scholarly journals CREB/TRH pathway in the central nervous system regulates energy expenditure in response to deprivation of an essential amino acid

2014 ◽  
Vol 39 (1) ◽  
pp. 105-113 ◽  
Author(s):  
T Xia ◽  
Q Zhang ◽  
Y Xiao ◽  
C Wang ◽  
J Yu ◽  
...  
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Amino Acid ◽  
Energy Expenditure ◽  
Essential Amino Acid ◽  
The Central Nervous System

scholarly journals 5-Hydroxytryptamine, Glutamate, and ATP: Much More Than Neurotransmitters

2021 ◽  
Vol 9 ◽  
Author(s):  
Rafael Franco ◽  
Rafael Rivas-Santisteban ◽  
Jaume Lillo ◽  
Jordi Camps ◽  
Gemma Navarro ◽  
...  
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Immune System ◽  
Amino Acid ◽  
Essential Amino Acid ◽  
Mammalian Cells ◽  
G Protein Coupled Receptors ◽  
Ionotropic Receptors ◽  
The Central Nervous System ◽  
G Protein Coupled

5-hydroxytryptamine (5-HT) is derived from the essential amino acid L-tryptophan. Although the compound has been studied extensively for its neuronal handling and synaptic actions, serotonin 5-HT receptors can be found extra-synaptically and not only in neurons but in many types of mammalian cells, inside and outside the central nervous system (CNS). In sharp contrast, glutamate (Glu) and ATP are better known as metabolism-related molecules, but they also are neurotransmitters, and their receptors are expressed on almost any type of cell inside and outside the nervous system. Whereas 5-hydroxytryptamine and Glu are key regulators of the immune system, ATP actions are more general. 5-hydroxytryptamine, ATP and Glu act through both G protein-coupled receptors (GPCRs), and ionotropic receptors, i.e., ligand gated ion channels. These are the three examples of neurotransmitters whose actions as holistic regulatory molecules are briefly put into perspective here.

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.

scholarly journals The oligodendrocyte-myelin glycoprotein belongs to a distinct family of proteins and contains the HNK-1 carbohydrate.

1990 ◽  
Vol 110 (2) ◽  
pp. 471-479 ◽  
Author(s):  
D D Mikol ◽  
J R Gulcher ◽  
K Stefansson
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Amino Acid ◽  
Terminal Segment ◽  
Platelet Glycoprotein ◽  
Glycoprotein Ib ◽  
Attachment Sites ◽  
Initial Adhesion ◽  
The Central Nervous System ◽  
Oligodendrocyte Myelin Glycoprotein

The complete primary structure of the human oligodendrocyte-myelin glycoprotein (OMgp), a glycophospholipid-linked membrane protein of oligodendrocytes and central nervous system myelin, has been determined. The deduced amino acid sequence predicts a polypeptide of 433 amino acids which includes a 17-amino acid leader sequence. OMgp consists of four domains: (a) a short cysteine-rich motif at the NH2 terminus; (b) a series of tandem leucine-rich repeats (LRs) present in several other proteins where they may play roles in adhesion; (c) a serine/threonine-rich region that contains probable attachment sites for O-linked carbohydrates; and (d) a hydrophobic COOH-terminal segment that is likely to be cleaved concomitant with the attachment of lipid during biosynthesis of OMgp. OMgp shares the first three of its four domains with the platelet glycoprotein Ib, which is responsible for the initial adhesion of platelets to the exposed subendothelium during hemostasis. Together with glycoprotein Ib and several other proteins, OMgp belongs to a family of proteins that contain both an NH2-terminal cysteine-rich motif and an adjacent series of LRs. In addition, we report that a subpopulation of OMgp molecules contains the HNK-1 carbohydrate, which has been shown to mediate interactions among cells in the central nervous system.

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