Release of aquatic carbon from two peatland catchments in E. Finland during the spring snowmelt period

Spring snowmelt in the arctic and boreal regions represents the most significant event in the hydrological year. We measured concentrations and fluxes of different carbon species in 2 small contrasting (control v drained) forested peatland catchments in E. Finland between April and June 2008 and compared these to long-term annual fluxes. Measurements were made using a combination of continuous sensors (CO₂, temperature, pH, discharge) and routine spot sampling (DOC, POC, DIC, CO₂, CH₄, N₂O). The highest concentrations of CO₂ and CH₄ in streamwater were observed under low flow conditions before the spring flood event, reflecting accumulation and downstream release of gaseous C at the end of the winter period. Over the length of the study mean CH₄ concentrations were 10× higher in the drained site. The snowmelt event was associated with a dilution of DOC and CO₂, with the drained catchment showing a much flashier hydrological response compared to the control site, and post-event, a slower recovery in DOC and CO₂ concentrations. Fluxes of all carbon species during the snowmelt event were significant and represented 37?C45% of the annual flux. This highlights the challenge of quantifying aquatic C fluxes in areas with large temporal variability and suggests that inability to ??capture?? the spring snowmelt event may lead to under-estimation of C fluxes in northern regions.     

Homologous sequences in adenovirus E1A and human papillomavirus E7 proteins mediate interaction with the same set of cellular proteins.

Studies of adenovirus E1A oncoprotein mutants suggest that the association of E1A with the retinoblastoma protein (pRB) is necessary for E1A-mediated transformation. Mutational analysis of E1A indicates that two regions of pRB are required for E1A to form stable complexes with the retinoblastoma protein. In addition to pRB binding, these regions are necessary for E1A association with several other cellular proteins, including p130, p107, cyclin A, and p33cdk2. Here we show that short synthetic peptides containing the pRB-binding sequences of E1A are sufficient for interaction with p107, cyclin A, and p130. The E7 protein of human papillomavirus type 16 contains an element that binds to pRB and appears to be functionally homologous to the E1A sequences. Peptides containing this region of the E7 protein were able to interact with p107, cyclin A, and p130 in addition to pRB. These findings suggest that the common mechanism of transformation used by these viral oncogenes involves their association with a set of polypeptides.     

The regions of the retinoblastoma protein needed for binding to adenovirus E1A or SV40 large T antigen are common sites for mutations

The protein product of the retinoblastoma (RB) gene is thought to function in a pathway that restricts cell proliferation. Recently, transforming proteins from three different classes of DNA tumor viruses have been shown to form complexes with the RB protein. Genetic studies suggest that these interactions with the RB protein are important steps in transformation by these viruses. In order to understand better the function of the RB-viral oncoprotein complexes, we have mapped the regions of the RB protein that are necessary for these associations. Two non-contiguous regions of RB were found to be essential for complex formation with adenovirus E1A or SV40 large T antigen. These two regions are found between amino acids 393 and 572 and 646 and 772. Interestingly, these binding sites on RB overlap with the positions of naturally occurring, inactivating mutations of the RB gene. These results strongly suggest that these viral oncoproteins are targeting a protein domain that is an important site in the normal function of the RB protein.     

Automated approach for the evaluation of glutathione-S-transferase P1-1 inhibition by organometallic anticancer compounds

A novel automated method based on sequential injection analysis (SIA), a non-segmented flow injection technique, was developed to evaluate glutathione S-transferase P1-1 (GST P1-1) activity in the presence of organometallic complexes with putative anticancer activity. The assay is based on the reaction of L-glutathione (GSH) and 1-chloro-2,4-dinitrobenzene (CDNB) in the presence of GST P1-1 to afford the GS-DNB conjugate and the reaction may be monitored by an increase in absorbance at 340 nm. A series of ruthenium, iron, osmium and iridium complexes were evaluated as GST P1-1 inhibitors by evaluating their half-maximal inhibitory concentration (IC₅₀). An iridium compound displays the lowest IC₅₀ value of 6.7 ± 0.7 µM and an iron compound displays the highest IC₅₀ value of 275 ± 9 µM. The SIA method is simple to use, robust, reliable, and efficient and uses fewer reagents than batch methods and each analysis takes only 5 minutes.