Open Access

Erratum to: Breast cancer proteomics reveals correlation between estrogen receptor status and differential phosphorylation of PGRMC1

  • Hans Neubauer1,
  • Susan E Clare1, 2,
  • Wojciech Wozny3,
  • Gerhard P Schwall3,
  • Slobodan Poznanovic3,
  • Werner Stegmann3,
  • Ulrich Vogel4,
  • Karl Sotlar4, 5,
  • Diethelm Wallwiener1,
  • Raffael Kurek1, 6,
  • Tanja Fehm1 and
  • Michael A Cahill3, 7Email author
Breast Cancer Research200911:401

Published: 13 January 2009

The original article was published in Breast Cancer Research 2008 10:R85

Following the publication of our article [1] we noticed an error in the abstract, within the paragraph headed 'Results'. The serine residue, serine-181, referred to in this paragraph should be serine-180.

The paragraph should therefore read as follows:

Proteins significantly differentially abundant between estrogen receptor negative and estrogen receptor positive tumors at the 0.1% level were consistent with published profiles, suggesting an altered keratin pool, and increased inflammation and wound responses in estrogen receptor negative tumors. Two of three spots of PGRMC1 were more abundant in estrogen receptor negative tumors. Phosphatase treatment of breast tumor proteins indicated that the PGRMC1 isoforms differed in their phosphorylation status. Simultaneous mutation of PGRMC1 serine-56 and serine-180 fully abrogated the sensitivity of stably transfected MCF7 breast cancer cells to peroxide-induced cell death. Immune fluorescence revealed that PGRMC1 was primarily expressed in ER-negative basal epithelial cells of mammary ductules. Even in advanced tumors, high levels of ER or PGRMC1 were almost mutually exclusive in individual cells. In five out of five examined ductal in situ breast cancers of comedo type, PGRMC1 was expressed in glucose transporter 1 negative or positive poorly oxygenated cells surrounding the necrotic core, surrounded by a more distal halo of ER-positive cells.


Authors’ Affiliations

Department of Obstetrics and Gynecology, University of Tuebingen
Department of Surgery, Indiana University School of Medicine
ProteoSys AG, Carl-Zeiss-Straße
Department of Pathology, University of Tuebingen
Department of Pathology, Ludwig-Maximilians-University of Munich
Merck-Serono – Global Clinical Development Unit Oncology
School of Biomedical Sciences, Charles Sturt University


  1. Neubauer N, Clare SE, Wonzy W, Schwall GP, Poznanovic S, Stegmann W, Vogel U, Sotlar K, Wallwiener D, Kurek R, Fehm T, Cahill MA: Breast cancer proteomics reveals correlation between estrogen receptor status and differential phosphorylation of PGRMC1. Breast Cancer Research. 2008, 10: R85-10.1186/bcr2155.View ArticlePubMedPubMed CentralGoogle Scholar


© BioMed Central Ltd 2009