The importance of the m7G moiety for substrate binding and recognition is confirmed by the observation that RNA molecules without 5′ cap guanosine are not methylated by CMTr1, and human cap MTases generally appear to act only on a capped 5′ end of RNA (Supplementary Fig. S5).
Due to the similarities between human CaP tumors and the PSP KIMAP tumors, this preclinical model may supplement the current transgenic models to study CaP more accurately.
Several tumor marker genes characteristic of human CaP were uniquely identified in KIMAP tumors, including hepsin, maspin, Nkx3.1, CD10 and PSP94 (similar to PSA), etc.
The purpose of the current study is to investigate the therapeutic potential of small interference RNA (siRNA) targeting PSCA on human CaP cells.
Ueda, H. et al. Expression of a synthetic gene for human cap binding protein (Human IF-4E) in Escherichia coli and fluorescence studies on interaction with mRNA cap structure analogues.
To validate the functional importance of amino-acid residues predicted to be critical for the substrate binding and enzymatic activity of human cap MTases, a mutagenesis analysis was performed.
Specifically, in the androgen insensitive human CaP line PC-3, 24 h calcitriol pre-treatment yielded a 36% increase in cell death at the −15 °C isotherm compared to temperature-matched controls (60% viable vs. 96%, respectively).
In this study, we demonstrate that the new model possesses a tumor architecture of heterogeneity and multifocality similar to that of human CaP, by utilizing a new compound scoring system to compare with the PSP94 (approved gene symbol Msmb) gene-directed transgenic mouse CaP model (TGMAP).
TRAMP-C2 cells, human CaP lines and primary TRAMP tumors expressed CD1d.
These critical functions are conserved in fungi and the human capping system can replace that of Saccharomyces cerevisiae [2].
