Junji Yodoi - Academia.edu (original) (raw)
Papers by Junji Yodoi
Summary It is important throughout the life of animals to regulate the oxygen concentration and t... more Summary It is important throughout the life of animals to regulate the oxygen concentration and to scavenge oxygen radicals. Reactive oxygen species (ROS) are generated as by-products in the respiratory system and are increased under inflammatory conditions. Oxidative stress is induced by ROS production which exceeds the cell's ability to detoxify ROS and is involved in many diseases, such as heart failure, Alzheimer's disease, Parkinson's disease and cancer. Among the key antioxidant enzymes, thioredoxin and glutaredoxin play important roles in cell defense against oxidative stress and the maintenance of redox homeostasis. Thioredoxin is a small redox active protein distributed ubiquitously in various mammalian tissues and cells and acts not only as an antioxidant but also an anti-inflammatory and an antiapoptotic protein. Here we discuss the roles of thioredoxin on oxygen stress and redox regulation.
Summary It is important throughout the life of animals to regulate the oxygen concentration and t... more Summary It is important throughout the life of animals to regulate the oxygen concentration and to scavenge oxygen radicals. Reactive oxygen species (ROS) are generated as by-products in the respiratory system and are increased under inflammatory conditions. Oxidative stress is induced by ROS production which exceeds the cell's ability to detoxify ROS and is involved in many diseases, such as heart failure, Alzheimer's disease, Parkinson's disease and cancer. Among the key antioxidant enzymes, thioredoxin and glutaredoxin play important roles in cell defense against oxidative stress and the maintenance of redox homeostasis. Thioredoxin is a small redox active protein distributed ubiquitously in various mammalian tissues and cells and acts not only as an antioxidant but also an anti-inflammatory and an antiapoptotic protein. Here we discuss the roles of thioredoxin on oxygen stress and redox regulation.
The EMBO Journal, Apr 1, 1999
Hypoxia-inducible factor 1 α (HIF1α) and its related factor, HLF, activate expression of a group ... more Hypoxia-inducible factor 1 α (HIF1α) and its related factor, HLF, activate expression of a group of genes such as erythropoietin in response to low oxygen. Transfection analysis using fusion genes of GAL4DBD with various fragments of the two factors delineated two transcription activation domains which are inducible in response to hypoxia and are localized in the C-terminal half. Their sequences are conserved between HLF and HIF1α. One is designated NAD (N-terminal activation domain), while the other is CAD (C-terminal activation domain). Immunoblot analysis revealed that NADs, which were rarely detectable at normoxia, became stabilized and accumulated at hypoxia, whereas CADs were constitutively expressed. In the mammalian two-hybrid system, CAD and NAD baits enhanced the luciferase expression from a reporter gene by co-transfection with CREB-binding protein (CBP) prey, whereas CAD, but not NAD, enhanced β-galactosidase expression in yeast by CBP co-expression, suggesting that NAD and CAD interact with CBP/p300 by a different mechanism. Co-transfection experiments revealed that expression of Ref-1 and thioredoxin further enhanced the luciferase activity expressed by CAD, but not by NAD. Amino acid replacement in the sequences of CADs revealed a specific cysteine to be essential for their hypoxiainducible interaction with CBP. Nuclear translocation of thioredoxin from cytoplasm was observed upon reducing O 2 concentrations.
Oxidative stress and disease, Nov 29, 2005
Drug News & Perspectives, 2002
Thioredoxin (Trx) is a small multifunctional protein with a redox active dithiol/disulfide in the... more Thioredoxin (Trx) is a small multifunctional protein with a redox active dithiol/disulfide in the active-site sequence Cys-Gly-Pro-Cys. Trx functions as a key molecule in the maintenance of cellular redox balance. In addition to the cytoprotective action against oxidative stresses, Trx is involved in various cellular processes including gene expression, signal transduction, proliferation and apoptosis. Recently, various proteins sharing Trx-like active-site sequences have been found and classified as part of the Trx superfamily. Trx and these Trx-related molecules constitute a cellular redox regulation system, and further studies to clarify their biological functions will provide new therapeutic strategies for the disorders caused or complicated by oxidative stresses. (c) 2002 Prous Science. All rights reserved.
Biochemical and Biophysical Research Communications, Sep 1, 2005
Immunology Letters, Apr 3, 2003
The pathogenesis of bronchial asthma is chronic airway inflammation caused by immune cells such a... more The pathogenesis of bronchial asthma is chronic airway inflammation caused by immune cells such as T lymphocytes and eosinophils. Eosinophils release cytotoxic products including reactive oxygen species at the site of inflammation, leading to epithelial damage. Human thioredoxin (TRX), a redox-regulating protein with antioxidant activity, is induced and secreted from cells by oxidative stress. This study was undertaken to investigate the clinical significance of TRX in the pathogenesis of asthma. We collected blood samples from 48 patients with bronchial asthma with or without attack, and measured serum ECP and pulmonary function as well as serum TRX. The serum TRX levels in patients with asthma were significantly increased in patients with mild (34.63 [28.40-42.73] ng/ml, medians with 25 and 75% interquartiles, P=0.0064) and moderate (38.83 [35.14-50.80] ng/ml, P=0.0017) asthma attacks compared with those during the asymptomatic period. The serum TRX levels were inversely correlated with FEV(1.0)% (r=-0.44, P=0.039) and %PEF (r=-0.49, P=0.020) during attack. There was a significant correlation between the serum TRX and the serum eosinophil cationic protein (rs=0.32, P=0.016). These findings suggest that serum TRX is related to the state of asthma exacerbation and allergic inflammation.
Journal of Immunology, Oct 1, 1980
T lymphocytes in the mesenteric lymph nodes of rats infected with Nippostrongylus brasiliensis sp... more T lymphocytes in the mesenteric lymph nodes of rats infected with Nippostrongylus brasiliensis spontaneously released a soluble factor that selectively potentiated the IgE-forming cell response of antigen-primed cells to homologous antigen. The factor could enhance the IgE response of DNP-OA-primed cells to DNP-HSA and T cell-replacing factor. In contrast, the treatment of OA-primed T cells with the factor failed to enhance either the IgE or IgG response of the mixture of DNP-KLH primed cells and OA-primed T cells to DNP-OA. The results collectively suggested that the target cells of the IgE-potentiating factor are B cells. Indeed, IgE potentiating factor was absorbed by B cells rather than T cells or thymocytes. Evidence was obtained that IgE-potentiating factor could be absorbed by IgE-bearing B cells or IgE-coupled Sepharose, indicating that the factor had affinity for IgE. It appeared that the potentiating factor bound to IgE-bearing B cells and selectively enhanced the differentiation of IgE-B cells to IgE-forming cells. It was also found that the major source of the factor was Fc epsilon R-bearing T cells.
Antioxidants & Redox Signaling, Sep 1, 2006
Oxidative stresses are largely mediated by intracellular protein oxidations by reactive oxygen sp... more Oxidative stresses are largely mediated by intracellular protein oxidations by reactive oxygen species (ROS). Host cells are equipped with antioxidants that scavenge ROS. The cellular reduction/oxidation (redox) balance is maintained by ROS and antioxidants. Accumulating evidence suggests that the redox balance plays an important role in cellular signaling through the redox modification of cysteine residues in various important components of the signal transduction pathway. Thioredoxin (TRX) is a small protein playing important roles in cellular responses, including cell growth, cell cycle, gene expression, and apoptosis, to maintain the redox circumstance. Moreover, many recent papers have shown that the redox regulation by TRX is deeply involved in the pathogenesis of various oxidative stress-associated disorders. This review focuses on TRX and its related molecules, and discusses the role of TRX-dependent redox regulation in oxidative stress-induced signal transduction.
International Archives of Allergy and Immunology, 2011
Pathophysiology, Jun 1, 1998
Iubmb Life, Nov 1, 2006
Is There An Answer? is intended to serve as a forum in which readers to IUBMB Life may pose quest... more Is There An Answer? is intended to serve as a forum in which readers to IUBMB Life may pose questions of the type that intrigue biochemists but for which there may be no obvious answer or one may be available but not widely known or easily accessible. Readers are invited to e-mail
Biochemical and Biophysical Research Communications, Aug 1, 2007
The development and treatment of asthma remains a subject of considerable interest in the medical... more The development and treatment of asthma remains a subject of considerable interest in the medical community. Previous studies implicate an important role of cytokines in the pathology of asthma. In this current study, we examined whether redox-active protein thioredoxin 1 (TRX1) could prevent airway remodeling in an ovalbumin (OVA)-driven mouse chronic antigen exposure asthma model. Balb/c mice were sensitized and then challenged nine times with OVA (days 19-45). In this protocol, airway remodeling was established by day 34. Administration of recombinant human TRX1 during antigen challenge (days 18-32) significantly inhibited airway remodeling, eosinophilic pulmonary inflammation, airway hyperresponsiveness and resulted in decreased lung expression of eotaxin, macrophage inflammatory protein-1a and IL-13. Airway remodeling and eosinophilic pulmonary inflammation was also prevented in chronic OVA-exposed Balb/c human TRX1 transgenic mice. Importantly, TRX1-administration, after the establishment of airway remodeling (days 35-45), resulted in improved airway pathology. Our results suggest TRX1 prevents the development of airway remodeling, and also improves established airway remodeling by inhibiting production of chemokines and Th2 cytokines in the lungs.
Immunology Today, Jul 1, 1983
The IgE response is regulated by antigen-speck helper and suppressor T cells. Here Kimishige Ishi... more The IgE response is regulated by antigen-speck helper and suppressor T cells. Here Kimishige Ishizaka and his colleagues discuss recent work which indicates that soluble IgE-binding T-cell factors provide an additional, isotypespecific level of control on the antibody response.
Journal of Immunology, Jul 1, 1980
T lymphocytes in the mesenteric lymph nodes of rats infected with Nippostrongylus brasiliensis sp... more T lymphocytes in the mesenteric lymph nodes of rats infected with Nippostrongylus brasiliensis spontaneously released a soluble factor that selectively potentiated the IgE-forming cell response of antigen-primed cells to homologous antigen. The factor could enhance the IgE response of DNP-OA-primed cells to DNP-HSA and T cell-replacing factor. In contrast, the treatment of OA-primed T cells with the factor failed to enhance either the IgE or IgG response of the mixture of DNP-KLH primed cells and OA-primed T cells to DNP-OA. The results collectively suggested that the target cells of the IgE-potentiating factor are B cells. Indeed, IgE potentiating factor was absorbed by B cells rather than T cells or thymocytes. Evidence was obtained that IgE-potentiating factor could be absorbed by IgE-bearing B cells or IgE-coupled Sepharose, indicating that the factor had affinity for IgE. It appeared that the potentiating factor bound to IgE-bearing B cells and selectively enhanced the differentiation of IgE-B cells to IgE-forming cells. It was also found that the major source of the factor was Fc epsilon R-bearing T cells.
Clinical Reviews in Allergy, Jun 1, 1989
Conclusion The importance of FcεR2/LgE-BF system on the IgE regulation has been clarified in bot... more Conclusion The importance of FcεR2/LgE-BF system on the IgE regulation has been clarified in both human as well as rodents. Recent cloning of human low affinity FcεR (FcεR2) will help us to clarify the dynamic regulatory mechanism of IgE regulation. The unique lectin-like molecular property of human FcεR2 and its variable expression on hematopietic cell lineages including T, B lymphocytes, monocytes, and eosinophils may indicate the multiple functions of this receptor system. In the context of the IgE regulation by humanT cells, an interesting question is whether all the IgE-BFs from T cells (59, 60) are the products of this FcεR2 gene or not. The possible regulatory effects of the natural ligand of FcεR2, IgE, lymphokines including various interleukins, γIFN, SFA (4, 6), and Inducers of IgE-BF on the expression and processing of FcεR2 gene products are to be clarified.
Journal of Toxicological Sciences, Oct 17, 2001
Oxidative stress and disease, Sep 12, 2003
CRC Press eBooks, Jul 20, 2001
Summary It is important throughout the life of animals to regulate the oxygen concentration and t... more Summary It is important throughout the life of animals to regulate the oxygen concentration and to scavenge oxygen radicals. Reactive oxygen species (ROS) are generated as by-products in the respiratory system and are increased under inflammatory conditions. Oxidative stress is induced by ROS production which exceeds the cell's ability to detoxify ROS and is involved in many diseases, such as heart failure, Alzheimer's disease, Parkinson's disease and cancer. Among the key antioxidant enzymes, thioredoxin and glutaredoxin play important roles in cell defense against oxidative stress and the maintenance of redox homeostasis. Thioredoxin is a small redox active protein distributed ubiquitously in various mammalian tissues and cells and acts not only as an antioxidant but also an anti-inflammatory and an antiapoptotic protein. Here we discuss the roles of thioredoxin on oxygen stress and redox regulation.
Summary It is important throughout the life of animals to regulate the oxygen concentration and t... more Summary It is important throughout the life of animals to regulate the oxygen concentration and to scavenge oxygen radicals. Reactive oxygen species (ROS) are generated as by-products in the respiratory system and are increased under inflammatory conditions. Oxidative stress is induced by ROS production which exceeds the cell's ability to detoxify ROS and is involved in many diseases, such as heart failure, Alzheimer's disease, Parkinson's disease and cancer. Among the key antioxidant enzymes, thioredoxin and glutaredoxin play important roles in cell defense against oxidative stress and the maintenance of redox homeostasis. Thioredoxin is a small redox active protein distributed ubiquitously in various mammalian tissues and cells and acts not only as an antioxidant but also an anti-inflammatory and an antiapoptotic protein. Here we discuss the roles of thioredoxin on oxygen stress and redox regulation.
The EMBO Journal, Apr 1, 1999
Hypoxia-inducible factor 1 α (HIF1α) and its related factor, HLF, activate expression of a group ... more Hypoxia-inducible factor 1 α (HIF1α) and its related factor, HLF, activate expression of a group of genes such as erythropoietin in response to low oxygen. Transfection analysis using fusion genes of GAL4DBD with various fragments of the two factors delineated two transcription activation domains which are inducible in response to hypoxia and are localized in the C-terminal half. Their sequences are conserved between HLF and HIF1α. One is designated NAD (N-terminal activation domain), while the other is CAD (C-terminal activation domain). Immunoblot analysis revealed that NADs, which were rarely detectable at normoxia, became stabilized and accumulated at hypoxia, whereas CADs were constitutively expressed. In the mammalian two-hybrid system, CAD and NAD baits enhanced the luciferase expression from a reporter gene by co-transfection with CREB-binding protein (CBP) prey, whereas CAD, but not NAD, enhanced β-galactosidase expression in yeast by CBP co-expression, suggesting that NAD and CAD interact with CBP/p300 by a different mechanism. Co-transfection experiments revealed that expression of Ref-1 and thioredoxin further enhanced the luciferase activity expressed by CAD, but not by NAD. Amino acid replacement in the sequences of CADs revealed a specific cysteine to be essential for their hypoxiainducible interaction with CBP. Nuclear translocation of thioredoxin from cytoplasm was observed upon reducing O 2 concentrations.
Oxidative stress and disease, Nov 29, 2005
Drug News & Perspectives, 2002
Thioredoxin (Trx) is a small multifunctional protein with a redox active dithiol/disulfide in the... more Thioredoxin (Trx) is a small multifunctional protein with a redox active dithiol/disulfide in the active-site sequence Cys-Gly-Pro-Cys. Trx functions as a key molecule in the maintenance of cellular redox balance. In addition to the cytoprotective action against oxidative stresses, Trx is involved in various cellular processes including gene expression, signal transduction, proliferation and apoptosis. Recently, various proteins sharing Trx-like active-site sequences have been found and classified as part of the Trx superfamily. Trx and these Trx-related molecules constitute a cellular redox regulation system, and further studies to clarify their biological functions will provide new therapeutic strategies for the disorders caused or complicated by oxidative stresses. (c) 2002 Prous Science. All rights reserved.
Biochemical and Biophysical Research Communications, Sep 1, 2005
Immunology Letters, Apr 3, 2003
The pathogenesis of bronchial asthma is chronic airway inflammation caused by immune cells such a... more The pathogenesis of bronchial asthma is chronic airway inflammation caused by immune cells such as T lymphocytes and eosinophils. Eosinophils release cytotoxic products including reactive oxygen species at the site of inflammation, leading to epithelial damage. Human thioredoxin (TRX), a redox-regulating protein with antioxidant activity, is induced and secreted from cells by oxidative stress. This study was undertaken to investigate the clinical significance of TRX in the pathogenesis of asthma. We collected blood samples from 48 patients with bronchial asthma with or without attack, and measured serum ECP and pulmonary function as well as serum TRX. The serum TRX levels in patients with asthma were significantly increased in patients with mild (34.63 [28.40-42.73] ng/ml, medians with 25 and 75% interquartiles, P=0.0064) and moderate (38.83 [35.14-50.80] ng/ml, P=0.0017) asthma attacks compared with those during the asymptomatic period. The serum TRX levels were inversely correlated with FEV(1.0)% (r=-0.44, P=0.039) and %PEF (r=-0.49, P=0.020) during attack. There was a significant correlation between the serum TRX and the serum eosinophil cationic protein (rs=0.32, P=0.016). These findings suggest that serum TRX is related to the state of asthma exacerbation and allergic inflammation.
Journal of Immunology, Oct 1, 1980
T lymphocytes in the mesenteric lymph nodes of rats infected with Nippostrongylus brasiliensis sp... more T lymphocytes in the mesenteric lymph nodes of rats infected with Nippostrongylus brasiliensis spontaneously released a soluble factor that selectively potentiated the IgE-forming cell response of antigen-primed cells to homologous antigen. The factor could enhance the IgE response of DNP-OA-primed cells to DNP-HSA and T cell-replacing factor. In contrast, the treatment of OA-primed T cells with the factor failed to enhance either the IgE or IgG response of the mixture of DNP-KLH primed cells and OA-primed T cells to DNP-OA. The results collectively suggested that the target cells of the IgE-potentiating factor are B cells. Indeed, IgE potentiating factor was absorbed by B cells rather than T cells or thymocytes. Evidence was obtained that IgE-potentiating factor could be absorbed by IgE-bearing B cells or IgE-coupled Sepharose, indicating that the factor had affinity for IgE. It appeared that the potentiating factor bound to IgE-bearing B cells and selectively enhanced the differentiation of IgE-B cells to IgE-forming cells. It was also found that the major source of the factor was Fc epsilon R-bearing T cells.
Antioxidants & Redox Signaling, Sep 1, 2006
Oxidative stresses are largely mediated by intracellular protein oxidations by reactive oxygen sp... more Oxidative stresses are largely mediated by intracellular protein oxidations by reactive oxygen species (ROS). Host cells are equipped with antioxidants that scavenge ROS. The cellular reduction/oxidation (redox) balance is maintained by ROS and antioxidants. Accumulating evidence suggests that the redox balance plays an important role in cellular signaling through the redox modification of cysteine residues in various important components of the signal transduction pathway. Thioredoxin (TRX) is a small protein playing important roles in cellular responses, including cell growth, cell cycle, gene expression, and apoptosis, to maintain the redox circumstance. Moreover, many recent papers have shown that the redox regulation by TRX is deeply involved in the pathogenesis of various oxidative stress-associated disorders. This review focuses on TRX and its related molecules, and discusses the role of TRX-dependent redox regulation in oxidative stress-induced signal transduction.
International Archives of Allergy and Immunology, 2011
Pathophysiology, Jun 1, 1998
Iubmb Life, Nov 1, 2006
Is There An Answer? is intended to serve as a forum in which readers to IUBMB Life may pose quest... more Is There An Answer? is intended to serve as a forum in which readers to IUBMB Life may pose questions of the type that intrigue biochemists but for which there may be no obvious answer or one may be available but not widely known or easily accessible. Readers are invited to e-mail
Biochemical and Biophysical Research Communications, Aug 1, 2007
The development and treatment of asthma remains a subject of considerable interest in the medical... more The development and treatment of asthma remains a subject of considerable interest in the medical community. Previous studies implicate an important role of cytokines in the pathology of asthma. In this current study, we examined whether redox-active protein thioredoxin 1 (TRX1) could prevent airway remodeling in an ovalbumin (OVA)-driven mouse chronic antigen exposure asthma model. Balb/c mice were sensitized and then challenged nine times with OVA (days 19-45). In this protocol, airway remodeling was established by day 34. Administration of recombinant human TRX1 during antigen challenge (days 18-32) significantly inhibited airway remodeling, eosinophilic pulmonary inflammation, airway hyperresponsiveness and resulted in decreased lung expression of eotaxin, macrophage inflammatory protein-1a and IL-13. Airway remodeling and eosinophilic pulmonary inflammation was also prevented in chronic OVA-exposed Balb/c human TRX1 transgenic mice. Importantly, TRX1-administration, after the establishment of airway remodeling (days 35-45), resulted in improved airway pathology. Our results suggest TRX1 prevents the development of airway remodeling, and also improves established airway remodeling by inhibiting production of chemokines and Th2 cytokines in the lungs.
Immunology Today, Jul 1, 1983
The IgE response is regulated by antigen-speck helper and suppressor T cells. Here Kimishige Ishi... more The IgE response is regulated by antigen-speck helper and suppressor T cells. Here Kimishige Ishizaka and his colleagues discuss recent work which indicates that soluble IgE-binding T-cell factors provide an additional, isotypespecific level of control on the antibody response.
Journal of Immunology, Jul 1, 1980
T lymphocytes in the mesenteric lymph nodes of rats infected with Nippostrongylus brasiliensis sp... more T lymphocytes in the mesenteric lymph nodes of rats infected with Nippostrongylus brasiliensis spontaneously released a soluble factor that selectively potentiated the IgE-forming cell response of antigen-primed cells to homologous antigen. The factor could enhance the IgE response of DNP-OA-primed cells to DNP-HSA and T cell-replacing factor. In contrast, the treatment of OA-primed T cells with the factor failed to enhance either the IgE or IgG response of the mixture of DNP-KLH primed cells and OA-primed T cells to DNP-OA. The results collectively suggested that the target cells of the IgE-potentiating factor are B cells. Indeed, IgE potentiating factor was absorbed by B cells rather than T cells or thymocytes. Evidence was obtained that IgE-potentiating factor could be absorbed by IgE-bearing B cells or IgE-coupled Sepharose, indicating that the factor had affinity for IgE. It appeared that the potentiating factor bound to IgE-bearing B cells and selectively enhanced the differentiation of IgE-B cells to IgE-forming cells. It was also found that the major source of the factor was Fc epsilon R-bearing T cells.
Clinical Reviews in Allergy, Jun 1, 1989
Conclusion The importance of FcεR2/LgE-BF system on the IgE regulation has been clarified in bot... more Conclusion The importance of FcεR2/LgE-BF system on the IgE regulation has been clarified in both human as well as rodents. Recent cloning of human low affinity FcεR (FcεR2) will help us to clarify the dynamic regulatory mechanism of IgE regulation. The unique lectin-like molecular property of human FcεR2 and its variable expression on hematopietic cell lineages including T, B lymphocytes, monocytes, and eosinophils may indicate the multiple functions of this receptor system. In the context of the IgE regulation by humanT cells, an interesting question is whether all the IgE-BFs from T cells (59, 60) are the products of this FcεR2 gene or not. The possible regulatory effects of the natural ligand of FcεR2, IgE, lymphokines including various interleukins, γIFN, SFA (4, 6), and Inducers of IgE-BF on the expression and processing of FcεR2 gene products are to be clarified.
Journal of Toxicological Sciences, Oct 17, 2001
Oxidative stress and disease, Sep 12, 2003
CRC Press eBooks, Jul 20, 2001