| dc.description.abstract | Research in the past few decades has worked on the use of therapeutically valuable proteins from different protein expression systems. The ideal foreign protein expression system would be the one that produces the most safe, biologically active material at the lowest cost. Plant-based expression systems have emerged as a serious competitive force in the large-scale production of recombinant proteins. Most recombinant genes can be expressed in cultured rice cells; therefore, it is essential to determine which expression cassettes offer the most advantages for the production of the recombinant protein. The knowledge of protein signal sequences has become a crucial tool for pharmaceutical scientists who genetically modify bacteria, plants, and animals to produce effective drugs. By adding a specific tag to the desired proteins, one can, for instance, tag them for excretion, making them much easier to harvest. Though general features of secretion signals are conserved between plants and animals, the broad sequence variability among signal peptides suggests differing efficiency of signal peptide recognition. To increase the secretion of recombinant protein in rice suspension cells, we generated overexpression vectors using different endogenous N-terminal signal peptides (αAmylase3,CIN1,33kD) fused with green florescence protein (GFP) and mouse granulocyte-macrophage stimulation factor (mGM-CSF), respectively. We detected the secreted GFP by Western blotting. Comparison of different signal peptides for secretion of GFP in rice suspension culture, we found that αAmylase3 is the better signal peptide for secreted the GFP out. To examine whether the supremacy of the αAmylase3 signal is specific for GFP, we’ll subsequently analyze the secretion efficiency of mGM-CSF and intend to develop a high efficiency secretion system in rice suspension cells. | en_US |