Journal
AMERICAN JOURNAL OF PATHOLOGY
Volume 181, Issue 2, Pages 380-387Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.ajpath.2012.04.029
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Funding
- NIH [RO1 CA39481, RO1 CA47282, RO1 CA120975, T32 AA07463]
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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-beta 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 protumorigenic cues. (Am J Pathol 2012, 181:380-387; http://dx.doi.org/10.1016/j.ajpath.2012.04.029)
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