Effect of triethyltin on Ca2+ movement in Madin–Darby canine kidney cells
Autor: | Jan Cr, Chen Wc, Chang Ht, Huang Jk, Jiann Bp, Chou Kj |
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Rok vydání: | 2002 |
Předmět: |
0301 basic medicine
medicine.medical_specialty Thapsigargin Fura-2 Health Toxicology and Mutagenesis Cell Culture Techniques Kidney Toxicology 03 medical and health sciences chemistry.chemical_compound Dogs 0302 clinical medicine Canine kidney Internal medicine medicine Animals Enzyme Inhibitors Dose-Response Relationship Drug 030102 biochemistry & molecular biology Madin Darby canine kidney cell General Medicine Cell biology Cytosol Endocrinology chemistry 030220 oncology & carcinogenesis Calcium Environmental Pollutants Triethyltin Compounds Ca2 signaling Signal Transduction Toxicant |
Zdroj: | Human & Experimental Toxicology. 21:457-462 |
ISSN: | 1477-0903 0960-3271 |
DOI: | 10.1191/0960327102ht276oa |
Popis: | The effects of the environmental toxicant, triethyltin, on Ca2 + mobilization in Madin–Darby canine kidney (MDCK) cells have been examined. Triethyltin induced an increase in cytosolic free Ca2 + levels ([Ca2 +]i) at concentrations larger than 2 mM in a concentrationdependent manner. Within 5 min, the [Ca2 +]i signal was composed of a gradual rise and a sustained phase. The [Ca2 +]i signal was partly reduced by removing extracellular Ca2 +. In Ca2 +-free medium, pretreatment with thapsigargin (1 mM), an endoplasmic reticulum Ca2 + pump inhibitor, reduced 50 mM triethyltin-induced [Ca2 +]i increase by 80%. Conversely, pretreatment with triethyltin abolished thapsigargin-induced Ca2 + release. Pretreatment with U73122 (2 mM) to inhibit phospholipase C-coupled inositol 1,4,5-trisphosphate formations failed to alter 50 mM triethyltin-induced Ca2 + release. Incubation with triethyltin at a concentration (1 mM) that did not increase basal [Ca2 +]i for 3 min did not alter ATP (10 mM)and bradykinin (1 mM)-induced [Ca2 +]i increases. Collectively, this study shows that triethyltin altered Ca2 + movement in renal tubular cells by releasing Ca2 + from multiple stores in an inositol 1,4,5-trisphosphate-independent manner, and by inducing Ca2 + influx. |
Databáze: | OpenAIRE |
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