Biochemical changes in the rat brain associated with dinitrophenol-induced brain edema. 1978

C T Dragomir, and D Alexianu, and D Ungureanu, and A Barbier, and I Dinu, and C Eşanu, and D T Stefánescu, and S Mihåileanu

The present paper was designed to the study of cerebral edema induced by intracarotid infusion of dinitrophenol. The determinations included variations in three lysosomal enzymes (acid phosphatase, cathepsin C and beta-glucuronidase), Na+-K+-ATP-ase, changes in cerebral RNA and protein concentrations and the synthesis of these macromolecules in vitro. In experimental brain edema a drastic drop in the activity of lysosomal enzymes took place. The acid phosphatase decreased to less than 30% of controls. Cathepsin C and beta-glucuronidase were reduced about 30% and 50% of control levels respectively. Protein concentration in the cerebral tissue also decreased by more than 50%. The concentration of RNA, RNA synthesis, and the level of Na+-K+-ATP-ase remained unchanged. Protein synthesis was stimulated by 75% (against controls). All these phenomena were suppressed when the animals subjected to the action of dinitrophenol were concomitantly treated with the antiacidotic substance, tris (hydroxymethyl) aminomethane.

UI MeSH Term Description Entries
D008247 Lysosomes A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured or undergoes MEMBRANE FUSION. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed). Autolysosome,Autolysosomes,Lysosome
D001921 Brain The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM. Encephalon
D001923 Brain Chemistry Changes in the amounts of various chemicals (neurotransmitters, receptors, enzymes, and other metabolites) specific to the area of the central nervous system contained within the head. These are monitored over time, during sensory stimulation, or under different disease states. Chemistry, Brain,Brain Chemistries,Chemistries, Brain
D001929 Brain Edema Increased intracellular or extracellular fluid in brain tissue. Cytotoxic brain edema (swelling due to increased intracellular fluid) is indicative of a disturbance in cell metabolism, and is commonly associated with hypoxic or ischemic injuries (see HYPOXIA, BRAIN). An increase in extracellular fluid may be caused by increased brain capillary permeability (vasogenic edema), an osmotic gradient, local blockages in interstitial fluid pathways, or by obstruction of CSF flow (e.g., obstructive HYDROCEPHALUS). (From Childs Nerv Syst 1992 Sep; 8(6):301-6) Brain Swelling,Cerebral Edema,Cytotoxic Brain Edema,Intracranial Edema,Vasogenic Cerebral Edema,Cerebral Edema, Cytotoxic,Cerebral Edema, Vasogenic,Cytotoxic Cerebral Edema,Vasogenic Brain Edema,Brain Edema, Cytotoxic,Brain Edema, Vasogenic,Brain Swellings,Cerebral Edemas, Vasogenic,Edema, Brain,Edema, Cerebral,Edema, Cytotoxic Brain,Edema, Cytotoxic Cerebral,Edema, Intracranial,Edema, Vasogenic Brain,Edema, Vasogenic Cerebral,Swelling, Brain
D002403 Cathepsins A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES. Cathepsin
D004140 Dinitrophenols Organic compounds that contain two nitro groups attached to a phenol.
D005966 Glucuronidase Endo-beta-D-Glucuronidase,Endoglucuronidase,Exo-beta-D-Glucuronidase,beta-Glucuronidase,Endo beta D Glucuronidase,Exo beta D Glucuronidase,beta Glucuronidase
D000135 Acid Phosphatase An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.2. Acid beta-Glycerophosphatase,Acid beta Glycerophosphatase
D000251 Adenosine Triphosphatases A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA. ATPases,Adenosinetriphosphatase,ATPase,ATPase, DNA-Dependent,Adenosine Triphosphatase,DNA-Dependent ATPase,DNA-Dependent Adenosinetriphosphatases,ATPase, DNA Dependent,Adenosinetriphosphatases, DNA-Dependent,DNA Dependent ATPase,DNA Dependent Adenosinetriphosphatases,Triphosphatase, Adenosine
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

Related Publications

C T Dragomir, and D Alexianu, and D Ungureanu, and A Barbier, and I Dinu, and C Eşanu, and D T Stefánescu, and S Mihåileanu
November 1981, Experimental eye research,
C T Dragomir, and D Alexianu, and D Ungureanu, and A Barbier, and I Dinu, and C Eşanu, and D T Stefánescu, and S Mihåileanu
December 1975, Journal of neurochemistry,
C T Dragomir, and D Alexianu, and D Ungureanu, and A Barbier, and I Dinu, and C Eşanu, and D T Stefánescu, and S Mihåileanu
May 1987, Neurologia medico-chirurgica,
C T Dragomir, and D Alexianu, and D Ungureanu, and A Barbier, and I Dinu, and C Eşanu, and D T Stefánescu, and S Mihåileanu
February 1967, Klinische Wochenschrift,
C T Dragomir, and D Alexianu, and D Ungureanu, and A Barbier, and I Dinu, and C Eşanu, and D T Stefánescu, and S Mihåileanu
January 1991, Roczniki Panstwowego Zakladu Higieny,
C T Dragomir, and D Alexianu, and D Ungureanu, and A Barbier, and I Dinu, and C Eşanu, and D T Stefánescu, and S Mihåileanu
May 1977, Biochemical pharmacology,
C T Dragomir, and D Alexianu, and D Ungureanu, and A Barbier, and I Dinu, and C Eşanu, and D T Stefánescu, and S Mihåileanu
March 1969, No to shinkei = Brain and nerve,
C T Dragomir, and D Alexianu, and D Ungureanu, and A Barbier, and I Dinu, and C Eşanu, and D T Stefánescu, and S Mihåileanu
January 2014, BioMed research international,
C T Dragomir, and D Alexianu, and D Ungureanu, and A Barbier, and I Dinu, and C Eşanu, and D T Stefánescu, and S Mihåileanu
April 1983, Neurochemical research,
C T Dragomir, and D Alexianu, and D Ungureanu, and A Barbier, and I Dinu, and C Eşanu, and D T Stefánescu, and S Mihåileanu
January 1982, Experimental brain research,
Copied contents to your clipboard!