Procalcitonin (PCT) is a marker of severe bacterial infections and organ failure due to sepsis. The purpose of the present study was to identify the appropriate cutoff level of PCT based on the findings of a blood culture and polymerase chain reaction (PCR). The PCT levels were measured in 116 patients in an intensive care unit who were suspected of having bacteremia, to examine its relationship with a blood culture or PCR. The PCT levels were significantly high in patients with bacteremia, but they were also moderately high in some patients who were positive for fungus DNA. The area under the curve was significantly higher for PCT than for C-reactive protein. The appropriate cutoff values of PCT for bacteremia were 0.38 microg/L for the high negative predictive value and 0.83 microg/L for the high positive predictive value. Procalcitonin was slightly related to mortality, and the combination of a blood culture and PCR was thus found to increase the sensitivity for mortality. These findings suggest that PCT is useful for the diagnosis of bacteremia and that the diagnostic value of PCT in combination a with blood culture and PCR for bacterial infection or mortality further increases.

An Aβ42 analog crosslinked within the molecule at the 17th and 28th amino acid residues exhibited high aggregative ability and potent neurotoxicity comparable to those of E22P-Aβ42.

Our panfungal PCR approach allows for the highly sensitive and specific detection and identification of a wide spectrum of fungal pathogens, which provides indispensable information for managing IFDs, especially refractory or breakthrough IFDs during antifungal therapy in high-risk patients with haematologic disorders.

Rare-earth-free phosphors based on vanadate compounds were investigated, where the vanadates included chloride vanadates (M II 2 VO 4 Cl), pyrovanadates (M II 2 V 2 O 7 ), orthovanadates (M II 3 (VO 4 ) 2 ) with divalent cations M II of Mg, Sr, Ba, and Zn, and oxofluorovanadates (A I VOF 4 ) with an alkali metal A I . A chloride pyrolysis method and a liquid phase precipitation method were proposed for preparing the chloride vanadates and pyro-and orthovanadates, respectively. These vanadate compounds showed self-activated photoluminescence (PL) based on the VO 4 clusters against the ultraviolet (UV) light irradiation. The colors of PL covered almost the whole visible-light region from blue to yellow as Sr 2 VO 4 Cl (deep blue), Ca 2 VO 4 Cl (sky blue), Ba 2 V 2 O 7 (green), Sr 2 V 2 O 7 (yellowish green), Zn 3 (VO 4 ) 2 (yellow), and Mg 3 (VO 4 ) 2 (yellow). A correlation was suggested from these compounds between the luminescent colors and the structural feature as the longer V-O distances in the VO 4 tetrahedra in the crystal structures led to the longer wavelength in PL. This seemed to be also applicable for the oxofluorovanadates A I VOF 4 (A I = K and Cs) which contain the VOF 4 polyhedra with one O 2ion and four Fions as the ligands, as they exhibited the reddish PL.

Rapid weight reduction reduced the wrestlers' cross-sectional areas of muscle and fat tissues, which tended to recover through rehydration after the weigh-in. These results suggest that rapid weight reduction of wrestlers induced changes in different regions of the body.

The fluorite-related cubic structure of yttria-stabilized zirconia, Zr(0.75)(8)Y(0.24)(2)O(1.87)(9), has been studied by single-crystal X-ray diffraction using synchrotron radiation and by EXAFS. Two diffraction data sets obtained at X-ray energies of 512 and 10 eV below the Y K edge revealed that in the average structure Zr atoms are displaced from the origin of the space group Fm3;m along <111> by 0.19 Å, while Y atoms reside at the origin. Approximately 48% of the O atoms occupy the ideal position in the fluorite-type structure, while 43% of O atoms are displaced from the ideal position along <001> by 0.31 Å. The remaining 9% of O atoms are presumably sited at interstitial positions. Local structures around Zr and Y are investigated by combining the results of single-crystal X-ray diffraction and EXAFS studies.

Characterization of amyloid β (Aβ) oligomers, the transition species present prior to the formation of Aβ fibrils and that have cytotoxicity, has become one of the major topics in the investigations of Alzheimer’s disease (AD) pathogenesis. However, studying pathophysiological properties of Aβ oligomers is challenging due to the instability of these protein complexes in vitro. Here, we report that conformation-restricted Aβ42 with an intramolecular disulfide bond at positions 17 and 28 (SS-Aβ42) formed stable Aβ oligomers in vitro. Thioflavin T binding assays, nondenaturing gel electrophoresis, and morphological analyses revealed that SS-Aβ42 maintained oligomeric structure, whereas wild-type Aβ42 and the highly aggregative Aβ42 mutant with E22P substitution (E22P-Aβ42) formed Aβ fibrils. In agreement with these observations, SS-Aβ42 was more cytotoxic compared to the wild-type and E22P-Aβ42 in cell cultures. Furthermore, we developed a monoclonal antibody, designated TxCo-1, using the toxic conformation of SS-Aβ42 as immunogen. X-ray crystallography of the TxCo-1/SS-Aβ42 complex, enzyme immunoassay, and immunohistochemical studies confirmed the recognition site and specificity of TxCo-1 to SS-Aβ42. Immunohistochemistry with TxCo-1 antibody identified structures resembling senile plaques and vascular Aβ in brain samples of AD subjects. However, TxCo-1 immunoreactivity did not colocalize extensively with Aβ plaques identified with conventional Aβ antibodies. Together, these findings indicate that Aβ with a turn at positions 22 and 23, which is prone to form Aβ oligomers, could show strong cytotoxicity and accumulated in brains of AD subjects. The SS-Aβ42 and TxCo-1 antibody should facilitate understanding of the pathological role of Aβ with toxic conformation in AD.

Amyloid β (Aβ) oligomers play a critical role in the pathology of Alzheimer's disease. Recently, we reported that a conformation‐restricted Aβ42 with an intramolecular disulfide bond through cysteine residues at positions 17/28 formed stable oligomers with potent cytotoxicity. To further optimize this compound as a toxic conformer model, we synthesized three analogues with a combination of cysteine and homocysteine at positions 17/28. The analogues with Cys‐Cys, Cys‐homoCys, or homoCys‐Cys, but not the homoCys‐homoCys analogue, exhibited potent cytotoxicity against SH‐SY5Y and THP‐1 cells even at 10 nM. In contrast, the cytotoxicity of conformation‐restricted analogues at positions 16/29 or 18/27 was significantly weaker than that of wild‐type Aβ42. Furthermore, thioflavin‐T assay, non‐denaturing gel electrophoresis, and morphological studies suggested that the majority of these conformation‐restricted analogues exists in an oligomeric state in cell culture medium, indicating that the toxic conformation of Aβ42, rather than the oligomeric state, is essential to induce cytotoxicity.