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- W566985514 abstract "Mammary epithelial cells secrete milk constituents by several routes. Milk lipid is enveloped by a milk fat globule membrane (MFGM) derived from the apical cell surface, and contains some of its constituent proteins. Soluble milk proteins are secreted by exocytosis. Some studies suggest these pathways are controlled independently, and may therefore provide a way to control milk composition. We propose to study secretion of the aqueous and lipid constituents of milk by comparing the secretion of butyrophilin, the major MFGM protein, with that of casein, the most abundant soluble proteins, in cultures of bovine mammary epithelial cells. Mammary epithelial cells were prepared from tissue of non-lactating, late-pregnant cows by collagenase digestion and density gradient centrifugation, and stored in liquid nitrogen. Cryopreserved cells were cultured initially on tissue culture plastic, then transferred to a reconstituted basement membrane (EHS matrix) and cultured in serum-free medium containing lactogenic hormones. On EHS matrix, cells formed multicellular structures covered in matrix (“mammospheres“), and secreted casein and butyrophilin. Unlike murine mammospheres, bovine mammospheres did not contain one central luminal space, and immunohistochemistry showed milk proteins distributed between the cells. Immunoblotting showed casein and butyrophilin present in both culture medium and an EGTA extract of luminal proteins. However, the results show that bovine mammary epithelialcells differentiate and secrete both soluble and MFGM proteins in primary culture, making this system suitable for study of control of mammary secretory pathways." @default.
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- W566985514 date "2006-03-11" @default.
- W566985514 modified "2023-10-16" @default.
- W566985514 title "Milk Secretion in Cultured Mammary Epithelial Cells" @default.
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- W566985514 doi "https://doi.org/10.1007/0-306-46865-4_25" @default.
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