Faculty Profiles - TOYOKUNI Shinya

Papers - TOYOKUNI Shinya

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Oxidative stress in pancreatic β-cells of GK rat, a model of non-obese NIDDM International journal

Ihara, Y, Yamada, Y, Uchida, K, Toyokuni, S, Seino, Y

DIABETES Vol. 47 page： A263 - A263 1998.5

Significant deposition of 4-hydroxy-2-nonenal-modified-protein adducts in human alcoholic liver disease; Positive correlation with parenchymal iron. International journal

Ohhira, M; Ohtake, T; Matsumoto, A; Saito, H; Kawashima, T; Ikuta, K; Tanaka, K; Fujimoto, Y; Ono, M; Toyokuni, S; Kohgo, Y

GASTROENTEROLOGY Vol. 114 ( 4 ) page： A1315 - A1315 1998.4

The role of oxidative DNA damage in human arsenic carcinogenesis: Detection of 8-OHdG in arsenic related Bowen's disease.

Matsui, M; Nishigori, C; Toyokuni, S; Takada, J; Akaboshi, M; Ochi, H; Ishikawa, M; Imamura, S

JOURNAL OF INVESTIGATIVE DERMATOLOGY Vol. 110 ( 4 ) page： 526 - 526 1998.4

The role of oxidative DNA damage in human arsenic carcinogenesis: Detection of 8-OHdG in arsenic related Bowen's disease. International journal

Matsui, M, Nishigori, C, Toyokuni, S, Takada, J, Akaboshi, M, Ochi, H, Ishikawa, M, Imamura, S

JOURNAL OF INVESTIGATIVE DERMATOLOGY Vol. 110 ( 4 ) page： 526 - 526 1998.4

Enhanced hepatic lipid peroxidation in chronic hepatitis C Reviewed International journal

Kageyama F., Kobayashi Y., Koide S., Murohisa G., Otake M., Shimizu E., Sasada Y., Suzuki F., Kawasaki T., Nakamura H., Toyokuni S., Uchida K.

Japanese Pharmacology and Therapeutics Vol. 26 ( SUPPL. 2 ) page： 149 - 152 1998.4

Enhanced hepatic lipid peroxidation in chronic hepatitis C Reviewed International journal

Kageyama F, Kobayashi Y, Koide S, Murohisa G, Otake M, Shimizu E, Sasada Y, Suzuki F, Kawasaki T, Nakamura H, Toyokuni S, Uchida K

Japanese Pharmacology and Therapeutics Vol. 26 ( SUPPL. 2 ) page： 149 - 152 1998.4

Involvement of nitric oxide in survival of random pattern skin flap

Um SC, Suzuki S, Toyokuni S, Kim BM, Tanaka T, Hiai H, Nishimura Y

PLASTIC AND RECONSTRUCTIVE SURGERY Vol. 101 ( 3 ) page： 785 - 792 1998.3

Involvement of nitric oxide in survival of random pattern skin flap

UM SC

Plast Reconstr Surg Vol. 101 ( 3 ) page： 785 - 792 1998.3

Major targets of ROS-induced cancer in rats are p15/p16 oncosuppressor genes

Toyokuni, S; Tanaka, T; Iwasa, Y; Kondo, S; Hiai, H

FREE RADICAL BIOLOGY AND MEDICINE Vol. 25 page： S119 - S119 1998

A processed grain food AOB inhibits hepatic injury in endotoxemic rats

Minamiyama, Y; Takemura, S; Toyokuni, S; Tanimoto, Y; Sato, EF; Inoue, M

BIOLOGICAL OXIDANTS AND ANTIOXIDANTS: MOLECULAR MECHANISMS AND HEALTH EFFECTS page： 349 - 357 1998

A processed grain food inhibits hepatic injury in endotoxemic rats Reviewed

Minamiyama Y, Takemura S, Toyokuni S, Tanimoto Y, Sato EF, Inoue M

JOURNAL OF NUTRITIONAL SCIENCE AND VITAMINOLOGY Vol. 44 ( 4 ) page： 547 - 559 1998

Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Center for Academic Publications Japan

Although various antioxidants have been tested as therapeutics for endotoxemic subjects, the results of their efficacy are conflicting. Antioxidant biofactor (AOB) is a unique processed grain food that exhibits strong antioxidant activity (Minamiyama et al, J Nutr Sci Vitaminol, 40: 467-477, 1994). The present study was carried out to test the effect of AOB on hepatic injury in rats induced by lipopolysaccharide (LPS). Intravenous administration of LPS induced liver injury with a concomitant increase in hepatic generation of nitric oxide (NO) and 4-hydroxy-2nonenal (HNE) modified proteins in the control group. The administration of AOB significantly inhibited the LPS-induced hepatic injury and generation of HNE-modified proteins and increased the survival rate of endotoxemic rats without affecting NO generation and plasma levels of tumor necrosis factor-α (TNF-α) and interferon-γ (IFN-γ). AOB scavenged superoxide radicals without affecting NO production by LPS-stimulated macrophage cell line J 774.2 cells. AOB also inhibited lipid peroxidation induced by LPS in the cells. These results suggested that AOB might scavenge superoxide radicals and decrease toxic metabolites including HNE, thereby inhibiting liver injury in endotoxemic rats.

DOI： 10.3177/jnsv.44.547

Other Link： https://jlc.jst.go.jp/DN/JALC/00085275768?from=CiNii

Oxidative stress and cancer: The role of redox regulation

Toyokuni S

BIOTHERAPY Vol. 11 ( 2-3 ) page： 147 - 154 1998

A study of imprint smear cytology during surgery of mucinous cystic tumor of ovary. A special reference to borderline malignancy.:A special reference to borderline malignancy International journal

SHIMIZU Keiko, OGURA Seiko, MURATA Masayoshi, TAKAO Yumi, TOYOKUNI Shinya, SAKURAI Masami

The Journal of the Japanese Society of Clinical Cytology Vol. 37 ( 6 ) page： 583 - 590 1998

Language：Japanese Publishing type：Research paper (scientific journal) Publisher：The Japanese Society of Clinical Cytology

Objective: Preoperative diagnosis of ovarian tumors is often difficult. Additional squashed smear cytology during surgery was undertaken for the correct diagnosis of mucinous cystic tumors of the ovary. Study Design: We reviewed the cytological findings of imprint smear during surgery of 34 cases with mucinous cystic tumors of the ovary, especially borderline malignant cases, that we have experienced over an 8 year period (1990-1997). Additional squashed smears were applied in some recent cases and compared with the routine imprint smears. Results: Characteristic cytological findings of mucinous cystic tumors of borderline malignancy were relatively clear background, crowded clumps of cells, and papillary and ball-like architectures. In some cases, an additinal squashed smear technique was useful for the correctdiagnosis, because the structure of cell clusters became more apparent. Conclusion: It was possible to differentiate borderline cases from malignancies, but was difficult to differentiate borderline cases from benign cases by cytological examinations. The additional of the squashed smear technique was useful for correct cytological diagnosis.

DOI： 10.5795/jjscc.37.583

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Oxidative stress and cancer: The role of redox regulation Reviewed

S Toyokuni

BIOTHERAPY Vol. 11 ( 2-3 ) page： 147 - 154 1998

Immunohistochemical detection of 4-hydroxy-2-nonenal-modified-protein adducts in human alcoholic liver diseases

Ohhira M., Ohtake T., Matsumoto A., Saito H., Ikuta K., Fujimoto Y., Ono M., Toyokuni S., Kohgo Y.

Alcoholism: Clinical and Experimental Research Vol. 22 ( 3 SUPPL. 1 ) 1998

Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Alcoholism: Clinical and Experimental Research

4-Hydroxy-2-nonenal (HNE) is one of the major components of lipid peroxidation product and has been shown to react with proteins to form HNE-protein adducts. HNE-protein adducts are relatively stable and can be used as a marker of radical-mediated cellular damage. We report herein the immunohistochemical analysis of HNE-protein adducts in human alcoholic liver diseases using a specific monoclonal antibody HNEJ-2. Cytoplasm of hepatocytes and bile duct epithelia was positively stained for HNE-protein adducts, and the nucleus was negligibly stained. The immunohistochemical intensity of hepatocytes was classified into three groups: strong, moderate, and faint staining. Strong staining was found in 43% of alcoholic liver diseases and in 4% of viral liver diseases. Hepatocytes of alcoholic liver diseases contained a higher amount of HNE-protein adducts than those of viral liver diseases, and the difference was statistically significant (p = 0.005; χ2 test). Semiquantitative analysis of the histological intensities of HNE-protein adducts and iron indicated a significant positive correlation (p = 0.084; Spearman's rank correlation). The localization of HNE-protein adducts and iron in hepatocytes appeared to be identical. These data suggested the correlation between HNE-protein adducts and iron. Our results indicate that HNE-protein adducts, a marker of oxidative stress-induced damage, are increased in human alcoholic liver damage, and that hepatic siderosis may act on the production of free radicals. Copyright © 1998 by The Research Society on Alcoholism.

DOI： 10.1111/acer.1998.22.s3_part1.145s

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A processed grain food AOB inhibits hepatic injury in endotoxemic rats Reviewed International journal

Minamiyama, Y, Takemura, S, Toyokuni, S, Tanimoto, Y, Sato, EF, Inoue, M

BIOLOGICAL OXIDANTS AND ANTIOXIDANTS: MOLECULAR MECHANISMS AND HEALTH EFFECTS page： 349 - 357 1998

New biomarker evidence of oxidative DNA damage in patients with non-insulin-dependent diabetes mellitus

Leinonen J., Lehtimäki T., Toyokuni S., Okada K., Tanaka T., Hiai H., Ochi H., Laippala P., Rantalaiho V., Wirta O., Pasternack A., Alho H.

FEBS Letters Vol. 417 ( 1 ) page： 150 - 152 1997.11

Language：Japanese Publishing type：Research paper (scientific journal) Publisher：FEBS Letters

Urinary 8-hydroxy-2'-deoxyguanosine (8-OHdG) has been reported to serve as a sensitive biomarker of oxidative DNA damage and also of oxidative stress. We have investigated oxidative DNA damage in patients with non-insulin-dependent diabetes mellitus (NIDDM) by urinary 8-OHdG assessments. We determined the total urinary excretion of and OHdG from 24 h urine samples of 81 NIDDM patients 9 years after the initial diagnosis and of 100 non-diabetic control subjects matched for age and gender. The total 24 h urinary excretion of 8-OHdG was markedly higher in NIDDM patients than in control subjects (68.2 ± 39.4 μg vs, 49.6 ± 37.7 μg, P= 0.001). High glycosylated hemoglobin was associated with a high level of urinary 8-OHdG. The increased excretion of urinary and OHdG is seen as indicating an increased systemic level of oxidative DNA damage in NIDDM patients.

DOI： 10.1016/S0014-5793(97)01273-8

Scopus

New biomarker evidence of oxidative DNA damage in patients with non-insulin-dependent diabetes mellitus

Leinonen J, Lehtimaki T, Toyokuni S, Okada K, Tanaka T, Hiai H, Ochi H, Laippala P, Rantalaiho V, Wirta O, Pasternack A, Alho H

FEBS LETTERS Vol. 417 ( 1 ) page： 150 - 152 1997.11

Protein modification by lipid peroxidation products: Formation of malondialdehyde-derived N epsilon-(2-propenal)lysine in proteins Reviewed International journal

Uchida K, Sakai K, Itakura K, Osawa T, Toyokuni S

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS Vol. 346 ( 1 ) page： 45 - 52 1997.10

Protein modification by lipid peroxidation products: Formation of malondialdehyde-derived N(ε)(2-propenal)lysine in proteins

Uchida K., Sakai K., Itakura K., Osawa T., Toyokuni S.

Archives of Biochemistry and Biophysics Vol. 346 ( 1 ) page： 45 - 52 1997.10

Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Archives of Biochemistry and Biophysics

Malondialdehyde (MDA), a naturally occurring dialdehyde produced in the membrane lipid peroxidation, is known to react with lysine residues of proteins, but the MDA-lysine adducts generated in the proteins have not been characterized adequately. In the present study, we provide evidence that the enaminal-type MDA-lysine adduct, N(ε)-(2-propenal)lysine, is formed in human low-density lipoprotein (LDL) upon reaction with MDA or Cu2+. We found that the incubation of N(α)acetyllysine with MDA generated N(α)-acetyl-N(ε)- (2-propenal)lysine as the predominant product. In addition, a polyclonal antiserum raised against the MDA-modified protein was found to contain antibody populations that could be purified by affinity gel prepared by covalent attachment of N(α)-acetyl-N(ε)-(2-propenal)lysine. It was concluded that the affinity-purified anti-N(ε)-(2-propenal) lysine antibody was highly specific to the enaminal derivative of both lysine residues and phosphatidylethanolamine, based on the observations that (i) MDA was the only aldehyde which generated immunoreactive materials in proteins; (ii) among structurally defined MDA-lysine adducts tested, the antibody recognized the enaminal adduct only; and (iii) immunoreactivity to N(2-propenal)serine was still significant but much weaker than its reactivity to N-(2- propenal)ethanol- amine. Furthermore, analysis of antibody recognition sites with a variety of N-(2-propenal)alkylamines revealed that the mono-specific antibody recognized the N-2-propenal-N-ethyl moiety [-(CH2)2-NH-CH=CH - CHO] of enaminal adducts. Determination by a competitive enzyme-linked immunosorbent assay demonstrated that N(ε)-(2-propenal)lysine accounted for 33.7 and 3.1% of the lysine residues that disappeared during in vitro incubation of LDL with MDA and Cu2+, respectively. These results suggest that N(ε)-(2-propenal)lysine represents a major form of MDA covalently attached to proteins.

DOI： 10.1006/abbi.1997.0266

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