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Systematic identification of genomic markers of drug sensitivity in cancer cells
It was found that mutated cancer genes were associated with cellular response to most currently available cancer drugs, and systematic pharmacogenomic profiling in cancer cell lines provides a powerful biomarker discovery platform to guide rational cancer therapeutic strategies. Expand
Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis.
The observations suggest that coordinated CD44, MMP-9, and TGF-beta function may provide a physiological mechanism of tissue remodeling that can be adopted by malignant cells to promote tumor growth and invasion. Expand
CD44 is the principal cell surface receptor for hyaluronate
CD44 is a broadly distributed cell surface protein thought to mediate cell attachment to extracelular matrix components or specific cell surface ligands. We have created soluble CD44-immunoglobulinExpand
Extracellular matrix remodelling: the role of matrix metalloproteinases
MMPs play an important role in the control of cellular interactions with and response to their environment in conditions that promote tissue turnover, be they physiological or pathological, such as inflammation and cancer. Expand
Functional structure and composition of the extracellular matrix
The extracellular matrix appears to be a very dynamic structure, which has a prominent role in normal development as well as in a variety of disease processes and Matrix metalloproteinases are essential actors in this complex interplay between cells and the extrace cellular matrix. Expand
Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion.
It is shown that CD44 associates with a proteolytic form of the matrix metalloproteinase-9 (MMP-9) on the surface of mouse mammary carcinoma and human melanoma cells and defines a mechanism for CD44-mediated tumor invasion. Expand
Matrix metalloproteinases in tumor invasion and metastasis.
  • I. Stamenkovic
  • Biology, Medicine
  • Seminars in cancer biology
  • 1 December 2000
Findings that a growing number of proteolytically active MMPs may localize to the cell surface in association with adhesion receptors, and that MMP substrates include latent cytokines and growth factors, provide a new conceptual framework for the mechanisms whereby M MPs influence tumor behavior. Expand
A 39-kDa protein on activated helper T cells binds CD40 and transduces the signal for cognate activation of B cells.
Data indicate that the 39-kDa membrane protein expressed on activated Th is a binding protein for CD40 and functions to transduce the signal for Th-dependent B-cell activation. Expand
EZH2 is essential for glioblastoma cancer stem cell maintenance.
It is shown that targeted pharmacologic disruption of EZH2 by the S-adenosylhomocysteine hydrolase inhibitor 3-deazaneplanocin A (DZNep), or its specific downregulation by short hairpin RNA (shRNA), strongly impairs GBM cancer stem cell (CSC) self-renewal in vitro and tumor-initiating capacity in vivo. Expand
CD44 anchors the assembly of matrilysin/MMP-7 with heparin-binding epidermal growth factor precursor and ErbB4 and regulates female reproductive organ remodeling.
It is demonstrated that CD44 heparan sulfate proteoglycan recruits proteolytically active matrix metalloproteinase 7 (matrilysin, MMP-7) and heparin-binding epidermal growth factor precursor (pro-HB-EGF) to form a complex on the surface of tumor cell lines, postpartum uterine and lactating mammary gland epithelium, and uterine smooth muscle. Expand