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Serglycin Is Implicated in the Promotion of Aggressive Phenotype of Breast Cancer Cells

Korpetinou, Angeliki ; Skandalis, Spyros S. ; Moustakas, Aristidis ; Happonen, Kaisa LU ; Tveit, Heidi ; Prydz, Kristian ; Labropoulou, Vassiliki T. ; Giannopoulou, Efstathia ; Kalofonos, Haralambos P. and Blom, Anna LU orcid , et al. (2013) In PLoS ONE 8(10).
Abstract
Serglycin is a proteoglycan expressed by some malignant cells. It promotes metastasis and protects some tumor cells from complement system attack. In the present study, we show for the first time the in situ expression of serglycin by breast cancer cells by immunohistochemistry in patients' material. Moreover, we demonstrate high expression and constitutive secretion of serglycin in the aggressive MDA-MB-231 breast cancer cell line. Serglycin exhibited a strong cytoplasmic staining in these cells, observable at the cell periphery in a thread of filaments near the cell membrane, but also in filopodia-like structures. Serglycin was purified from conditioned medium of MDA-MB-231 cells, and represented the major proteoglycan secreted by these... (More)
Serglycin is a proteoglycan expressed by some malignant cells. It promotes metastasis and protects some tumor cells from complement system attack. In the present study, we show for the first time the in situ expression of serglycin by breast cancer cells by immunohistochemistry in patients' material. Moreover, we demonstrate high expression and constitutive secretion of serglycin in the aggressive MDA-MB-231 breast cancer cell line. Serglycin exhibited a strong cytoplasmic staining in these cells, observable at the cell periphery in a thread of filaments near the cell membrane, but also in filopodia-like structures. Serglycin was purified from conditioned medium of MDA-MB-231 cells, and represented the major proteoglycan secreted by these cells, having a molecular size of similar to 250 kDa and carrying chondroitin sulfate side chains, mainly composed of 4-sulfated (similar to 87%), 6-sulfated (similar to 10%) and non-sulfated (similar to 3%) disaccharides. Purified serglycin inhibited early steps of both the classical and the lectin pathways of complement by binding to C1q and mannose-binding lectin. Stable expression of serglycin in less aggressive MCF-7 breast cancer cells induced their proliferation, anchorage-independent growth, migration and invasion. Interestingly, over-expression of serglycin lacking the glycosaminoglycan attachment sites failed to promote these cellular functions, suggesting that glycanation of serglycin is a pre-requisite for its oncogenic properties. Our findings suggest that serglycin promotes a more aggressive cancer cell phenotype and may protect breast cancer cells from complement attack supporting their survival and expansion. (Less)
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
PLoS ONE
volume
8
issue
10
article number
e78157
publisher
Public Library of Science (PLoS)
external identifiers
  • wos:000326373800014
  • scopus:84893671911
  • pmid:24205138
ISSN
1932-6203
DOI
10.1371/journal.pone.0078157
language
English
LU publication?
yes
id
4b0fe2ae-9d8d-4ef9-8094-5dd3dde505c4 (old id 4205368)
date added to LUP
2016-04-01 13:53:49
date last changed
2022-05-19 21:42:00
@article{4b0fe2ae-9d8d-4ef9-8094-5dd3dde505c4,
  abstract     = {{Serglycin is a proteoglycan expressed by some malignant cells. It promotes metastasis and protects some tumor cells from complement system attack. In the present study, we show for the first time the in situ expression of serglycin by breast cancer cells by immunohistochemistry in patients' material. Moreover, we demonstrate high expression and constitutive secretion of serglycin in the aggressive MDA-MB-231 breast cancer cell line. Serglycin exhibited a strong cytoplasmic staining in these cells, observable at the cell periphery in a thread of filaments near the cell membrane, but also in filopodia-like structures. Serglycin was purified from conditioned medium of MDA-MB-231 cells, and represented the major proteoglycan secreted by these cells, having a molecular size of similar to 250 kDa and carrying chondroitin sulfate side chains, mainly composed of 4-sulfated (similar to 87%), 6-sulfated (similar to 10%) and non-sulfated (similar to 3%) disaccharides. Purified serglycin inhibited early steps of both the classical and the lectin pathways of complement by binding to C1q and mannose-binding lectin. Stable expression of serglycin in less aggressive MCF-7 breast cancer cells induced their proliferation, anchorage-independent growth, migration and invasion. Interestingly, over-expression of serglycin lacking the glycosaminoglycan attachment sites failed to promote these cellular functions, suggesting that glycanation of serglycin is a pre-requisite for its oncogenic properties. Our findings suggest that serglycin promotes a more aggressive cancer cell phenotype and may protect breast cancer cells from complement attack supporting their survival and expansion.}},
  author       = {{Korpetinou, Angeliki and Skandalis, Spyros S. and Moustakas, Aristidis and Happonen, Kaisa and Tveit, Heidi and Prydz, Kristian and Labropoulou, Vassiliki T. and Giannopoulou, Efstathia and Kalofonos, Haralambos P. and Blom, Anna and Karamanos, Nikos K. and Theocharis, Achilleas D.}},
  issn         = {{1932-6203}},
  language     = {{eng}},
  number       = {{10}},
  publisher    = {{Public Library of Science (PLoS)}},
  series       = {{PLoS ONE}},
  title        = {{Serglycin Is Implicated in the Promotion of Aggressive Phenotype of Breast Cancer Cells}},
  url          = {{https://lup.lub.lu.se/search/files/3652949/4359141}},
  doi          = {{10.1371/journal.pone.0078157}},
  volume       = {{8}},
  year         = {{2013}},
}