Uptake of transmitter amino acids by glial plasmalemmal vesicles from different regions of rat central nervous system

1994 ◽  
Vol 19 (9) ◽  
pp. 1145-1150 ◽  
Author(s):  
Yoichi Nakamura ◽  
Hirohiko Kubo ◽  
Kiyoshi Kataoka
Keyword(s):  
Amino Acids ◽  
Central Nervous System ◽  
Nervous System ◽  
Plasmalemmal Vesicles ◽  
Transmitter Amino Acids

Recent Advances in the Pharmacology of Excitatory Amino Acids in the Mammalian Central Nervous System

Excitotoxins ◽  
1983 ◽  
pp. 43-54 ◽  
Author(s):  
J. Davies ◽  
R. H. Evans ◽  
A. W. Jones ◽  
K. N. Mewett ◽  
D. A. S. Smith ◽  
...  
Keyword(s):  
Amino Acids ◽  
Central Nervous System ◽  
Nervous System ◽  
Excitatory Amino Acids ◽  
Mammalian Central Nervous System ◽  
Recent Advances

scholarly journals Inhibition of choline acetyltransferase by excitatory amino acids as a possible mechanism for cholinergic dysfunction in the central nervous system

2001 ◽  
Vol 77 (4) ◽  
pp. 1136-1144 ◽  
Author(s):  
Nelson E. Loureiro-dos-Santos ◽  
Ricardo A. M. Reis ◽  
Regina C. C. Kubrusly ◽  
Olga M. M. S. De Almeida ◽  
Patricia F. Gardino ◽  
...  
Keyword(s):  
Amino Acids ◽  
Central Nervous System ◽  
Nervous System ◽  
Choline Acetyltransferase ◽  
Excitatory Amino Acids ◽  
Cholinergic Dysfunction ◽  
The Central Nervous System

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.

FEATURES OF THE PRODUCTION TECHNOLOGY LOW-PROTEIN FOODS

2021 ◽  
Vol 14 (3(53)) ◽  
pp. 98-104
Author(s):  
Alexey Iosifovich Grigel
Keyword(s):  
Amino Acids ◽  
Central Nervous System ◽  
Nervous System ◽  
Life Support ◽  
Hereditary Disease ◽  
Bakery Products ◽  
Severe Damage ◽  
Low Protein ◽  
The Central Nervous System ◽  
Manufacturing Technologies

Phenylketonuria is a hereditary disease associated with a violation of the metabolism of amino acids, in particular phenylalanine. It is accompanied by the accumulation of phenylalanine and its toxic products in the tissues, which leads to severe damage to the central nervous system, manifested, in particular, in a violation of mental development. An important component of the life support of such patients is the observance of a low-protein diet. The article describes the features of manufacturing technologies for lowprotein products, including such as low-protein pasta and cereals, low-protein dry mixes, small-piece bakery products. The technological process and equipment for the production of low-protein products are described, as well as the characteristics of the intake range of products are given.

scholarly journals D-Serine in Neurobiology: CNS Neurotransmission and Neuromodulation

2014 ◽  
Vol 41 (2) ◽  
pp. 164-176 ◽  
Author(s):  
Sanaa K. Bardaweel ◽  
Muhammed Alzweiri ◽  
Aman A. Ishaqat
Keyword(s):  
Amino Acids ◽  
Central Nervous System ◽  
Human Physiology ◽  
Nervous System ◽  
Living Systems ◽  
Cns Development ◽  
Human Central Nervous System ◽  
High Affinity ◽  
Aspartate Receptor ◽  
Living Organisms

Homochirality is fundamental for life. L-Amino acids are exclusively used as substrates for the polymerization and formation of peptides and proteins in living systems. However, D- amino acids were recently detected in various living organisms, including mammals. Of these D-amino acids, D-serine has been most extensively studied. D-Serine was found to play an important role as a neurotransmitter in the human central nervous system (CNS) by binding to the N-methyl- D-aspartate receptor (NMDAr). D-Serine binds with high affinity to a co-agonist site at the NMDAr and, along with glutamate, mediates several vital physiological and pathological processes, including NMDAr transmission, synaptic plasticity and neurotoxicity. Therefore, a key role for D-serine as a determinant of NMDAr mediated neurotransmission in mammalian CNS has been suggested. In this context, we review the known functions of D-serine in human physiology, such as CNS development, and pathology, such as neuro-psychiatric and neurodegenerative diseases related to NMDAr dysfunction.

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