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Expression
of Glycodelin in MCF-7 Breast Cancer Cells Induces Differentiation into
Organized Acinar Epithelium |
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Meerit KAdamAdarAdainen,
Markku SeppAdalAda, Ismo Virtanen, and Leif C. Andersson |
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Department
of Obstetrics and Gynecology (MK, MS), Helsinki University Central Hospital,
Department of Anatomy (IV), University of Helsinki, and Department of Pathology
(LCA), Haartman Institute, University of Helsinki, Helsinki, Finland |
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Glycodelin, a 28-kd human
glycoprotein found in glandular epithelial cells of endometrium and seminal
vesicle, was originally considered specific for the reproductive tract.
Glycodelin has significant amino-acid sequence homology with [beta]-lactoglobulins
from various species. We report herein the expression of glycodelin in normal
and neoplastic glandular epithelia outside the reproductive tract including
breast, sweat glands, parabronchial glands, hidradenoma, and pancreatic
cystadenoma. The localization of glycodelin in highly differentiated acinar
epithelia led us to investigate a possible role for glycodelin in epithelial
organization. Transfection of glycodelin cDNA into MCF-7 breast cancer cells
induced a dramatically altered growth behavior with formation of acinar
configurations and an inability to grow in semisolid media because of apoptosis.
The glycodelin-expressing cells also displayed strongly up-regulated expression
of markers of organized epithelia, such as cytokeratins 8 and 18 as well
as E-cadherin, and changes in intracellular distribution of [beta]-catenin.
The rate of proliferation was also suppressed. These results show that,
besides being a product of glandular epithelial cells, expression of glycodelin
is accompanied by the acquisition of a phenotype of organized glandular
epithelium |
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