Virus-induced heterodimer formation between IRF-5 and IRF-7 modulates assembly of the IFNA enhanceosome in vivo and transcriptional activity of IFNA genes.

Transcription factors of the interferon regulatory factor (IRF) family have been identified as critical mediators of early inflammatory gene transcription in infected cells. We have shown previously that IRF-5, like IRF-3 and IRF-7, is a direct transducer of virus-mediated signaling and plays a role in the expression of multiple cytokines/chemokines. The present study is focused on the molecular mechanisms underlying the formation and function of IRF-5/IRF-7 heterodimers in infected cells.

A novel gene (PLU-1) containing highly conserved putative DNA/chromatin binding motifs is specifically up-regulated in breast cancer.

A novel human gene (PLU-1) has been identified which shows a highly restricted expression in normal adult tissues but which is consistently expressed in breast cancers. A fragment of the PLU-1 cDNA was identified by differentially screening a fetal brain library with cDNAs prepared from ce-1 cells (a human mammary epithelial cell line overexpressing c-ErbB2) treated or untreated with the antibody 4D5, which inhibits c-ErbB2 phosphorylation. Clones covering the full cDNA sequence of 6.

Adhesion molecules in breast cancer: role of alpha 2 beta 1 integrin.

An early event in the development of breast carcinomas is the loss of normal tissue architecture. In benign lesions and in situ tumours both luminal and myoepithelial cells are present, but in most invasive cancers the malignant cell has the phenotype of the luminal cell, and proliferates without contacting the myoepithelial cells or the basement membrane. The reduction in cell contacts is clearly crucial for the initiation of metastatic growth, and is accompanied by a loss of expression or function of cell adhesion molecules.

Transmembrane signaling by the alpha subunit of the type I interferon receptor is essential for activation of the JAK kinases and the transcriptional factor ISGF3.

The Type I interferon (IFN) receptor has a multisubunit structure. The component of the receptor that has been most thoroughly studied is the alpha subunit. Expression of the alpha subunit in mouse L-929 cells confers antiviral response to human IFN alpha 8, but not to human IFN alpha 2 or IFN beta.