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American Journal of Pathology, Vol 86, 123-131, Copyright © 1977 by American Society for Investigative Pathology

REGULAR ARTICLES

Glucose-6-phosphate dehydrogenase isoenzymes in acinar epithelial cells separated from the mammary gland of the rat at intervals during the course of lactation

MM Scalise, RB Thorp Jr, TG Pretlow 2d and TM Murad

Acinar epithelial cells were purifed from suspensions of cells from the lactating mammary glands of rats. As described previously, this purififaction was accomplished by sedimentation in an isokinetic gradient of Ficoll (polysucrose) in tissue culture medium, and the purity of the separated cells was established by electron microscopy and by histochemical markers. Isoenzymes of glucose-6-phosphate dehydrogenase were investigated at various intervals during lactation in separated populations of stromal and acinar cells. Acinar cells contained three- to eightfold more glucose-6-phosphate dehydrogenase activity than did stromal cells. The proportions of the respective isoenzymes varied during the course of lactation, and the observed changes were parallel in purified acinar cells and in the lactating mammary glands from which the cell suspensions were obtained. The availability of purified acinar cells in the investigation of interactions between hormones and cells from the mammary gland permits a greater degree of specificity than has been possible in the study of mammary cell suspensions which contain myoepithelial cells, duct cells, acinar cells, endothelial cells, fibroblasts, fat cells, mast cells, plasma cells, and blood cells.




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Copyright © 1977 by the American Society for Investigative Pathology.