Biomaterial Database

The effect of intoxication by ceresan on the activity of phosphatases and esterases in the rat thalamus. 1980

J Wigowska-Sowińska

The effect of Ceresan (Methoxyethylmercury chloride) on the histoenzymatic pattern of the thalamus was studied. The experimental animals were treated intragastrically with 100 mg of Ceresan for 6 consecutive days, and the activity of various hydrolases of the thalamus was investigated histochemically. Ingestion of large doses of Ceresan caused widespread alterations in activity of the thalamic hydrolases. A generalized increase of activity was found with respect to TPPase, acP and NsE, while AChE, BuTJ and ATPase activities appeared distinctly reduced. The thalamic neuroglia of experimental rats demonstrated enzymic activities which could not be detected in control animals, and these were: AChE, NsE, acP and TPPase -- in astrocytes, and ATPase -- in oligodendroglia. The changes in the histoenzymatic pattern of the thalamus caused by Ceresan ingestion were topographically highly differentiated. The anterior and lateral nuclei of the thalamus seem to be more sensitive towards Ceresan intoxication than the posterior ones.

UI	MeSH Term	Description	Entries
D008767	Methylmercury Compounds	Organic compounds in which mercury is attached to a methyl group.	Methyl Mercury Compounds,Compounds, Methyl Mercury,Compounds, Methylmercury,Mercury Compounds, Methyl
D002091	Butyrylcholinesterase	An aspect of cholinesterase (EC 3.1.1.8).	Pseudocholinesterase,Benzoylcholinesterase,Butyrylthiocholinesterase
D004950	Esterases	Any member of the class of enzymes that catalyze the cleavage of an ester bond and result in the addition of water to the resulting molecules.	Esterase
D000110	Acetylcholinesterase	An enzyme that catalyzes the hydrolysis of ACETYLCHOLINE to CHOLINE and acetate. In the CNS, this enzyme plays a role in the function of peripheral neuromuscular junctions. EC 3.1.1.7.	Acetylcholine Hydrolase,Acetylthiocholinesterase,Hydrolase, Acetylcholine
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
D000255	Adenosine Triphosphate	An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.	ATP,Adenosine Triphosphate, Calcium Salt,Adenosine Triphosphate, Chromium Salt,Adenosine Triphosphate, Magnesium Salt,Adenosine Triphosphate, Manganese Salt,Adenylpyrophosphate,CaATP,CrATP,Manganese Adenosine Triphosphate,MgATP,MnATP,ATP-MgCl2,Adenosine Triphosphate, Chromium Ammonium Salt,Adenosine Triphosphate, Magnesium Chloride,Atriphos,Chromium Adenosine Triphosphate,Cr(H2O)4 ATP,Magnesium Adenosine Triphosphate,Striadyne,ATP MgCl2
D000469	Alkaline Phosphatase	An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.1.
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
D013788	Thalamus	Paired bodies containing mostly GRAY MATTER and forming part of the lateral wall of the THIRD VENTRICLE of the brain.	Thalamencephalon,Thalamencephalons