Hydroxy fatty acids from cerebrosides of the central nervous system: GLC determination and mass spectrometric identification

Lipids ◽  
1968 ◽  
Vol 3 (5) ◽  
pp. 431-438 ◽  
Author(s):  
P. Capella ◽  
C. Galli ◽  
R. Fumagalli
Keyword(s):  
Fatty Acids ◽  
Central Nervous System ◽  
Nervous System ◽  
Mass Spectrometric ◽  
Hydroxy Fatty Acids ◽  
Spectrometric Identification ◽  
Mass Spectrometric Identification ◽  
The Central Nervous System

scholarly journals Biological Chemistry in Intermediate Lipid Metabolism Disorder

2019 ◽  
Vol 70 (7) ◽  
pp. 2647-2651
Author(s):  
Alina Plesea Condratovici ◽  
Alina Mihaela Elisei ◽  
Decebal Vasincu ◽  
Iulian Dan Cuciureanu ◽  
Aurel Nechita ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Central Nervous System ◽  
Nervous System ◽  
Abdominal Cavity ◽  
Intestinal Wall ◽  
Pathological Process ◽  
The Body ◽  
Lipid Metabolism Disorder ◽  
Fat Deposits ◽  
The Central Nervous System

Any pathological process is accompanied by quantitative and qualitative changes in metabolism, which is the main form of life manifestation. Metabolism disorders (it is the permanent exchange of substances between the body and the environment) arise if the activity of the central nervous system is affected; the trophic function of the nervous system directs nutrition and metabolism. In this function, the coordinating role belongs to the central nervous system and is made by means of the endocrine glands. Lipids introduced into the body are digested mainly with the help of the pancreatic and intestinal juice and are resorbed through the walls of the small intestine. Even in the intestinal wall, the re-synthesis of fatty acids and glycerine fat occurs. A certain amount of neutral fat is probably resorbed without being split into fatty acids and glycerine. Fats are mainly resorbed through the lymphatic system, in part (about 30%) by means of the portal vein system; the entire fat emulsion penetrates into the blood and its main mass is deposited in certain fat deposits: the adipose subcutaneous cell tissue, the epiploon and the mesenterium of the abdominal cavity, as well as in the fatty layers of the various organs. In fat deposits, processes of lipid formation from carbohydrates and of transformation of higher fatty acids can occur. Lipids from fat deposits are subject to oxidation, especially at the liver level.

scholarly journals A biophysical study on molecular physiology of the uncoupling proteins of the central nervous system

2015 ◽  
Vol 35 (4) ◽  
Author(s):  
Tuan Hoang ◽  
Miljan Kuljanin ◽  
Matthew D. Smith ◽  
Masoud Jelokhani-Niaraki
Keyword(s):  
Escherichia Coli ◽  
Fatty Acids ◽  
Central Nervous System ◽  
Nervous System ◽  
Recombinant Protein Expression ◽  
Uncoupling Proteins ◽  
Molecular Physiology ◽  
Biophysical Study ◽  
The Central Nervous System ◽  
Self Association

Uncoupling proteins (UCP)2, UCP4 and UCP5 transport protons across the inner membrane of mitochondria in the central nervous system (CNS). Novel recombinant protein expression allowed expression of UCPs in Escherichia coli membranes. Functional neuronal UCPs formed multimers in membranes and interacted with various fatty acids (FAs) to transport protons. Self-association and unique ion transport properties of UCPs distinguish their physiological roles in the CNS.

Mass spectrometric identification of C20 fatty acids bovine lens using the pyrrolidide derivative

Lipids ◽  
1978 ◽  
Vol 13 (3) ◽  
pp. 190-194 ◽  
Author(s):  
Anthony J. Valicenti ◽  
Clifford J. Chapman ◽  
Ralph T. Holman ◽  
Jacques R. Chipault
Keyword(s):  
Fatty Acids ◽  
Mass Spectrometric ◽  
Bovine Lens ◽  
Spectrometric Identification ◽  
Mass Spectrometric Identification

scholarly journals Serotonin Promotes Serum Albumin Interaction with the Monomeric Amyloid β Peptide

2021 ◽  
Vol 22 (11) ◽  
pp. 5896
Author(s):  
Ekaterina A. Litus ◽  
Alexey S. Kazakov ◽  
Evgenia I. Deryusheva ◽  
Ekaterina L. Nemashkalova ◽  
Marina P. Shevelyova ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Central Nervous System ◽  
Nervous System ◽  
Serum Albumin ◽  
Quaternary Structure ◽  
Amyloid Β ◽  
Resonance Spectroscopy ◽  
Amyloid Β Peptide ◽  
Structural Differences ◽  
The Central Nervous System

Prevention of amyloid β peptide (Aβ) deposition via facilitation of Aβ binding to its natural depot, human serum albumin (HSA), is a promising approach to preclude Alzheimer’s disease (AD) onset and progression. Previously, we demonstrated the ability of natural HSA ligands, fatty acids, to improve the affinity of this protein to monomeric Aβ by a factor of 3 (BBRC, 510(2), 248–253). Using plasmon resonance spectroscopy, we show here that another HSA ligand related to AD pathogenesis, serotonin (SRO), increases the affinity of the Aβ monomer to HSA by a factor of 7/17 for Aβ40/Aβ42, respectively. Meanwhile, the structurally homologous SRO precursor, tryptophan (TRP), does not affect HSA’s affinity to monomeric Aβ, despite slowdown of the association and dissociation processes. Crosslinking with glutaraldehyde and dynamic light scattering experiments reveal that, compared with the TRP-induced effects, SRO binding causes more marked changes in the quaternary structure of HSA. Furthermore, molecular docking reveals distinct structural differences between SRO/TRP complexes with HSA. The disintegration of the serotonergic system during AD pathogenesis may contribute to Aβ release from HSA in the central nervous system due to impairment of the SRO-mediated Aβ trapping by HSA.

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