
Vol 42 (20) ◽  
pp. 2029-2035 ◽  
Author(s):  
Ahmed H. Hikal ◽  
George W. Lipe ◽  
William Slikker ◽  
Andrew C. Scallet ◽  
Syed F. Ali ◽  
...  
Keyword(s):  
Amino Acids ◽  
Rat Brain ◽  
Acute Effects

RP-LC with Fluorescence Detection of Amino Acids in Rat Brain Synaptosomes

2011 ◽  
Vol 73 (1-2) ◽  
pp. 157-163 ◽  
Author(s):  
Xiaoyuan Mao ◽  
Yonggang Cao ◽  
Dongyu Min ◽  
Feng Guo ◽  
Ni Xie ◽  
...  
Keyword(s):  
Amino Acids ◽  
Rat Brain ◽  
Fluorescence Detection ◽  
Rat Brain Synaptosomes ◽  
Brain Synaptosomes

Effect of Cycloheximide on In Vitro and In Vivo Protein Synthesis by Certain Tissues of Rats and Pigeons with Special Reference to Muscle

1973 ◽  
Vol 51 (12) ◽  
pp. 933-941 ◽  
Author(s):  
Njanoor Narayanan ◽  
Jacob Eapen
Keyword(s):  
Amino Acids ◽  
Body Weight ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Incorporation ◽  
Contrast Administration ◽  
Acid Incorporation ◽  
Tissue Homogenates

The effect of cycloheximide in vitro and in vivo on the incorporation of labelled amino acids into protein by muscles, liver, kidneys, and brain of rats and pigeons was studied. In vitro incorporation of amino acids into protein by muscle microsomes, myofibrils, and myofibrillar ribosomes was not affected by cycloheximide. In contrast, administration of the antibiotic into intact animals at a concentration of 1 mg/kg body weight resulted in considerable inhibition of amino acid incorporation into protein by muscles, liver, kidneys, and brain. This inhibition was observed in all the subcellular fractions of these tissues during a period of 10–40 min after the administration of the precursor. Tissue homogenates derived from in vivo cycloheximide-treated animals did not show significant alteration in in vitro amino acid incorporation with the exception of brain, which showed a small but significant enhancement.

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