Regulatable Expression of the Interferon-Induced Double-Stranded RNA Dependent Protein Kinase PKR Induces Apoptosis and Fas Receptor Expression

Double-Stranded RNA-Dependent Protein Kinase (PKR)-Dependent Apoptosis Induction by a Novel Small Compound

-Induced Cytokine Expression Mycobacterium Protein Kinase PKR in A Role for Double-Stranded RNA-Activated

The mouse antiphosphotyrosine immunoreactive kinase, TIK, is indistinguishable from the double-stranded RNA-dependent, interferon-induced protein kinase, PKR.

The mouse TIK protein, a serine/threonine kinase, was originally isolated from a murine pre-B cell expression library by its ability to bind anti-phosphotyrosine antibodies (Icely et al., J. Biol. Chem. 266, 16073-16077, 1991). The 67 kDa protein was found to have an associated autophosphorylation activity when incubated with ATP. Our results show that TIK is actually the mouse interferon-induc...

Double-Stranded RNA-dependent Protein Kinase (PKR) of Lung Cancer Cells via Up-Regulation of the ) Induces Apoptosis

Adenoviral-mediated overexpression of the melanoma differentiationassociated gene 7 (Ad-mda7) induces apoptosis in a wide range of cancer cells, although the mechanism is not well understood. We report that Ad-mda7 induces and activates the double-stranded RNA-dependent protein kinase (PKR), which leads to phosphorylation of the subunit of eukaryotic translation initiation factor 2 (eIF-2 ) and...

Double-stranded RNA-independent dimerization of interferon-induced protein kinase PKR and inhibition of dimerization by the cellular P58IPK inhibitor.

The interferon (IFN)-induced, double-stranded RNA-activated protein kinase (PKR) mediates the antiviral and antiproliferative actions of IFN, in part, via its translational inhibitory properties. Previous studies have demonstrated that PKR forms dimers and that dimerization is likely to be required for activation and/or function. In the present study we used multiple approaches to examine the m...