ssists in the correct disulfide pairing and proper folding of the mature peptide

Regarding the differentially expressed proteins, many of the listed FH1 Proteins in Table 2 and Figure S3 are related to the protein synthesis process that seems to be upregulated, except for some protein spots of the elongation factor 2 that show a reduction in their levels. This may be a response to compensate for the processing of proteins that occurs after irradiation. This response may also enhance the synthesis of specific proteins that will possibly play a role in the stress response. The results obtained from the analyses of translation inhibition and proteomic profile after irradiation place de novo protein synthesis as an important cellular response to gamma radiation. The prosegment, which serves as an intramolecular chaperone, assists in the correct disulfide pairing and proper folding of the mature peptide and keeps the mature peptide inactive until it is cleaved by various proteolytic enzymes. This affected in increased insulin availability and a concomitant protection for liver glycogen stores. Such conditions are also likely due to Sb induced interference in neoglucogenesis pathways. The designed Sb nanomedicines therefore provided newer directions in diabetes management. The nanoparticles are likely to aid further in diabetic control and serve as an adjunct therapeutic. It is worth noting that, although Histamine Phosphate are mostly downregulated, processed forms of these molecules are upregulated and may even be functional. Interestingly, the two chaperones localized in the endoplasmic reticulum are upregulated after gamma radiation exposure, which may indicate an important role of this compartment in the ionizing radiation stress response, suggesting the existence of an unfolded protein response-like in this condition.

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