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The effects of trimethyltin on the Ca+2, Mg+2 and Ca+2 + Mg+2-dependent ATPases of human neuroblastoma GM 3320. 1987

J P Chambers, and E Rizopoulos, and D L Armstrong, and M J Wayner, and J J Valdes

Data presented here indicate neuroblastoma GM 3320 tissue homogenates exhibit ouabain insensitive Ca+2-dependent, Mg+2-independent, Mg+2-dependent, Ca+2-independent and Ca+2 + Mg+2-dependent ATPase activities. Inclusion of trimethyltin in homogenate preparations of these cells appears to discriminate between these various ATPase activities. At low concentrations (25 microM), trimethyltin preferentially stimulated the Ca+2-dependent, Mg+2-independent ATPase activity while inhibiting the Ca+2 + Mg+2-ATPase activity approximately 70%. At 75 microM trimethyltin, the Ca+2 + Mg+2-dependent ATPase activity is inhibited greater than 95% while the Ca+2-dependent, Mg+2-independent activity is essentially unchanged from control activity and the Mg+2-dependent, Ca+2-independent activity is inhibited approximately 50%. At concentrations greater than 75 microM, trimethyltin significantly inhibits the Ca+2-dependent, Mg+2-independent ATPase activity. Thus, at trimethyltin concentrations of 50-75 microM, preferential inhibition of the Mg+2-dependent, Ca+2-independent and Ca+2 + Mg+2-dependent ATPase activities of neuroblastoma GM 3320 is achieved.

UI MeSH Term Description Entries
D009447 Neuroblastoma A common neoplasm of early childhood arising from neural crest cells in the sympathetic nervous system, and characterized by diverse clinical behavior, ranging from spontaneous remission to rapid metastatic progression and death. This tumor is the most common intraabdominal malignancy of childhood, but it may also arise from thorax, neck, or rarely occur in the central nervous system. Histologic features include uniform round cells with hyperchromatic nuclei arranged in nests and separated by fibrovascular septa. Neuroblastomas may be associated with the opsoclonus-myoclonus syndrome. (From DeVita et al., Cancer: Principles and Practice of Oncology, 5th ed, pp2099-2101; Curr Opin Oncol 1998 Jan;10(1):43-51) Neuroblastomas
D002460 Cell Line Established cell cultures that have the potential to propagate indefinitely. Cell Lines,Line, Cell,Lines, Cell
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
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
D000252 Calcium-Transporting ATPases Cation-transporting proteins that utilize the energy of ATP hydrolysis for the transport of CALCIUM. They differ from CALCIUM CHANNELS which allow calcium to pass through a membrane without the use of energy. ATPase, Calcium,Adenosinetriphosphatase, Calcium,Ca(2+)-Transporting ATPase,Calcium ATPase,Calcium Adenosinetriphosphatase,Adenosine Triphosphatase, Calcium,Ca2+ ATPase,Calcium-ATPase,ATPase, Ca2+,ATPases, Calcium-Transporting,Calcium Adenosine Triphosphatase,Calcium Transporting ATPases,Triphosphatase, Calcium Adenosine
D014220 Trialkyltin Compounds Organometallic compounds which contain tin and three alkyl groups. Compounds, Trialkyltin
D014298 Trimethyltin Compounds Organic compounds composed of tin and three methyl groups. Affect mitochondrial metabolism and inhibit oxidative phosphorylation by acting directly on the energy conserving processes. Compounds, Trimethyltin
D017301 Ca(2+) Mg(2+)-ATPase An enzyme that catalyzes the hydrolysis of ATP and is activated by millimolar concentrations of either Ca(2+) or Mg(2+). Unlike CA(2+)-TRANSPORTING ATPASE it does not require the second divalent cation for its activity, and is not sensitive to orthovanadate. (Prog Biophys Mol Biol 1988;52(1):1). A subgroup of EC 3.6.1.3. ATPase, Calcium Magnesium,ATPase, Magnesium,Adenosinetriphosphatase, Calcium, Magnesium,Adenosinetriphosphatase, Magnesium,Calcium Magnesium ATPase,Calcium Magnesium Adenosinetriphosphatase,Magnesium ATPase,Magnesium Adenosinetriphosphatase,Adenosine Triphosphatase, Calcium, Magnesium,Adenosine Triphosphatase, Magnesium,Ca Mg-ATPase,Ca2+-Mg2+ ATPase,Calcium Magnesium Adenosine Triphosphatase,Mg2+-ATPase,Mg2+-Dependent ATPase,ATPase, Ca2+-Mg2+,ATPase, Mg2+-Dependent,Adenosinetriphosphatase, Calcium Magnesium,Ca Mg ATPase,Ca2+ Mg2+ ATPase,Magnesium Adenosine Triphosphatase,Mg2+ ATPase,Mg2+ Dependent ATPase

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