Mj. Page et al., Proteomic definition of normal human luminal and myoepithelial breast cells purified from reduction mammoplasties, P NAS US, 96(22), 1999, pp. 12589-12594
Citations number
49
Categorie Soggetti
Multidisciplinary
Journal title
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Normal human luminal and myoepithelial breast cells separately purified fro
m a set of 10 reduction mammoplasties by using a double antibody magnetic a
ffinity 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 identifie
d 170 proteins that were elevated 2-fold or more between the two breast cel
l 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 myo
epithelial 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 prot
ein expression map of the normal human breast and the basis for future stud
ies of purified breast cancer cells.