The signaling processes in plants that initiate cellular responses to biotic and abiotic factors are believed to be located in the plasma membrane (PM). A better understanding of the PM proteome response to environmental stresses might lead to new strategies for improving stress-tolerant crops. A sub-cellular proteomics approach was applied to monitor changes in abundance of PM-associated protein in response to salinity, a key abiotic stress affecting rice productivity worldwide. Proteome was extracted from a root plasma-membrane-rich fraction of a rice salt tolerant variety, IR651, grown under saline and normal conditions. Comparative two-dimensional electrophoresis revealed that 24 proteins were differentially expressed in response to salt stress. From these, eight proteins were identified by mass spectrometry analysis. Most of the proteins identified are likely to be PM-associated and are known to be involved in several important mechanisms of plant adaptation to salt stress. These include regulation of PM pumps and channels, membrane structure, oxidative stress defense, signal transduction, protein folding, and the methyl cycle. To investigate the correlation between mRNA and protein level in response to salinity, we performed quantitative Real-Time PCR analysis of three genes that were salt responsive at the protein level, including 1,4-Benzoquinone reductase, a putative remorin and a hypersensitive induced response protein. No concordance was detected between the changes in levels of gene and protein expression. Our results indicate that the proteomics approach is suitable for expression analysis of membrane associated proteins under salt stress.

Glycation is a general spontaneous process in proteins which has significant impact on their physical and functional properties. These changes in protein properties could be related to several pathological consequences such as cataract, arteriosclerosis and Alzheimer’s disease. Among the proteins, glycation of Human serum albumin (HSA) is of special interest. Human serum albumin is the most abundant protein in the plasma and because of its high sensitivity for glycation, undergoes structural and functional changes due to binding of reducing sugars in vitro. The glycation process occurs by plasma glucose in vivo which has great impacts on the three dimensional structure of protein. These changes are efficient and stable enough which makes the protein to be considered as a new special disease marker instead of HbA1C for diabetes. In some cases, glycated albumin was used as an alternative marker for glycemic control. Glycated albumin reacts with glucose ten times more rapidly than HbA1C and has shorter half-life which makes it more reliable for indicating glycemic states. In this review, glycation of Human Serum Albumin has been overviewed, starting from overall concepts of glycation, followed by some Examples of pathological consequences of protein glycation. The BSA aggregation was reviewed in terms of structural and biological impacts of glycation on the protein followed by reporting documents which indicate possibility of glycated albumin to be used as specific marker for diabetes. Finally, some of the studies related to the models of glycated albumin have been briefly described, with an emphasis on In vitro studies. It is interesting to note the relationship found between in vitro glycation experiments and the propensity of proteins to form amyloid structures, a point that could be further explored as to its significance in hyperglycemic states.

Reactive oxygen species (ROS) are identified to control the expression and activity of various essential signaling intermediates involved in cellular proliferation, apoptosis, and differentiation. Indeed, ROS represents a double-edged sword in supporting cell survival and death. Many common pathological processes, including various cancer types and neurodegenerative diseases, are inflammation and oxidative stress triggers, or even initiate them. Keap1-Nrf2 is a master antioxidant pathway in cytoprotective mechanisms through Nrf2 target gene expression. Activation of the Nfr2 pathway benefits cells in the early stages and reduces the level of ROS. In contrast, hyperactivation of Keap1-Nrf2 creates a context that supports the survival of both healthy and cancerous cells, defending them against oxidative stress, chemotherapeutic drugs, and radiotherapy. Considering the dual role of Nrf2 in suppressing or expanding cancer cells, determining its inhibitory/stimulatory position and targeting can represent an impressive role in cancer treatment. This review focused on Nrf2 modulators and their roles in sensitizing breast cancer cells to chemo/radiotherapy agents.