Phosphorylation of myosin in mammary myoepithelial cells in response to oxytocin.
The response of mammary myoepithelial cells to oxytocin was studied by monitoring the level of phosphorylation of the 20,000 mol wt light chain of myosin. Myoepithelial cells were obtained by collagenase dispersion of involuted rat mammary tissue. The cells were equilibrated with [32P]orthophosphate, and then stimulated with oxytocin. Phosphorylated proteins were separated by polyacrylamide gel electrophoresis, and incorporation of 32P into the proteins was detected by autoradiography. Nanomolar concentrations of oxytocin caused a 3-fold increase in the level of phosphorylation of the myosin light chain within 0.5 min. When the cells were incubated with oxytocin in a calcium-free medium, there was only a transient phosphorylation of myosin. However, readdition of calcium to these cells resulted in phosphorylation of the myosin light chain. The results suggest that calcium is involved in the intracellular events following stimulation of the cells with oxytocin.
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D004848:Epithelium / Q000378:metabolism; D005260:Female; D008321:Mammary Glands, Animal / Q000187:drug effects / Q000378:metabolism*; D008970:Molecular Weight; D009218:Myosins / Q000378:metabolism*; D010121:Oxytocin / Q000494:pharmacology*; D010710:Phosphates / Q000378:metabolism; D010766:Phosphorylation; D051381:Rats
D010710:Phosphates; D010121:Oxytocin; D009218:Myosins; D002118:Calcium