[Research progress on intralymphatic immunotherapy].

Intralymphatic immunotherapy (ILIT) is an effective and safe causative treatment for allergic diseases. Compared with conventional specific immunotherapy such as subcutaneous immunotherapy (SCIT) and sublingual immunotherapy (SLIT), ILIT could significantly reduce treatment duration. This article will review the results of previous researches focusing on ILIT.

Variation of nanoparticle fraction and compositions in two-stage double peaks aging precipitation of Al-Zn-Mg alloy.

Atom probe tomography (APT) coupling high-resolution transmission electron microscopy (HRTEM) was used to analyze the fraction and compositions of different nanoparticles in two-stage double peaks aging process of Al-Zn-Mg alloy. Al content is found to be closely related to the size of nanoparticles and it can be greater than ~ 50.0 at. % in the nanoparticle with the equivalent radius under ~ 3.0 nm. Correspondingly, Al content of the nanoparticle, with the equivalent radius over ~ 5.0 nm, is measured under ~ 40.0 at. %. Evolution from Guinier-Preston (G.P.) zone to η phase is a growing process where Mg and Zn atoms enter the nanoparticle, therefore rejecting Al atoms. G.P. zones can take up a number fraction of ~ 85.0 and ~ 22.7% of nanoparticles in the first and second peak-aged samples, respectively, and even in the over-aged (T73) sample, they can still be found. As aging time increases, fraction of η' phases monotonically rises to the peak value (~ 54.5%) in the second peak-aged state and then drops, which is significant for the second hardness peak and directly proves their function as the transitional medium. In T73 state, ~ 63.3% nanoparticles compose of η phases, which were measured to still contain ~ 10.2 to ~ 36.4 at. % Al atoms.

PRAME promotes in vitro leukemia cells death by regulating S100A4/p53 signaling.

OBJECTIVE: PRAME (Preferentially Expressed Antigen in Melanoma) is a tumor-associated antigen recognized by immunocytes, and it induces cytotoxic T cell-mediated responses in melanoma. PRAME is expressed in a wide variety of tumors, but in contrast with most other tumor-associated antigens, it is also expressed in leukemias. The physiologic role of PRAME remains elusive. Recently, it has found PRAME could be involved in the regulation of cell death in leukemias, but the mechanism of the function is unclear. Here, we confirm that PRAME induces leukemias cell death by regulation of S100A4/p53 signaling. MATERIALS AND METHODS: The pCDNA3-PRAME plasmid and its control were transfected with the KG-1 cells. The pCDNA3-PRAME transfected KG-1 cells were then transiently transfected with S100A4 cDNA or wt-p53 siRNA. The PRAME siRNA and its control were transfected with the K562 cells. The PRAME siRNA transfected K562 cells were then transiently transfected with S100A4 siRNA or pGMp53-Lu. PRAME, S100A4 and P53 were detected by Western blot assay in different time point. Annexin V/propidium iodide and MTT methods were used to detect apoptosis and cell survival rate. RESULTS: KG-1 cells overexpressing the PRAME gene significantly induces apoptosis and decreases proliferation in vitro, followed by down-regulation of S100A4 and up-regulation of p53. Up-regulation of S100A4 by S100A4 transfection inhibits PRAME-induced p53 up-regulation. Furthermore, up-regulation of S100A4 by S100A4 transfection or down-regulation of p53 by p53 siRNA transfection reduces apoptosis and increases proliferation in vitro. Knockdown of PRAME in K562 cells significantly increases proliferation in vitro, followed by up-regulation of S100A4 and down-regulation of p53. The downregulation of S100A4 by S100A4 siRNA transfection increased p53 expression. Furthermore, downregulation of S100A4 by S100A4 siRNA transfection or up-regulation of p53 by p53 transfection decreases proliferation in vitro. CONCLUSIONS: Our results suggest that the leukemias expressing high levels of PRAME has a favorable prognosis. PRAME promotes in vitro leukemia cells death by regulating S100A4/p53 signaling.

Genetic and molecular analyses of picA, a plant-inducible locus on the Agrobacterium tumefaciens chromosome.

picA is an Agrobacterium tumefaciens chromosomal locus, identified by Mu d11681 mutagenesis, that is inducible by certain acidic polysaccharides found in carrot root extract. Cloning and genetic analysis of a picA::lacZ fusion defined a region of the picA promoter that is responsible for the induction of this locus. Furthermore, we identified a possible negative regulator of picA expression upstream of the picA locus. This sequence, denoted pgl, has extensive homology to polygalacturonase genes from several organisms and inhibited the induction of the picA promoter when present in multiple copies in A. tumefaciens. DNA sequence analysis indicated at least two long open reading frames (ORFs) in the picA region. S1 nuclease mapping was used to identify the transcription initiation site of picA. Mutation of ORF1, but not ORF2, of the picA locus was responsible for an increased aggregation of A. tumefaciens, forming "ropes" in the presence of pea root cap cells. In addition, a potato tuber disk virulence assay indicated that a preinduced picA mutant was more virulent than was the wild-type control, a further indication that the picA locus regulates the surface properties of the bacterium in the presence of plant cells or plant cell extracts.