Large scale RNAi screen reveals that the inhibitor of DNA binding 2 (ID2) protein is repressed by p53 family member p63 and functions in human keratinocyte differentiation.

The inhibitor of DNA binding 2, dominant negative helix-loop-helix protein, ID2, acts as an oncogene and elevated levels of ID2 have been reported in several malignancies. Whereas some inducers of the ID2 gene have been characterized, little is known regarding the proteins capable to repress its expression. We developed siRNA microarrays to perform a large scale loss-of-function screen in human adult keratinocytes engineered to express GFP under the control of the upstream region of ID2 gene.

Identification of a rhabdomyosarcoma targeting peptide by phage display with sequence similarities to the tumour lymphatic-homing peptide LyP-1.

Rhabdomyosarcoma (RMS) is the most common soft tissue sarcoma in children. To improve existing therapies and broaden the spectrum of cytotoxic agents that can be used in RMS treatment, we performed a phage-display-based screening for peptides that bind specifically to RMS cells. Two peptides binding to RMS and to other tumour cell lines, but not to normal skeletal muscle cells and fibroblasts, were isolated from phage-displayed random peptide libraries.

A fluorescent Tie1 reporter allows monitoring of vascular development and endothelial cell isolation from transgenic mouse embryos.

Tie1 is an endothelial receptor tyrosine kinase essential for development and maintenance of the vascular system. Here we report generation of transgenic mice expressing enhanced green fluorescent protein (EGFP) or a chimeric protein consisting of a Zeosin resistance marker and EGFP under the control of mouse Tie1 promoter. Intravital monitoring of fluorescence showed that the EGFP reporter recapitulates the Tie1 expression pattern in the developing vasculature, and flow cytometry using EGFP allowed the isolation of essentially pure Tie1-expressing endothelial cells from transgenic mouse embryos.