NDLI: Loss of LARGE2 disrupts functional glycosylation of -dystroglycan in prostate cancer.

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Loss of LARGE2 disrupts functional glycosylation of -dystroglycan in prostate cancer.

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Loss of LARGE2 disrupts functional glycosylation of -dystroglycan in prostate cancer.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Cohen, Michael B. Beltran-valero De Bernabé, Daniel Henry, Michael D. Miller, Michael R. Huang, Qin Stipp, Christopher S. Campbell, Kevin P. Meier, Melissa M. Smith, Brian J. Lynch, Charles F. Esser, Alison K.
Description	Author Affiliation: Esser AK ( Department of Molecular Physiology and Biophysics, The Roy J. and Lucille A. Carver College of Medicine, University of Iowa, Iowa City, Iowa 52242, USA.)
Abstract	Dystroglycan (DG) is a cell surface receptor for extracellular matrix proteins and is involved in cell polarity, matrix organization, and mechanical stability of tissues. Previous studies documented loss of DG protein expression and glycosylation in a variety of cancer types, but the underlying mechanisms and the functional consequences with respect to cancer progression remain unclear. Here, we show that the level of expression of the ßDG subunit as well as the glycosylation status of the DG subunit inversely correlate with the Gleason scores of prostate cancers; furthermore, we show that the functional glycosylation of DG is substantially reduced in prostate cancer metastases. Additionally, we demonstrate that LARGE2 (GYLTL1B), a gene not previously implicated in cancer, regulates functional DG glycosylation in prostate cancer cell lines; knockdown of LARGE2 resulted in hypoglycosylation of DG and loss of its ability to bind laminin-111 while overexpression restored ligand binding and diminished growth and migration of an aggressive prostate cancer cell line. Finally, our analysis of LARGE2 expression in human cancer specimens reveals that LARGE2 is significantly down-regulated in the context of prostate cancer, and that its reduction correlates with disease progression. Our results describe a novel molecular mechanism to account for the commonly observed hypoglycosylation of DG in prostate cancer.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	4
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-01-25
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Dystroglycans Genetics Physiology Gene Expression Regulation, Neoplastic Glycosyltransferases Membrane Proteins Prostatic Neoplasms Metabolism Cell Line, Tumor Cell Movement Cell Proliferation Cell Separation Disease Progression Epithelium Extracellular Matrix Flow Cytometry Glycosylation Immunohistochemistry Laminin Microscopy, Fluorescence Neoplasm Invasiveness RNA, Small Interfering Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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