Document Type
Article
Publication Date
8-2012
Abstract
Decorin, an archetypal member of the small leucine-rich proteoglycan gene family, has a broad binding repertoire that encompasses matrix structural components, such as collagens, and growth factors, particularly those that belong to the transforming growth factor-β ligand superfamily. Within the tumor microenvironment, stromal decorin has an inherent proclivity to directly bind and down-regulate several receptor tyrosine kinases, which are often overexpressed in cancer cells. The decorin interactome commands a powerful antitumorigenic signal by potently repressing and attenuating tumor cell proliferation, survival, migration, and angiogenesis. This collection of interacting molecules also regulates key downstream signaling processes indirectly via the sequestration of growth factors or directly via the antagonism of receptor tyrosine kinases. We propose that decorin can be considered a "guardian from the matrix" because of its innate ability to oppose pro-tumorigenic cues.
© 2012 American Society for Investigative Pathology.
Recommended Citation
Neill, Thomas; Schaefer, Liliana; and Iozzo, Renato V., "Mini-Review: Decorin, a Guardian from the Matrix" (2012). Department of Pathology, Anatomy, and Cell Biology Faculty Papers. Paper 96.
https://jdc.jefferson.edu/pacbfp/96
Comments
This article is the author's final version prior to publication. The published version of this article is available from the American Journal of Pathology, Volume 181, Issue 2, August 2012, Pages 380-387. DOI: 10.1016/j.ajpath.2012.04.029. © Elsevier B.V.