Proteomic definition of normal human luminal and myoepithelial breast cells purified from reduction mammoplasties

Martin J. Page, Bob Amess, R. Reid Townsend, Raj Parekh, Athula Herath, Luc Brusten, Marketa J. Zvelebil, Robert C. Stein, Michael D. Waterfield, Susan C. Davies, Michael J. O'Hare

Research output: Contribution to journalArticlepeer-review

183 Scopus citations

Abstract

Normal human luminal and myoepithelial breast cells separately purified from a set of 10 reduction mammoplasties by using a double antibody magnetic affinity cell sorting and Dynabead immunomagnetic technique were used in two- dimensional gel proteome studies. A total of 43,302 proteins were detected across the 20 samples, and a master image for each cell type comprising a total of 1,738 unique proteins was derived. Differential analysis identified 170 proteins that were elevated 2-fold or more between the two breast cell types, and 51 of these were annotated by tandem mass spectrometry. Muscle- specific enzyme isoforms and contractile intermediate filaments including tropomyosin and smooth muscle (SM22) alpha protein were detected in the myoepithelial cells, and a large number of cytokeratin subclasses and isoforms characteristic of luminal cells were detected in this cell type. A further 134 nondifferentially regulated proteins were also annotated from the two breast cell types, making this the most extensive study to date of the protein expression map of the normal human breast and the basis for future studies of purified breast cancer cells.

Original languageEnglish
Pages (from-to)12589-12594
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume96
Issue number22
DOIs
StatePublished - Oct 26 1999

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