Brain tumors induced in rats by human adenovirus type 12

Oncogenesis of human adenovirus type 12 in the brain of rats was examined. Newborn rats of Sprague-Dawley and Donryu&#12288;strains were injected intracranially with human adenovirus type 12.&#12288;The incidence of intracranial tumors was 91% (30/33) in SpragueDawley&#12288;and 56% (14/25) in Donryu rats. Except for one tumor nodule&#12288;located in the parietal cortex of a Sprague.Dawley rat, all tumors&#12288;developed in the paraventricular areas or in the meninges. Tumors were quite similar histologically to those induced in hamsters and&#12288;mice resembling the undifferentiated human brain tumors such as medulloblastoma,&#12288;ependymoblastoma and embryonic gliomas. From&#12288;the histological features and primary sites of tumor development, it is&#12288;suggested that the tumors in the brain of rats induced by adenovirus type 12 originate from the embryonic cells in the&#12288;paraventricular area&#12288;and also from the undifferentiated supporting cells of the peripheral&#12288;nerves in the&#12288;leptomeninges.</p

Magnetization Plateaus in the Spin-1/2 Kagome Antiferromagnets: Volborthite and Vesignieite

The magnetization of two spin-1/2 kagome antiferromagnets, volborthite and vesignieite, has been measured in pulsed magnetic fields up to 68 T. A magnetization plateau is observed for each compound near the highest magnetic field. Magnetizations at saturation are approximately equal to 0.40Ms for both compounds, where Ms is the fully saturated magnetization, irrespective of a difference in the distortion of the kagome lattice between the two compounds. It should be noted that these values of magnetizations are significantly larger than Ms/3 predicted theoretically for the one-third magnetization plateau in the spin-1/2 kagome antiferromagnet. The excess magnetization over Ms/3 is nearly equal to the sum of the magnetizations gained at the second and third magnetization steps in volborthite, suggesting that there is a common origin for the excess magnetization and the magnetization steps.Comment: 4 pages, 4 figures. Phys. Rev. B, accepte

Open String on Symmetric Product

We develop some basic properties of the open string on the symmetric product which is supposed to describe the open string field theory in discrete lightcone quantization (DLCQ). After preparing the consistency conditions of the twisted boundary conditions for Annulus/M\"obius/Klein Bottle amplitudes in generic non-abelian orbifold, we classify the most general solutions of the constraints when the discrete group is $S_N$. We calculate the corresponding orbifold amplitudes from two viewpoints -- from the boundary state formalism and from the trace over the open string Hilbert space. It is shown that the topology of the world sheet for the short string and that of the long string in general do not coincide. For example the annulus sector for the short string contains all the sectors (torus, annulus, Klein bottle, M\"obius strip) of the long strings. The boundary/cross-cap states of the short strings are classified into three categories in terms of the long string, the ordinary boundary and the cross-cap states, and the ``joint'' state which describes the connection of two short strings. We show that the sum of the all possible boundary conditions is equal to the exponential of the sum of the irreducible amplitude -- one body amplitude of long open (closed) strings. This is typical structure of DLCQ partition function. We examined that the tadpole cancellation condition in our language and derived the well-known gauge group $SO(2^{13})$.Comment: 56 pages, 11 figures, Late

Pan-Vertebrate Toll-Like Receptors During Evolution

Human toll-like receptors (TLRs) recognize pathogen-associated molecular patterns (PAMPs) to raise innate immune responses. The human TLR family was discovered because of its sequence similarity to fruit fly (Drosophila) Toll, which is involved in an anti-fungal response. In this review, we focus on the origin of the vertebrate TLR family highlighted through functional and phylogenetic analyses of TLRs in non-mammalian vertebrates. Recent extensive genome projects revealed that teleosts contain almost all subsets of TLRs that correspond to human TLRs (TLR1, 2, 3, 4, 5, 7, 8, and 9), whereas the urochordate Ciona intestinalis contains only a few TLR genes. Therefore, mammals likely obtained almost all TLR family members at the beginning of vertebrate evolution. This premise is further supported by several functional analyses of non-mammalian TLRs. We have summarized several teleost TLRs with unique properties distinct from mammalian TLRs to outline their specific roles. According to Takifugu rubripes genome project, the puffer fish possesses fish-specific TLR21 and 22. Surprisingly, phylogenetic analyses indicate that TLR21 and 22 emerged during an early period of vertebrate evolution in parallel with other TLRs and that the mammalian ancestor lost TLR21 and 22 during evolution. Our laboratory recently revealed that TLR22 recognizes double-strand RNA and induces interferon production through the TICAM-1 adaptor, as in TLR3, but unlike TLR3, TLR22 localizes to the cell surface. Therefore, differential expression of TLR3 and TLR22, rather than simple redundancy of RNA sensors, may explain the effective protection of fish from RNA virus infection in the water. In this review, we summarize the similarities and differences of the TLR family in various vertebrates and introduce these unique TLRs for a possible application to the field of clinical practices for cancer or virus infection

Comparison of Protein Profiles of Gingival Crevicular Fluids Collected from Incisors, Canines, and Molars

Many studies have shown that gingival crevicular fluid （GCF） reflects the inflammatory state of local periodontal tissues. GCF has been collected from several types of teeth in previous studies. However, there is no report that characterizes GCF by the type of tooth. In the present study, the protein profiles of GCF from different sites were comprehensively compared with each other. GCF was sampled from six healthy adult men （21-31 years old） with healthy periodontal tissues. Three separate GCF samples were collected at the maxillary central incisor, canine, and first molar of each individual. The protein profiles of GCF were analyzed using sodium dodecyl sulfate polyacrylamide gel electrophoresis and liquid chromatogram-tandem mass spectrometry （LC-MS/MS）. The band patterns on the sodium dodecyl sulfate polyacrylamide gel electrophoresis from the set of three GCF samples from each individual were similar, regardless of the type of tooth. The proteins contained in each band were identified by LC-MS/MS analysis, and they were found to be the same among the three GCF samples. A comprehensive and quantitative analysis of proteins in the GCF samples was performed by LC-MS/MS using isobaric tag labeling. In total, 86 proteins were identified in GCF. A small number of proteins were increased or decreased in GCF from the first molars compared with the other types of teeth in one or two individuals. However, overall, no proteins were found to exhibit a reproducibly different composition in any of the individuals. These analyses show that the protein profiles of GCF in healthy periodontal tissues are similar, regardless of the type of tooth