Journal
CELLULAR AND MOLECULAR BIOENGINEERING
Volume 9, Issue 1, Pages 1-11Publisher
SPRINGER
DOI: 10.1007/s12195-015-0417-4
Keywords
Fibronectin conformational flexibility; Fibronectin mechanics; Tumor stroma; Tumor progression
Funding
- NSF [DMR-1352299]
- NIH/NCI [R01 CA185293]
- Cornell Center on the Microenvironment Metastasis [NCI U54 CA143876]
- Division Of Materials Research
- Direct For Mathematical & Physical Scien [1352299] Funding Source: National Science Foundation
Ask authors/readers for more resources
Fibronectin (Fn) is an essential extracellular matrix (ECM) glycoprotein involved in both physiological and pathological processes. The structure-function relationship of Fn has been and is still being studied, as changes in its molecular structure are integral in regulating (or dysregulating) its biological activities via its cell, matrix component, and growth factor binding sites. Fn comprises three types of repeating modules; among them, FnIII modules are mechanically unstable domains that may be extended/unfolded upon cell traction and either uncover cryptic binding sites or disrupt otherwise exposed binding sites. Cells assemble Fn into a fibrillar network; its conformational flexibility implicates Fn as a critical mechanoregulator of the ECM. Fn has been shown to contribute to altered stroma remodeling during tumorigenesis. This review will discuss (i) the significance of the structure-function relationship of Fn at both the molecular and the matrix scales, (ii) the role of Fn mechanobiology in the regulation of tumorigenesis, and (iii) Fn-related advances in cancer therapy development.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available