Abstract
Transforming growth factor β (TGFβ) members are secreted in biologically inactive complexes that must be activated in order to enable binding to their cell surface receptors. Interestingly, many of the proteins that can activate TGFβ have been implicated in either suppressing or promoting tumorigenesis. Included among these are matrix proteins (thrombospondin-1), receptors (integrins αvβ6 and αvβ8) and proteases (matrix metalloproteases and plasmin). These proteins cannot only activate TGFβ, but can also modulate cell responsiveness to TGFβ. In this section, we review data highlighting the complexity and bidirectionality of TGFβ matrix interactions within the tumor microenvironment, and propose that these dynamic interactions are a critical spatial and temporal determinant of the effects of TGFβ on tumorigenesis.
Original language | English (US) |
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Pages (from-to) | 574-582 |
Number of pages | 9 |
Journal | Differentiation |
Volume | 70 |
Issue number | 9-10 |
DOIs | |
State | Published - Dec 2002 |
Keywords
- Extracellular matrix
- Integrin
- Latency-associated peptide
- Matrix metalloproteinase
- Plasmin
- Thrombospondin
- Transforming growth factor β
ASJC Scopus subject areas
- Molecular Biology
- Developmental Biology
- Cell Biology
- Cancer Research