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290 results on '"Higashimoto, Yuichiro"'

1. Erythropoiesis stimulating agents are associated with serum fibroblast growth factor 23 metabolism in patients on hemodialysis.

Author

Honda, Hirokazu, Tanaka, Kenji, Michihata, Tetsuo, Shibagaki, Keigo, Yuza, Toshitaka, Hirao, Keiichi, Tomosugi, Naohisa, Ganz, Tomas, and Higashimoto, Yuichiro

Subjects
erythroferrone, erythropoiesis, hepcidin 25, iron metabolism, phosphate
Abstract

BACKGROUND: This study aimed to determine associations among short- and long-acting erythropoiesis stimulating agents (ESAs), changes in serum fibroblast growth factor 23 (FGF23) and biomarkers of iron metabolism. METHODS: Among 108 patients on hemodialysis (HD), 44 received every 2 weeks or monthly doses of continuous erythropoiesis receptor activator (CERA), 31 received weekly doses of darbepoetin-α, 24 received three doses per week of epoetin-β and 9 were not treated with an ESA. Intact and C-terminal FGF23 and transferrin saturation (TSAT), ferritin, erythroferrone and hepcidin 25 were measured in blood samples collected before the HD session at the end of the dialysis week (baseline, Day 0) and on Days 3, 5, 7 and 14 thereafter. RESULTS: Levels of ferritin, hepcidin 25 and erythroferrone as well as TSAT were significantly decreased or elevated in patients treated with CERA compared with other types of ESAs. Levels of C-terminal FGF23 increased in all groups during the observation period. Levels of intact FGF23 and ratios of intact FGF23 to C-terminal FGF23 gradually decreased between Days 3 and 7 in the CERA but not in the other groups. Multivariate models associated changes in hepcidin 25 and phosphate with those of intact FGF23. CONCLUSION: The long-acting ESA CERA might influence levels of intact FGF23 by increasing FGF23 cleavage in patients on HD in association with prolonged hepcidin 25 suppression.

Published
2021

2. DNA Aptamer raised against Advanced Glycation End Products Improves Sperm Concentration, Motility, and Viability by Suppressing RAGE-induced Oxidative Stress and Inflammation in Testes of Diabetic Mice

Author

Mori, Yusaku, primary, Terasaki, Michishige, additional, Osaka, Naoya, additional, Fujikawa, Tomoki, additional, Yashima, Hironori, additional, Saito, Tomomi, additional, Kataoka, Yurie, additional, Ohara, Makoto, additional, Higashimoto, Yuichiro, additional, Matsui, Takanori, additional, and Yamagishi, Sho-ichi, additional

Published
2024
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3. DNA Aptamer Raised against Advanced Glycation End Products Improves Sperm Concentration, Motility, and Viability by Suppressing Receptors for Advanced Glycation End Product-Induced Oxidative Stress and Inflammation in the Testes of Diabetic Mice.

Author

Mori, Yusaku, Terasaki, Michishige, Osaka, Naoya, Fujikawa, Tomoki, Yashima, Hironori, Saito, Tomomi, Kataoka, Yurie, Ohara, Makoto, Higashimoto, Yuichiro, Matsui, Takanori, and Yamagishi, Sho-ichi

Subjects
ADVANCED glycation end-products, SEMEN, RECEPTOR for advanced glycation end products (RAGE), SPERMATOZOA, SPERMATOGENESIS, ORCHITIS, OXIDATIVE stress, DIABETIC angiopathies, TYPE 2 diabetes
Abstract

Type 2 diabetes mellitus (T2DM) is a risk factor for male infertility, but the underlying molecular mechanisms remain unclear. Advanced glycation end products (AGEs) are pathogenic molecules for diabetic vascular complications. Here, we investigated the effects of the DNA aptamer raised against AGEs (AGE-Apt) on testicular and sperm abnormalities in a T2DM mouse model. KK-Ay (DM) and wild-type (non-DM) 4- and 7-week-old male mice were sacrificed to collect the testes and spermatozoa for immunofluorescence, RT-PCR, and histological analyses. DM and non-DM 7-week-old mice were subcutaneously infused with the AGE-Apt or control-aptamer for 6 weeks and were then sacrificed. Plasma glucose, testicular AGEs, and Rage gene expression in 4-week-old DM mice and plasma glucose, testicular AGEs, oxidative stress, and pro-inflammatory gene expressions in 7-week-old DM mice were higher than those in age-matched non-DM mice, the latter of which was associated with seminiferous tubular dilation. AGE-Apt did not affect glycemic parameters, but it inhibited seminiferous tubular dilation, reduced the number of testicular macrophages and apoptotic cells, and restored the decrease in sperm concentration, motility, and viability of 13-week-old DM mice. Our findings suggest that AGEs-Apt may improve sperm abnormality by suppressing AGE–RAGE-induced oxidative stress and inflammation in the testes of DM mice. [ABSTRACT FROM AUTHOR]

Published
2024
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4. Subcutaneous Infusion of DNA-Aptamer Raised against Advanced Glycation End Products Prevents Loss of Skeletal Muscle Mass and Strength in Accelerated-Aging Mice

Author

Mori, Yusaku, primary, Ohara, Makoto, additional, Terasaki, Michishige, additional, Osaka, Naoya, additional, Yashima, Hironori, additional, Saito, Tomomi, additional, Otoyama-Kataoka, Yurie, additional, Omachi, Takemasa, additional, Higashimoto, Yuichiro, additional, Matsui, Takanori, additional, Fukui, Tomoyasu, additional, and Yamagishi, Sho-ichi, additional

Published
2023
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16. Inhibitory effects of RAGE-aptamer on development of monocrotaline-induced pulmonary arterial hypertension in rats

Author

Nakamura, Kazufumi, primary, Akagi, Satoshi, additional, Ejiri, Kentaro, additional, Yoshida, Masashi, additional, Miyoshi, Toru, additional, Sakaguchi, Masakiyo, additional, Amioka, Naofumi, additional, Suastika, Luh Oliva Saraswati, additional, Kondo, Megumi, additional, Nakayama, Rie, additional, Takaya, Yoichi, additional, Higashimoto, Yuichiro, additional, Fukami, Kei, additional, Matsubara, Hiromi, additional, and Ito, Hiroshi, additional

Published
2021
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18. Association of advanced glycation end products with sarcopenia and frailty in chronic kidney disease

Author

Keiichi Wakabayashi, Tomoyuki Otsuka, Tomoyasu Kadoguchi, Seiji Ueda, Higashimoto Yuichiro, Nao Nohara, Tomohito Gohda, Hajime Nagasawa, Junko Yabuuchi, Sho-ichi Yamagishi, Yusuke Suzuki, and Takanori Matsui

Subjects
0301 basic medicine, Glycation End Products, Advanced, Male, medicine.medical_specialty, Sarcopenia, medicine.medical_treatment, Blotting, Western, lcsh:Medicine, 030204 cardiovascular system & hematology, Gastroenterology, Article, 03 medical and health sciences, Mice, 0302 clinical medicine, Insulin resistance, Glycation, Internal medicine, medicine, Animals, Humans, Endothelial dysfunction, Renal Insufficiency, Chronic, lcsh:Science, Muscle, Skeletal, Pathological, Exercise, Dialysis, Aged, Multidisciplinary, Frailty, business.industry, lcsh:R, Health care, Middle Aged, medicine.disease, musculoskeletal system, Nephrectomy, Mice, Inbred C57BL, 030104 developmental biology, Nephrology, lcsh:Q, Female, business, Kidney disease
Abstract

Prevalence of sarcopenia is high in patients with chronic kidney disease (CKD), especially in those with dialysis. Various pathological conditions related to CKD, such as chronic inflammation, insulin resistance, and endothelial dysfunction, are thought to be associated with the development and progression of sarcopenia. Advanced glycation end products (AGE), one of the representative uremic toxins, have been shown to contribute to various CKD-associated complications. This study investigated the role of AGE in frailty and sarcopenia in patients and animals with CKD, respectively. In patients undergoing dialysis, serum AGE levels were significantly increased according to the frailty status and inversely associated with physical performance and activity. AGE accumulated in the gastrocnemius muscle of 5/6 nephrectomy mice in association with morphological abnormalities, capillary rarefaction, and mitochondrial dysfunction, all of which were completely inhibited by DNA-aptamer raised against AGE. Our present findings may suggest the pathological role of AGE in sarcopenia and frailty in CKD.

Published
2020

19. X-ray crystallographic and biochemical characterization of the inhibitory action of an iimidazole--dioxolane compound on heme oxygenase

Author

Sugishima, Masakazu, Higashimoto, Yuichiro, Oishi, Tohru, Takahashi, Hidenori, Sakamoto, Hiroshi, Noguchi, Masato, and Fukuyama, Keiichi

Subjects
X-ray crystallography -- Usage, Oxidases -- Structure, Oxidases -- Chemical properties, Hemoproteins -- Structure, Hemoproteins -- Research, Imidazole -- Chemical properties, Imidazole -- Structure, Biological sciences, Chemistry
Abstract

A study analyzes the X-ray crystallographic and biochemical characterization of the action of an iimidazole-dioxolane compound on heme oxygenase (HO), which is a potential therapeutic target in cancer. The analysis reveals that the catalytic reactions of the HO complexes stop completely in the presence of the imidazole-dioxolane compound, as verdoheme has lower reactivity with oxygen as compared to the heme.

Published
2007

20. Inhibitory effects of RAGE-aptamer on development of monocrotaline-induced pulmonary arterial hypertension in rats

Author

Nakamura, Kazufumi, Akagi, Satoshi, Ejiri, Kentaro, Yoshida, Masashi, Miyoshi, Toru, Sakaguchi, Masakiyo, Amioka, Naofumi, Suastika, Luh Oliva Saraswati, Kondo, Megumi, Nakayama, Rie, Takaya, Yoichi, Higashimoto, Yuichiro, Fukami, Kei, Matsubara, Hiromi, Ito, Hiroshi, Nakamura, Kazufumi, Akagi, Satoshi, Ejiri, Kentaro, Yoshida, Masashi, Miyoshi, Toru, Sakaguchi, Masakiyo, Amioka, Naofumi, Suastika, Luh Oliva Saraswati, Kondo, Megumi, Nakayama, Rie, Takaya, Yoichi, Higashimoto, Yuichiro, Fukami, Kei, Matsubara, Hiromi, and Ito, Hiroshi

Abstract

Background: The receptor for advanced glycation end products (RAGE), a transmembrane receptor belonging to the immunoglobulin superfamily, is overexpressed in pulmonary artery smooth muscle cells (PASMCs) in patients with pulmonary arterial hypertension (PAH) and is implicated in the etiology of PAH. Recently, we reported that RAGE-aptamer, a short and single-stranded DNA directed against RAGE, inhibited an inappropriate increase in cultured PASMCs in PAH. The aim of this study was to determine the efficacy of RAGEaptamer in monocrotaline-induced PAH in rats. Methods and Results: Rats were assigned to either an untreated control group, a group that received continuous subcutaneous administration of RAGE-aptamer immediately after monocrotaline injection, or a group that received control-aptamer immediately after monocrotaline injection. All rats survived 21 days after injection of monocrotaline and control-aptamer or RAGE-aptamer. Injection of monocrotaline with continuous subcutaneous delivery of control-aptamer resulted in higher right ventricular systolic pressure compared with controls. This increase was attenuated by continuous subcutaneous delivery of RAGE-aptamer. The proportion of small pulmonary arteries with full muscularization was greater in the monocrotaline and control-aptamer group than in the control group. Continuous subcutaneous delivery of RAGE-aptamer significantly reduced the percentage of small pulmonary arteries with full muscularization Conclusions: Continuous subcutaneous delivery of RAGE-aptamer suppresses development of monocrotaline-induced PAH in rats. Inhibition of RAGE ameliorates muscularization of 3 small pulmonary arteries. Treatment with RAGE-aptamer might be a new therapeutic option for PAH.

Published
2020

26. Initiation of a G2/M checkpoint after ultraviolet radiation requires p38 kinase

Author

Bulavin, Dmitry V., Higashimoto, Yuichiro, Popoff, Ian J., Gaarde, William A., Basrur, Venkatesha, Potapova, Olga, Appella, Ettore, and Fornace, Jr, Albert J.

Subjects
Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Author(s): Dmitry V. Bulavin [1]; Yuichiro Higashimoto [2]; Ian J. Popoff [3]; William A. Gaarde [3]; Venkatesha Basrur [2]; Olga Potapova [4]; Ettore Appella [2]; Albert J. Fornace, Jr (corresponding [...]

Published
2001
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29. PML regulates p53 acetylation and premature senescence induced by oncogenic Ras

Author

Pearson, Mark, Carbone, Roberta, Sebastiani, Carla, Cioce, Mario, Fagioli, Marta, Saito, Shin'ichi, Higashimoto, Yuichiro, Appella, Ettore, Minucci, Saverio, Pandolfi, Pier Paolo, and Pelicci, Pier Giuseppe

Subjects
Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Author(s): Mark Pearson [1]; Roberta Carbone [1]; Carla Sebastiani [2]; Mario Cioce [1]; Marta Fagioli [2]; Shin'ichi Saito [3]; Yuichiro Higashimoto [3]; Ettore Appella [3]; Saverio Minucci [1]; Pier Paolo [...]

Published
2000
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34. Influence of heparin molecular size on the induction of C- terminal unfolding in β2-microglobulin

Author

Fukasawa, Kanon, Higashimoto, Yuichiro, Motomiya, Yoshihiro, Uji, Yoshinori, and Ando, Yukio

Subjects
Biolayer interferometry, Heparin, Short Communication, Dialysis-related amyloidosis, β2-microglobulin
Abstract

Dialysis-related amyloidosis (DRA) is characterized by accumulation of amyloid β2- microglobulin (β2m) in the interstitial matrix. Matrix substances such as heparin have reportedly been strongly implicated in the pathogenesis of dialysis-related amyloidosis. In clinical setting of hemodialysis, two types of heparin, i.e., high and low molecular heparin (H.M.H. and L.M.H.) have been routinely used. Still commonly used is H.M.H., followed by L.M.H. preparations with distinct advantages. Here, we studied that the interaction of native and two amyloidogenic β2m variants: ΔN6β2m and D76N β2m with H.M.H. and L.M.H. We also investigated whether heparin could induce β2m to have an amyloidogenic conformation. Biolayer interferometry revealed that ΔN6β2m had a strong reaction and D76N β2m had a moderate reaction with H.M.H.. Furthermore,H.M.H. induced the C-terminal unfolding in a native β2m. By contrast, L.M.H. showed no reaction even with ΔN6β2m. This study showed firstly a direct binding of β2m with H.M.H.. H.M.H. would provoked a C-terminal unfolding of β2m, which indicated production of an amyloidogenic intermediate, i.e., β2m92-99. In addition, our findings also suggest that L.M.H. may provide beneficial effects against the development of the DRA.

Published
2016

38. Crucial role of RAGE in inappropriate increase of smooth muscle cells from patients with pulmonary arterial hypertension

Author

Nakamura, Kazufumi, primary, Sakaguchi, Masakiyo, additional, Matsubara, Hiromi, additional, Akagi, Satoshi, additional, Sarashina, Toshihiro, additional, Ejiri, Kentaro, additional, Akazawa, Kaoru, additional, Kondo, Megumi, additional, Nakagawa, Koji, additional, Yoshida, Masashi, additional, Miyoshi, Toru, additional, Ogo, Takeshi, additional, Oto, Takahiro, additional, Toyooka, Shinichi, additional, Higashimoto, Yuichiro, additional, Fukami, Kei, additional, and Ito, Hiroshi, additional

Published
2018
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39. RAGE-aptamer attenuates deoxycorticosterone acetate/salt-induced renal injury in mice

Author

Taguchi, Kensei, primary, Yamagishi, Sho-ichi, additional, Yokoro, Miyuki, additional, Ito, Sakuya, additional, Kodama, Goh, additional, Kaida, Yusuke, additional, Nakayama, Yosuke, additional, Ando, Ryotaro, additional, Yamada-Obara, Nana, additional, Asanuma, Katsuhiko, additional, Matsui, Takanori, additional, Higashimoto, Yuichiro, additional, Brooks, Craig R., additional, Ueda, Seiji, additional, Okuda, Seiya, additional, and Fukami, Kei, additional

Published
2018
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41. The Reactions of Heme- And Verdoheme-Heme Oxygenase-1 Complexes With FMN-depleted NADPH-cytochrome P450 Reductase : Electrons Required for Verdoheme Oxidation Can Be Transferred Through a Pathway Not Involving FMN

Author

Department of Medical Biochemistry, Kurume University School of Medicine, Department of Bioscience and Bioinformatics, Kyushu Institute of Technology, Department of Biochemistry and Cell Biology, Rice University, Higashimoto, Yuichiro, Sato, Hideaki, Sakamoto, Hiroshi, Takahashi, Kenichi, Palmer, Graham, Noguchi, Masato, Department of Medical Biochemistry, Kurume University School of Medicine, Department of Bioscience and Bioinformatics, Kyushu Institute of Technology, Department of Biochemistry and Cell Biology, Rice University, Higashimoto, Yuichiro, Sato, Hideaki, Sakamoto, Hiroshi, Takahashi, Kenichi, Palmer, Graham, and Noguchi, Masato

Abstract

type:Journal Article, Electrons utilized in the heme oxygenase (HO) reaction are provided by NADPH-cytochrome P450 reductase (CPR). To investigate the electron transfer pathway from CPR to HO, we examined the reactions of heme and verdoheme, the second intermediate in the heme degradation, complexed with rat HO-1 (rHO-1) using a rat FMN-depleted CPR; the FMN-depleted CPR was prepared by dialyzing the CPR mutant, Y140A/Y178A, against 2 M KBr. Degradation of heme in complex with rHO-1 did not occur with FMN-depleted CPR, notwithstanding that the FMN-depleted CPR was able to associate with the heme-rHO-1 complex with a binding affinity comparable with that of the wild-type CPR. Thus, the first electron to reduce the ferric iron of heme complexed with rHO-1 must be transferred from FMN. In contrast, verdoheme was converted to the ferric biliverdin-iron chelate with FMN-depleted CPR, and this conversion was inhibited by ferricyanide, indicating that electrons are certainly required for conversion of verdoheme to a ferric biliverdin-iron chelate and that they can be supplied from the FMN-depleted CPR through a pathway not involving FMN, probably via FAD. This conclusion was supported by the observation that verdoheme dimethyl esters were accumulated in the reaction of the ferriprotoporphyrin IX dimethyl ester-rHO-1 complex with the wild-type CPR. Ferric biliverdin-iron chelate, generated with the FMN-depleted CPR, was converted to biliverdin by the addition of the wild-type CPR or desferrioxamine. Thus, the final electron for reducing ferric biliverdin-iron chelate to release ferrous iron and biliverdin is apparently provided by the FMN of CPR., source:http://www.jbc.org/content/281/42/31659.long

Published
2017

42. Involvement of metals in enzymatic and nonenzymatic decomposition of C-terminal [alpha]-hydroxyglycine to amide: an implication for the catalytic role of enzyme-bound zinc in the peptidylamidoglycolate lyase reaction

Author

Takahashi, Kenichi, Harada, Saori, Higashimoto, Yuichiro, Shimokawa, Chizu, Sato, Hideaki, Sugishima, Masakazu, Kaida, Yasuhiko, and Noguchi, Masato

Subjects
Amides -- Chemical properties, Glycine -- Chemical properties, Metal catalysts -- Chemical properties, Transition metals -- Chemical properties, Biological sciences, Chemistry
Abstract

The significance of various transition metals in the enzymatic and nonenzymatic decomposition of C-terminal [alpha]-hydroxyglycine to amide is discussed. An increase in the pH of the reaction is shown to lead to a significant increase in the rate constant of metal catalysis, hence making the metal act as a general base.

Published
2009

43. Unfolding, aggregation and amyloid formation by tetramerization domain from mutant p53 associated with lung cancer

Author

Higashimoto, Yuichiro, Durell, Stewart R., Asanomi, Yuya, Anderson, Carl W., Takakusagi, Satoru, Appella, Ettore, Lewis, Marc S., Sakaguchi, Kazuyasu, and Uosaki, Kohei

Subjects
Peptides -- Chemical properties, Peptides -- Properties, Tumor suppressor genes -- Structure, Biological sciences, Chemistry
Abstract

A study to analyze the biochemical and biophysical properties of peptides corresponding to amino acids of wild-type human p53 that includes the tetramerization domain, and that of a cancer-derived mutant with valine substituted for glycine was conducted. The results suggest a new potential mechanism by which mutations that compromise tetramer formation inactivates p53 as a tumor suppressor.

Published
2006

50. Binding specificity of multiprotein signaling complexes is determined by both cooperative interactions and affinity preferences

Author

Houtman, Jon C.D., Higashimoto, Yuichiro, Dimasi, Nazzareno, Sangwoo Cho, Yamaguchi, Hiroshi, Bowden, Brent, Regan, Carole, Malchiodi, Emilio L., Mariuzza, Roy, Schuck, Peter, Appella, Ettore, and Samelson, Lawrence E.

Subjects
Enzymes -- Analysis, Tyrosine -- Analysis, Proteins -- Research, Proteins -- Properties, Biological sciences, Chemistry
Abstract

The multiple biochemical and biophysical methods are used to examine the binding properties of several SH2 and SH3 domain-containing signaling proteins as they interact with the adapter protein linker for activation of T-cells (LAT) to form multiprotein complexes. The binding specificity of these proteins for various LAT tyrosines appear to be constrained both by the affinity of binding and by cooperation protein-protein interactions.

Published
2004

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