Biomaterial Database

[Tocopherol level and lipid peroxidation in Wistar rat tissues during adaptation to cold]. 1995

N G Kolosova, and A R Kolpakov, and L E Panin

The content of lipid peroxidation (LPO) products and tocopherol was studied in the plasma, adrenals, brown fat, heart, thymus, liver tissue, microsomes and mitochondria of Wistar rats in various periods of cold acclimation (+4 degrees C during 2, 5, 24 hours and 5, 10, 15, and 49 days). Within the first 24 hours of cold exposure, there were periods of low levels of LPO products which, as their following elevation, did not coincide in time both for various tissues and for subcellular structures. The liver was used as an example to show that the activity of glutathione reductase and glutathione peroxidase enhanced. The rats' adaptation to moderately low temperatures occurred with the stabilized LPO processes and elevated body's tissue tocopherol levels: in the first hours of exposure by mobilizing its endogenous stores, on long-term exposure by enhancing its utilization from the diet.

UI	MeSH Term	Description	Entries
D008099	Liver	A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.	Livers
D008297	Male		Males
D003080	Cold Temperature	An absence of warmth or heat or a temperature notably below an accustomed norm.	Cold,Cold Temperatures,Temperature, Cold,Temperatures, Cold
D005979	Glutathione Peroxidase	An enzyme catalyzing the oxidation of 2 moles of GLUTATHIONE in the presence of HYDROGEN PEROXIDE to yield oxidized glutathione and water.	Cytosolic Glutathione Peroxidase,Glutathione Lipoperoxidase,Selenoglutathione Peroxidase,Glutathione Peroxidase, Cytosolic,Lipoperoxidase, Glutathione,Peroxidase, Glutathione,Peroxidase, Selenoglutathione
D005980	Glutathione Reductase	Catalyzes the oxidation of GLUTATHIONE to GLUTATHIONE DISULFIDE in the presence of NADP+. Deficiency in the enzyme is associated with HEMOLYTIC ANEMIA. Formerly listed as EC 1.6.4.2.	Glutathione-Disulfide Reductase,Reductase, Glutathione,Reductase, Glutathione-Disulfide
D000222	Adaptation, Physiological	The non-genetic biological changes of an organism in response to challenges in its ENVIRONMENT.	Adaptation, Physiologic,Adaptations, Physiologic,Adaptations, Physiological,Adaptive Plasticity,Phenotypic Plasticity,Physiological Adaptation,Physiologic Adaptation,Physiologic Adaptations,Physiological Adaptations,Plasticity, Adaptive,Plasticity, Phenotypic
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D013347	Subcellular Fractions	Components of a cell produced by various separation techniques which, though they disrupt the delicate anatomy of a cell, preserve the structure and physiology of its functioning constituents for biochemical and ultrastructural analysis. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p163)	Fraction, Subcellular,Fractions, Subcellular,Subcellular Fraction
D014810	Vitamin E	A generic descriptor for all TOCOPHEROLS and TOCOTRIENOLS that exhibit ALPHA-TOCOPHEROL activity. By virtue of the phenolic hydrogen on the 2H-1-benzopyran-6-ol nucleus, these compounds exhibit varying degree of antioxidant activity, depending on the site and number of methyl groups and the type of ISOPRENOIDS.
D015227	Lipid Peroxidation	Peroxidase catalyzed oxidation of lipids using hydrogen peroxide as an electron acceptor.	Lipid Peroxidations,Peroxidation, Lipid,Peroxidations, Lipid