ABSTRACT
Microwave radiations can be encountered regularly in daily lives. When WHO announced that microwave radiations were a kind of environmental energy which interfere with the physiological functions of the human body, great concerns have been raised over the damages microwave frequencies can do to human physiology. The immunological performance and the activities of the cellular inflammatory factor NFκB have been closely related in monocyte. Due to the effect of phorbol 12-myristate 13-acetate (PMA) on THP-1 monocytes, THP-1 monocytes would differentiate into macrophages and would then react with lipopolysaccharides (LPS), and the amount of NFκB increased in the THP-1 monocytes. Expression of cytokine is affected when cells are exposed to a frequency of 2450 MHz and at 900 W. Thus, in our experiments, an observation was made when THP-1 monocytes were stimulated with PMA and LPS to differentiate into macrophage, the amount of NFκB in cells increased exponentially, and the levels of NFκB expression were decreased by the exposure of microwave radiation. In conclusion, microwave radiations were found to inhibit the activity functions of THP-1 monocytes stimulated with PMA and LPS.
Subject(s)
Lipopolysaccharides , Monocytes , Humans , Lipopolysaccharides/pharmacology , Macrophages , Microwaves , NF-kappa B/metabolism , Tetradecanoylphorbol Acetate/pharmacologyABSTRACT
Degenerate primers were designed based on all possible sequences of the N-terminal and C-terminal regions of Delonix regia trypsin inhibitor (DrTI). Five hundred sixty-one bp of polymerase chain reaction (PCR) product was amplified using the above degenerate primers and genomic DNA and cDNA of Delonix regia as a template. The amplified PCR products were cloned and sequenced. DNA sequence analysis of cDNA and genomic clones of DrTI have the same nucleotide sequence in the coding region, and manifested a genomic clone without intervening sequences in the coding region. The amino acid sequence deduced from the DrTI genomic and cDNA clones agreed with that identified via amino acid sequencing analysis, except that two amino acid residues, Ser and Lys, existed between residues Lys141 and Ser142. DrTI open reading frame was then amplified and cloned in-frame with GST in pGEX4T-1 and overexpressed in Escherichia coli to yield a glutathione S-transferase (GST)-fusion protein with a calculated molecular mass of about 45 kDa. The recombinant DrTI (reDrTI) was derived by treating the GST-DrTI fusion protein with thrombin. Both the reDrTI and GST-DrTI fusion protein exhibited a strong identical inhibitory effect on trypsin activity.
