Entity

Time filter

Source Type

Morohongo, Japan

Nihon Institute of Medical Science is a private university in Moroyama, Saitama, Japan, established in 2007. The predecessor of the school, a vocational school, was founded in 1960. It is located next to Josai University in neighboring Sakado, Saitama. Wikipedia.


Taniguchi Y.,University of Tsukuba | Taniguchi Y.,Nihon Institute of Medical Science
Physical Review C - Nuclear Physics | Year: 2014

The structures of excited states in S34 are investigated using the antisymmetrized molecular dynamics and generator coordinate method (GCM). The GCM basis wave functions are calculated via energy variation with a constraint on the quadrupole deformation parameter β. By applying the GCM after parity and angular momentum projections, the coexistence of two positive- and one negative-parity superdeformed (SD) bands are predicted, and low-lying states and other deformed bands are obtained. The SD bands have structures of O16+O16 + two valence neutrons in molecular orbitals around the two O16 cores in a cluster picture. The configurations of the two valence neutrons are δ2 and π2 for the positive-parity SD bands and π1δ1 for the negative-parity SD band. The structural changes of the yrast states are also discussed. © 2014 American Physical Society. Source


Chiba Y.,Hokkaido University | Kimura M.,Hokkaido University | Taniguchi Y.,Nihon Institute of Medical Science
Physical Review C - Nuclear Physics | Year: 2016

Background: The sharp 1- resonances with enhanced isoscalar dipole transition strengths are observed in many light nuclei at relatively small excitation energies, but their nature has been unclear. Purpose: We show those resonances can be attributed to the cluster states with asymmetric configurations such as α+O16. We explain why asymmetric cluster states are strongly excited by the isoscalar dipole transition. We also provide a theoretical prediction of the isoscalar dipole transitions in Ne20 and Ti44. Method: The transition matrix is analytically derived to clarify the excitation mechanism. The nuclear model calculations by Brink-Bloch wave function and antisymmetrized molecular dynamics are also performed to provide a theoretical prediction for Ne20 and Ti44. Results: It is shown that the transition matrix is as large as the Weisskopf estimate even though the ground state is an ideal shell-model state. Furthermore, it is considerably amplified if the ground state has cluster correlation. The nuclear model calculations predict large transition matrix to the α+O16 and α+Ca40 cluster states comparable with or larger than the Weisskopf estimate. Conclusions: We conclude that the asymmetric cluster states are strongly excited by the isoscalar dipole transition. Combined with the isoscalar monopole transition that populates the 0+ cluster states, the isoscalar transitions are promising probes for asymmetric clusters. © 2016 American Physical Society. Source


Yokomori H.,Kitasato Medical Center Hospital | Oda M.,International University of Health and Welfare | Yoshimura K.,Nihon Institute of Medical Science | Hibi T.,Keio University
Micron | Year: 2012

Ultrastructure reports have described that liver sinusoidal endothelial cell (LSEC)s contain a cytoskeletal framework of filamentous actin. Small G protein has emerged as an important regulator of the actin cytoskeleton, and consequently, of cell morphology and motility. We investigated actin filaments in relation to SEF in LSECs using a heavy meromyosin-decorated reaction and thereby elucidated the roles of small G protein and actin cytoskeleton in the morphological and functional alterations of SEF. Caveolin-1 expression has also been found in fenestrations with many characteristics of liver sinusoidal endothelial cells. Currently, fenestral studies and human disease are revealing ways to increase the liver sieve's porosity, which is reduced through pathological mechanisms. Hepatic sinusoidal endothelial dysfunction, which is known to impair endothelium-dependent relaxation in the liver microcirculation, contributes to increased intrahepatic vascular resistance. © 2011 Elsevier Ltd. Source


Yokomori H.,Kitasato University | Oda M.,International University of Health and Welfare | Yoshimura K.,Nihon Institute of Medical Science | MacHida S.,Saitama University | And 2 more authors.
Journal of Gastroenterology | Year: 2011

Background: The apelin receptor (APJ) is related to angiotensin-like- receptor 1 (AGTRL1). This study was designed to elucidate the in vivo localization and changes of APJ in cirrhotic liver, and the in vitro changes of APJ expression in cultured hepatic stellate cells (HSCs) and capillarized sinusoidal endothelial cells (SECs) activated by growth factors. Methods: In vivo studies used control liver samples, cirrhotic liver samples from patients with Child's A cirrhosis undergoing surgical resection (Child-A-LC), and cirrhotic liver samples from autopsied cases of decompensated Child's C cirrhosis (Child-C-LC). Immunohistochemical (IHC), Western blot, laser-capture microdissection (LCM) coupled with reverse transcription -polymerase chain reaction (RT-PCR), and immunoelectron microscopic (IEM) studies for APJ expression were conducted. In vitro examinations used commercial human HSCs and SECs. APJ expression was examined in cultured HSCs activated by growth factors and in capillarized SECs activated by angiogenic factors. Results: The IHC study of liver samples revealed only slight APJ expression in hepatic sinusoids in control liver tissue. In cirrhotic liver (Child-A-LC and Child-C-LC), APJ expression was evident mainly along the sinusoids and on portal fibroblasts in fibrotic septa. Western blot analysis of whole-liver homogenate and LCM-PCR of sinusoids revealed overexpression of APJ in Child-C-LC samples. The results of IEM studies showed that APJ expression was increased significantly on HSCs, but it was sparse on SECs in Child-C-LC tissue. In vitro examination revealed that APJ was overexpressed in cultured HSCs activated by platelet-derived growth factor-β. Conclusions: Enhanced expression of APJ on HSCs in cirrhosis indicates markedly increased vascular remodeling. © 2010 Springer. Source


Yokomori H.,Kitasato University | Oda M.,International University of Health and Welfare | Yoshimura K.,Nihon Institute of Medical Science | Hibi T.,Keio University
Hepatology Research | Year: 2012

Aim: Apelin (APLN), the endogenous ligand of angiotensinlike receptor 1 (APJ), is a peptide necessary for embryonic and tumor angiogenesis. Little is known about the localization and changes of APLN expression including the sinusoids in human cirrhotic liver, which might contribute to portal hypertension. This study was designed to elucidate the localization and change of APLN expression in human liver during the progression of cirrhosis. Methods: Twelve normal liver specimens, eight specimens of Child-Pugh grade A cirrhosis, and 10 specimens of Child- Pugh grade C cirrhosis were studied. APLN protein and gene expression was examined by immunohistochemistry, western blotting, immunoelectronic microscopy, and laser captured microdissection (LCM) followed by polymerase chain reaction (PCR) in sinusoid. Results: In control liver tissue, APLN was localized mainly on arterial endothelial cells and hepatic arterioles in the portal tract. In cirrhotic liver tissue, aberrant APLN expression was observed in periportal capillary endothelial cells corresponding to capillarized sinusoids, and in proliferated arterial capillaries in the fibrotic septa. Significant overexpression of APLN at protein level in cirrhotic liver was demonstrated by western blotting (P < 0.01 Child-Pugh A and C versus control, P < 0.01 Child-Pugh A versus C). APLN mRNA expression in the sinusoid was confirmed by LCM-PCR. Conclusion: In humans, APLN protein and gene were overexpressed in cirrhotic liver compared with normal liver, and the magnitude increased as cirrhosis progressed. Especially in end-stage cirrhosis, APLN was strongly expressed in proliferated arterial capillaries directly connected with the sinusoids, suggesting a role of APLN in the proliferation of arterial capillaries in cirrhosis. © 2012 The Japan Society of Hepatology. Source

Discover hidden collaborations