University of Tsukuba

About: University of Tsukuba is a education organization based out in Tsukuba, Ibaraki, Japan. It is known for research contribution in the topics: Population & Gene. The organization has 36352 authors who have published 79483 publications receiving 1934752 citations. The organization is also known as: Tsukuba daigaku & Tsukuba University.

Suppression of hadrons with large transverse momentum in central Au + Au collisions at √sNN = 130 GeV

Abstract: Transverse momentum spectra for charged hadrons and for neutral pions in the range 1 Gev/c < P-T < 5 GeV/c have been measured by the PHENIX experiment at RHIC in Au + Au collisions at rootS(NN) = 130 GeV. At high p(T) the spectra from peripheral nuclear collisions are consistent with scaling the spectra from p + p collisions by the average number of binary nucleon-nucleon collisions. The spectra from central collisions are significantly suppressed when compared to the binary-scaled p + p expectation, and also when compared to similarly binary-scaled peripheral collisions, indicating a novel nuclear-medium effect in central nuclear collisions at RHIC energies.

Keap1-null mutation leads to postnatal lethality due to constitutive Nrf2 activation

Abstract: Transcription factor Nrf2 (encoded by Nfe2l2) regulates a battery of detoxifying and antioxidant genes, and Keap1 represses Nrf2 function. When we ablated Keap1, Keap1-deficient mice died postnatally, probably from malnutrition resulting from hyperkeratosis in the esophagus and forestomach. Nrf2 activity affects the expression levels of several squamous epithelial genes. Biochemical data show that, without Keap1, Nrf2 constitutively accumulates in the nucleus to stimulate transcription of cytoprotective genes. Breeding to Nrf2-deficient mice reversed the phenotypic Keap1 deficiencies. These experiments show that Keap1 acts upstream of Nrf2 in the cellular response to oxidative and xenobiotic stress.

Phase-contrast X-ray computed tomography for observing biological soft tissues.

Abstract: Biological soft tissues are almost transparent to hard X rays and therefore cannot be investigated without enhancement with a contrast medium, such as iodine. On the other hand, phase–contrast X–ray imaging is sensitive to light elements1–8. This is because the X–ray phase shift cross section is almost a thousand times larger than the X–ray absorption cross section for light elements such as hydrogen, carbon, nitrogen and oxygen4,5. Hence, phase–contrast X–ray imaging is a promising technique for observing the structure inside biological soft tissues without the need for staining and without serious radiation exposure. We have devised a means of observing biological tissues in three dimensions using a novel X–ray computed tomography (CT) by modifying the phase–contrast technique. To generate appropriate CT input data, we used phase–mapping images obtained using an X–ray interferometer6 and computer analysis of interference patterns9. Now, we present a three–dimensional observation result of a nonstained sample of a cancerous rabbit liver, using a synchrotron X–ray source. Phase–contrast X–ray CT was able to clearly differentiate the cancer lesion from the normal tissue. Moreover, fine structures corresponding to cancerous degeneration and fibrous tissues were clearly depicted.

Oxidative and electrophilic stresses activate Nrf2 through inhibition of ubiquitination activity of Keap1.

Abstract: The Keap1-Nrf2 system is the major regulatory pathway of cytoprotective gene expression against oxidative and/or electrophilic stresses. Keap1 acts as a stress sensor protein in this system. While Keap1 constitutively suppresses Nrf2 activity under unstressed conditions, oxidants or electrophiles provoke the repression of Keap1 activity, inducing the Nrf2 activation. However, the precise molecular mechanisms behind the liberation of Nrf2 from Keap1 repression in the presence of stress remain to be elucidated. We hypothesized that oxidative and electrophilic stresses induce the nuclear accumulation of Nrf2 by affecting the Keap1-mediated rapid turnover of Nrf2, since such accumulation was diminished by the protein synthesis inhibitor cycloheximide. While both the Cys273 and Cys288 residues of Keap1 are required for suppressing Nrf2 nuclear accumulation, treatment of cells with electrophiles or mutation of these cysteine residues to alanine did not affect the association of Keap1 with Nrf2 either in vivo or in vitro. Rather, these treatments impaired the Keap1-mediated proteasomal degradation of Nrf2. These results support the contention that Nrf2 protein synthesized de novo after exposure to stress accumulates in the nucleus by bypassing the Keap1 gate and that the sensory mechanism of oxidative and electrophilic stresses is closely linked to the degradation mechanism of Nrf2.