Odontoblasts derive from neural crest-derived odontogenic mesenchymal cells, and they are an important barrier of defense for the host. Survival and immunity of odontoblasts play important roles in protecting the dentin-pulp structure. Autophagy can eliminate damaged organelles and recycle cellular components to facilitate cellular homeostasis. Autophagy can be activated with external stressors, such as starvation, hypoxia, and infection. In this study, the role of autophagy in inflamed odontoblasts was explored, and its possible mechanism was investigated. Cell viability was not affected by mild lipopolysaccharide (LPS) stimulation, and autophagy was activated during this process. Immunofluorescence of light chain 3 confirmed that autophagy was induced with LPS treatment. Early-stage autophagy inhibition resulted in down-regulated cell viability, contrary to the up-regulated cell viability at late-stage autophagy inhibition. Western blot suggested that p-Akt and survivin were not activated in the early stage, and they gradually increased and peaked in the late stage. Meanwhile, autophagy was down-regulated through the Akt/mTOR/survivin pathway in the late stage. Thus, autophagy has a dual role in inflamed odontoblasts, which indicates its importance in maintaining the microenvironment homeostasis of odontoblasts. Autophagy was induced as a survival mechanism in the early stage, and it decreased through the Akt/mTOR/survivin signaling pathway in the late stage.
A gradient refractive index (GRIN) lens has a great potential for on-chip imaging and detection systems because of its flat surface with reduced defects. This paper reports a liquid thermal GRIN lens prepared using heat conduction between only one liquid, and uses it as a tunable optical tweezer for single living cell trapping in a flowing environment. This liquid GRIN lens consists of a trapezoidal region in the upper layer which is used to establish a GRIN profile by the heat conduction between three streams of benzyl alcohol with different temperatures, and subsequently a rhombus region in the lower layer with compensation liquids to form a steady square-law parabolic refractive index profile only in transverse direction. Simulations and experiments successfully show the real-time tunability of the focusing properties. The focal length can be modulated in the range of 500 μm with the minimum focal length of 430 μm. A considerable high enhancement factor achieves 5.4 whereas the full width at half maximum is 4 μm. The response time of the GRIN lens is about 20 ms. Based on this enhancement, tunable optical trapping for single human embryonic kidney 293 cell in the range of 280 μm is demonstrated by varying the focal length and working distance which is difficult for solid optical tweezers. The considerable quality of this liquid GRIN lens indicates on-chip applications especially in high quality optical imaging, detection and cells' handling.
Three recent isolates of measles virus Fu, IMA, and SMD obtained by using B95a cells did not exhibit hemadsorption with African green monkey red blood cells (AGM-RBC). After long-term passage in Vero cells, these Vero cell-adapted strains derived from three isolates obtained the activity to agglutinate AGM-RBC. The primary sequences of the hemagglutinin (H protein) and fusion glycoproteins (F protein) from these two types of viruses were compared and revealed that several important amino acid residues in the H protein do not converge. After adaptation, Fu strain has an Asn to Tyr substitution at position 481 and IMA strain has two substitutions--an Asp to Asn at position 14 and a Ser to Gly at position 546, SMD strain also has a Ser to Gly substitution at position 546. Since the sequences of the F protein were identical between both types of viruses, the hemadsorption alteration from negative to positive might be the result of these substitutions. Site-directed mutagenesis of the H genes were performed to confirm that the substitution of Ser --> Gly at position 546 and Asn --> Tyr at position 481 in the H protein were responsible for hemadsorption alteration. Anti-CD46 monoclonal antibody (M75 and M160) study made clear that these two substitutions also governed the MV H protein's interaction with CD46 receptor. Our results showed that two important amino acid residues in MV H protein govern the binding to CD46 receptor and hemadsorption. In this paper, we reported a novel amino acid residue at position 546 in MV H protein, which was critical for hemadsorption and CD46 binding.
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