ArticleThe Journal of biological chemistry2012
HER-2/neu-mediated down-regulation of biglycan associated with altered growth properties.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
17 citing papers in PubMed, 28 citations in OpenAlex.
- The Landscape of Small Leucine-Rich Proteoglycan Impact on Cancer Pathogenesis with a Focus on Biglycan and Lumican.Cancers · 2023Review
- Biglycan as a potential regulator of tumorgenicity and immunogenicity in K-RAS-transformed cells.Oncoimmunology · 2022Article
- The Role of Decorin and Biglycan Signaling in Tumorigenesis.Frontiers in oncology · 2021Review
- Three-Dimensional Models as a New Frontier for Studying the Role of Proteoglycans in the Normal and Malignant Breast Microenvironment.Frontiers in cell and developmental biology · 2020Review
- Tumor-induced escape mechanisms and their association with resistance to checkpoint inhibitor therapy.Cancer immunology, immunotherapy : CII · 2019Review
- Nimodipine-Dependent Protection of Schwann Cells, Astrocytes and Neuronal Cells from Osmotic, Oxidative and Heat Stress Is Associated with the Activation of AKT and CREB.International journal of molecular sciences · 2019Article
- Up-regulation of Biglycan is Associated with Poor Prognosis and PTEN Deletion in Patients with Prostate Cancer.Neoplasia (New York, N.Y.) · 2017Article
- Biglycan expression in the melanoma microenvironment promotes invasiveness via increased tissue stiffness inducing integrin-β1 expression.Oncotarget · 2017Article
- Proteoglycans: Potential Agents in Mammographic Density and the Associated Breast Cancer Risk.Journal of mammary gland biology and neoplasia · 2015Review
- Decoding the Matrix: Instructive Roles of Proteoglycan Receptors.Biochemistry · 2015Review
- Article
- Insights into the key roles of proteoglycans in breast cancer biology and translational medicine.Biochimica et biophysica acta · 2015Review
- A kinase inhibitor screen reveals protein kinase C-dependent endocytic recycling of ErbB2 in breast cancer cells.The Journal of biological chemistry · 2014Article
- Key roles for the small leucine-rich proteoglycans in renal and pulmonary pathophysiology.Biochimica et biophysica acta · 2014Review
- The role of novel and known extracellular matrix and adhesion molecules in the homeostatic and regenerative bone marrow microenvironment.Cell adhesion & migration · 2014Review
- Article
- Biglycan-mediated upregulation of MHC class I expression in HER-2/neu-transformed cells.OncoimmunologyArticle
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The extracellular matrix protein biglycan (Bgn) is a leucine-rich proteoglycan that is involved in the matrix assembly, cellular migration and adhesion, cell growth, and apoptosis. Although a distinct expression of Bgn was found in a number of human tumors, the role of this protein in the initiation and/or maintenance of neoplastic transformation has not been studied in detail. Using an in vitro model of oncogenic transformation, a down-regulation of Bgn expression as well as an altered secretion of different Bgn isoforms was found both in murine and human HER-2/neu oncogene-transformed cells when compared with HER-2/neu(-) cells. This was associated with a reduced growth, wound closure, and migration capacity. Vice versa, silencing of Bgn in HER-2/neu(-) fibroblasts increased the growth rate and migration capacity of these cells. Bgn expression was neither modulated in HER-2/neu(+) cells by transforming growth factor-β(1) nor by inhibition of the phosphoinositol 3-kinase and MAP kinase pathways. In contrast, inhibition of the protein kinase C (PKC) pathway led to the reconstitution of Bgn expression. In particular, the PKC target protein cAMP response element binding protein (CREB) is a major regulator of Bgn expression as the silencing of CREB by RNA interference was accompanied by ∼5000-fold increase in Bgn-mRNA expression in HER-2/neu(+) cells. Thus, Bgn inhibits the major properties of HER-2/neu-transformed cells, which is inversely modulated by the PKC signaling cascade.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.