Institution
Kumamoto University
Education•Kumamoto, Kumamoto, Japan•
About: Kumamoto University is a education organization based out in Kumamoto, Kumamoto, Japan. It is known for research contribution in the topics: Population & Cancer. The organization has 19602 authors who have published 35513 publications receiving 901260 citations. The organization is also known as: Kumamoto Daigaku.
Topics: Population, Cancer, Cell culture, Stem cell, Cellular differentiation
Papers published on a yearly basis
Papers
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TL;DR: Department of Urology, Fukushima Medical University, Fukushima, Department of Urolog, Shinshu University School of Medicine, Matsumoto, Nagano, University of Yamanashi Interdisciplinary Graduate School of medicine and Engineering, Chuo,Yamanashi.
Abstract: Department of Urology, Fukushima Medical University, Fukushima, Department of Urology, Shinshu University School of Medicine, Matsumoto, Nagano, Department of Urology, University of Yamanashi Interdisciplinary Graduate School of Medicine and Engineering, Chuo, Yamanashi, Department of Urology, University of Fukui Faculty of Medicine, Fukui, Department of Urology, University of Tokyo Faculty of Medicine, Tokyo, Department of Urology, Asahikawa Medical College, Asahikawa, Hokkaido, Department of Urology, Niigata University School of Medicine, Niigata, Department of Urology, Nagoya University Graduate School of Medicine, Nagoya, Aichi, Department of Urology, Graduate School of Medical Science, Kyushu University, Fukuoka, Department of Urology, Graduate School of medical Science, Kumamoto University, Kumamoto, Japan
163 citations
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TL;DR: The findings suggest that a redox change in HSA is related to the oxidation of several amino acid residues by different oxidants, and the ratio of the oxidized form to the normal form of albumin (HMA/HNA) could serve as a useful marker for evaluating systemic redox states, which would be useful for the evaluation of disease progression and therapeutic efficacy.
163 citations
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TL;DR: Evidence is provided that STAT3 plays an essential role in cytokine‐driven SAA expression, although the human SAA gene shows no typical STAT3 response element (RE) in its promoters, which is expected to aid the understanding of the inflammatory status of AA amyloidosis.
Abstract: Serum amyloid A (SAA) is a sensitive marker of acute-phase responses and known as a precursor protein of amyloid fibril in amyloid A (AA) (secondary) amyloidosis. Since the serum SAA level is also closely related to activity of chronic inflammatory disease and coronary artery disease, it is important to clarify the exact induction mechanism of SAA from the clinical point of view. Here we provide evidence that STAT3 plays an essential role in cytokine-driven SAA expression, although the human SAA gene shows no typical STAT3 response element (RE) in its promoters. STAT3 and nuclear factor κB (NF-κB) p65 first form a complex following interleukin (IL)-1 and IL-6 (IL-1+6) stimulation, after which STAT3 interacts with nonconsensus sequences at a 3′ site of the SAA gene promoter's NF-κB RE. Moreover, co-expression of p300 with STAT3 dramatically enhances the transcriptional activity of SAA. The formation of a complex with STAT3, NF-κB p65, and p300 is thus essential for the synergistic induction of the SAA gene by IL-1+6 stimulation. Our findings are expected to aid the understanding of the inflammatory status of AA amyloidosis to aid development of a therapeutic strategy for this disease by means of normalization of serum SAA levels.
163 citations
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TL;DR: Analysis of the expression of various genes that are thought to regulate serum Ca(++) levels in ATL showed that the overexpression of the receptor activator of nuclear factor kappaB (RANK) ligand gene correlated with hypercalcemia, and suggested that ATL cells induce the differentiation of HPCs to OCLs through RANKL expressed on their surface, in cooperation with M-CSF, and ultimately cause hyperCalcemia.
163 citations
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TL;DR: The results suggest that Rho-kinase is essential not only for actomyosin regulation but also for segregation of glial filaments into daughter cells which in turn ensures correct cytokinetic processes.
Abstract: Rho-associated kinase (Rho-kinase), which is activated by the small GTPase Rho, regulates formation of stress fibers and focal adhesions, myosin fiber organization, and neurite retraction through the phosphorylation of cytoskeletal proteins, including myosin light chain, the ERM family proteins (ezrin, radixin, and moesin) and adducin. Rho-kinase was found to phosphorylate a type III intermediate filament (IF) protein, glial fibrillary acidic protein (GFAP), exclusively at the cleavage furrow during cytokinesis. In the present study, we examined the roles of Rho-kinase in cytokinesis, in particular organization of glial filaments during cytokinesis. Expression of the dominant-negative form of Rho-kinase inhibited the cytokinesis of Xenopus embryo and mammalian cells, the result being production of multinuclei. We then constructed a series of mutant GFAPs, where Rho-kinase phosphorylation sites were variously mutated, and expressed them in type III IF-negative cells. The mutations induced impaired segregation of glial filament (GFAP filament) into postmitotic daughter cells. As a result, an unusually long bridge-like cytoplasmic structure formed between the unseparated daughter cells. Alteration of other sites, including the cdc2 kinase phosphorylation site, led to no remarkable defect in glial filament separation. These results suggest that Rho-kinase is essential not only for actomyosin regulation but also for segregation of glial filaments into daughter cells which in turn ensures correct cytokinetic processes.
163 citations
Authors
Showing all 19645 results
Name | H-index | Papers | Citations |
---|---|---|---|
Fred H. Gage | 216 | 967 | 185732 |
George D. Yancopoulos | 158 | 496 | 93955 |
Kenji Kangawa | 153 | 1117 | 110059 |
Tasuku Honjo | 141 | 712 | 88428 |
Hideo Yagita | 137 | 946 | 70623 |
Masashi Yanagisawa | 130 | 524 | 83631 |
Kazuwa Nakao | 128 | 1041 | 70812 |
Kouji Matsushima | 124 | 590 | 56995 |
Thomas E. Mallouk | 122 | 549 | 52593 |
Toshio Hirano | 120 | 401 | 55721 |
Eisuke Nishida | 112 | 349 | 45918 |
Hiroaki Shimokawa | 111 | 949 | 48822 |
Bernd Bukau | 111 | 271 | 38446 |
Kazuo Tsubota | 105 | 1379 | 48991 |
Toshio Suda | 104 | 580 | 41069 |