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Type I Collagen-Mediated Changes in Gene Expression and Function of Prostate Cancer Cells

  • Chapter
The Biology of Skeletal Metastases

Part of the book series: Cancer Treatment and Research ((CTAR,volume 118))

Abstract

Increasingly it is recognized that the extracellular matrix (ECM) plays a critical role in the normal development and differentiated phenotype of cells and tissues (Lee et al, 1999; Bokel et al, 2002). Engagement of ECM molecules by cells through surface receptors, including integrins, results in the activation of signaling pathways along with specific changes in gene expression. Intracellular signals direct proliferation, survival, migration, invasive potential and differentiation (Giancotti et al, 1999). A well characterized example of ECM influence over cell phenotype and gene expression is in the control of mammary epithelial cell differentiation by the particular composition of the ECM (Lee et al, 1999; Hansen et al, 2000). Mammary epithelial cells plated onto laminin-1 matrices express proteins associated with milk production, including ß-casein, whereas cells plated onto type I collagen do not. Additionally, laminin-1 confers on mammary epithelial cells the capability of being able to respond fully to prolactincontrolled expression of milk proteins. Cells plated onto type I collagen, however, fail to respond (Streuli et al, 1999). Another familiar example of ECM control over cell differentiation and gene expression occurs during osteoblast differentiation. Early studies indicated that contact with type I collagen is required for normal differentiation and eventual matrix secretion and mineralization (Gronowicz et al, 1994; Takeuchi et al, 1997). Subsequent studies showed that type I collagen directs osteoblast differentiation by influencing the activity of a specific transcription factor Cbfal, also called Runx2, associated with transcriptional activation of a series of genes associated with osteoblast formation (Xiao et al, 1998). The α2β1 integrin serves as the major molecular conduit that mediates type I collagen-dependent osteoblast maturation (Gronowicz et al, 1994; Takeuchi et al, 1997; Xiao et al, 1998). Cbfal/Runx2 activity, in response to type I collagen binding to the α2β1 integrin, is controlled post-translationally by phosphorylation by MAPK (Xiao et al, 2000). These two examples illustrate the importance of the ECM-directed gene expression for cellular differentiation, and highlight the convergence of intracellular signals that are required for phenotypic and genotypic control.

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  1. Cancer Drug Development Laboratory, Translational Genomics Research Institute, Gaithersburg, MD, USA

    Jeffrey Kiefer

  2. Department of Biological Sciences, University of Delaware, USA

    Angela Alexander & Mary C. Farach-Carson

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  1. University of Michigan Comprehensive Cancer Center University of Michigan School of Medicine, University of Michigan, Ann Arbor, Michigan, USA

    Evan T. Keller DVM, PhD (Associate Professor of Urology, Comparative Medicine and Pathology) (Associate Professor of Urology, Comparative Medicine and Pathology)

  2. Emory University School of Medicine, Emory University, Atlanta, Georgia, USA

    Leland W. K. Chung PhD (Professor of Urology, Hematology/Oncology, Biochemistry and the Winship Cancer Institute) (Professor of Urology, Hematology/Oncology, Biochemistry and the Winship Cancer Institute)

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Kiefer, J., Alexander, A., Farach-Carson, M.C. (2004). Type I Collagen-Mediated Changes in Gene Expression and Function of Prostate Cancer Cells. In: Keller, E.T., Chung, L.W.K. (eds) The Biology of Skeletal Metastases. Cancer Treatment and Research, vol 118. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-9129-4_5

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