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Reiko Inagi - One of the best experts on this subject based on the ideXlab platform.

  • the role of glyoxalase system in renal hypoxia
    Advances in Experimental Medicine and Biology, 2010
    Co-Authors: Reiko Inagi, Takanori Kumagai, Toshiro Fujita, Masaomi Nangaku
    Abstract:

    Methylglyoxal (MG), a highly reactive α-oxoaldehyde generated by oxidation of carbohydrate and glycolysis, binds to proteins and forms advanced glycation end products (AGE). MG and MG adducts have been implicated in oxidative stress-related diseases, therefore, MG detoxifying system such as the glyoxalase system (glyoxalase I) also contributes to progression of these diseases. Recent papers have emphasized the pathophysiological effects of MG and the glyoxalase system in acute Hypoxic Injury, which is associated with acute oxidative stress. We investigated the kinetics of MG level and glyoxalase I activity in renal acute Hypoxic Injury induced by ischemia-reperfusion (I/R). I/R induced tubulointerstitial Injury and the histological changes were associated with a significant decrease in renal glyoxalase I activity and an increase in MG level in the damaged tubular cells. Of note, rats over expressing human glyoxalase I showed amelioration of I/R-induced histological and functional damages and it was associated with a decrease in MG level in the lesion resulting in reduction of oxidative stress and tubular cell apoptosis. In conclusion, glyoxalase I has renoprotective effects in renal hypoxia such as I/R Injury via a reduction in cytotoxic MG level in tubular cells.

  • pathophysiological role of the glyoxalase system in renal Hypoxic Injury
    Annals of the New York Academy of Sciences, 2008
    Co-Authors: Takanori Kumagai, Masaomi Nangaku, Reiko Inagi
    Abstract:

    Methylglyoxal (MG), a reactive dicarbonyl compound mainly produced by metabolic pathways, such as glycolysis, binds to proteins or nucleic acids and forms advanced glycation end products. MG is efficiently metabolized by the glyoxalase system where MG is converted by glyoxalase I (GLO I) to S-D-lactoylglutathione. Although the glyoxalase system has been shown to play a pathological role in various diseases, including diabetic complications, its detailed pathophysiological function remains to be elucidated. We are interested in renal Hypoxic diseases, but very little information is available regarding the association between the glyoxalase system and renal Hypoxic diseases. Therefore, we investigated the biological role of GLO I in renal Hypoxic diseases by using the rat ischemia/reperfusion (I/R) Injury model. I/R induced the reduction of renal GLO I activity associated with morphological changes and renal dysfunction. Interestingly, the rats that overexpress human GLO I (GLO I Tg rats) showed amelioration of these manifestations in renal I/R (e.g., improvement of the tubulointerstitial Injury and renal function). Accumulation of renal MG adducts, carboxyethyllysine, induced by I/R also decreased in GLO I Tg rats compared to wild-type rats. These results demonstrate that GLO I has renoprotective effects in I/R Injury via reduction of protein modification by MG.

Martino Bolognesi - One of the best experts on this subject based on the ideXlab platform.

  • human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity
    Structure, 2003
    Co-Authors: Alessandra Pesce, Marcello Nardini, Thorsten Burmester, Sylvia Dewilde, Thomas Hankeln, Luc Moens, Paolo Ascenzi, Martino Bolognesi
    Abstract:

    Abstract Neuroglobin, mainly expressed in vertebrate brain and retina, is a recently identified member of the globin superfamily. Augmenting O 2 supply, neuroglobin promotes survival of neurons upon Hypoxic Injury, potentially limiting brain damage. In the absence of exogenous ligands, neuroglobin displays a hexacoordinated heme. O 2 and CO bind to the heme iron, displacing the endogenous HisE7 heme distal ligand. Hexacoordinated human neuroglobin displays a classical globin fold adapted to host the reversible bis-histidyl heme complex and an elongated protein matrix cavity, held to facilitate O 2 diffusion to the heme. The neuroglobin structure suggests that the classical globin fold is endowed with striking adaptability, indicating that hemoglobin and myoglobin are just two examples within a wide and functionally diversified protein homology superfamily.

  • human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity
    Structure, 2003
    Co-Authors: Alessandra Pesce, Marcello Nardini, Thorsten Burmester, Sylvia Dewilde, Thomas Hankeln, Luc Moens, Paolo Ascenzi, Martino Bolognesi
    Abstract:

    Abstract Neuroglobin, mainly expressed in vertebrate brain and retina, is a recently identified member of the globin superfamily. Augmenting O 2 supply, neuroglobin promotes survival of neurons upon Hypoxic Injury, potentially limiting brain damage. In the absence of exogenous ligands, neuroglobin displays a hexacoordinated heme. O 2 and CO bind to the heme iron, displacing the endogenous HisE7 heme distal ligand. Hexacoordinated human neuroglobin displays a classical globin fold adapted to host the reversible bis-histidyl heme complex and an elongated protein matrix cavity, held to facilitate O 2 diffusion to the heme. The neuroglobin structure suggests that the classical globin fold is endowed with striking adaptability, indicating that hemoglobin and myoglobin are just two examples within a wide and functionally diversified protein homology superfamily.

Masaomi Nangaku - One of the best experts on this subject based on the ideXlab platform.

  • the role of glyoxalase system in renal hypoxia
    Advances in Experimental Medicine and Biology, 2010
    Co-Authors: Reiko Inagi, Takanori Kumagai, Toshiro Fujita, Masaomi Nangaku
    Abstract:

    Methylglyoxal (MG), a highly reactive α-oxoaldehyde generated by oxidation of carbohydrate and glycolysis, binds to proteins and forms advanced glycation end products (AGE). MG and MG adducts have been implicated in oxidative stress-related diseases, therefore, MG detoxifying system such as the glyoxalase system (glyoxalase I) also contributes to progression of these diseases. Recent papers have emphasized the pathophysiological effects of MG and the glyoxalase system in acute Hypoxic Injury, which is associated with acute oxidative stress. We investigated the kinetics of MG level and glyoxalase I activity in renal acute Hypoxic Injury induced by ischemia-reperfusion (I/R). I/R induced tubulointerstitial Injury and the histological changes were associated with a significant decrease in renal glyoxalase I activity and an increase in MG level in the damaged tubular cells. Of note, rats over expressing human glyoxalase I showed amelioration of I/R-induced histological and functional damages and it was associated with a decrease in MG level in the lesion resulting in reduction of oxidative stress and tubular cell apoptosis. In conclusion, glyoxalase I has renoprotective effects in renal hypoxia such as I/R Injury via a reduction in cytotoxic MG level in tubular cells.

  • pathophysiological role of the glyoxalase system in renal Hypoxic Injury
    Annals of the New York Academy of Sciences, 2008
    Co-Authors: Takanori Kumagai, Masaomi Nangaku, Reiko Inagi
    Abstract:

    Methylglyoxal (MG), a reactive dicarbonyl compound mainly produced by metabolic pathways, such as glycolysis, binds to proteins or nucleic acids and forms advanced glycation end products. MG is efficiently metabolized by the glyoxalase system where MG is converted by glyoxalase I (GLO I) to S-D-lactoylglutathione. Although the glyoxalase system has been shown to play a pathological role in various diseases, including diabetic complications, its detailed pathophysiological function remains to be elucidated. We are interested in renal Hypoxic diseases, but very little information is available regarding the association between the glyoxalase system and renal Hypoxic diseases. Therefore, we investigated the biological role of GLO I in renal Hypoxic diseases by using the rat ischemia/reperfusion (I/R) Injury model. I/R induced the reduction of renal GLO I activity associated with morphological changes and renal dysfunction. Interestingly, the rats that overexpress human GLO I (GLO I Tg rats) showed amelioration of these manifestations in renal I/R (e.g., improvement of the tubulointerstitial Injury and renal function). Accumulation of renal MG adducts, carboxyethyllysine, induced by I/R also decreased in GLO I Tg rats compared to wild-type rats. These results demonstrate that GLO I has renoprotective effects in I/R Injury via reduction of protein modification by MG.

David W. Walker - One of the best experts on this subject based on the ideXlab platform.

  • Original Article Maternal Dietary Creatine Supplementation Does Not Alter the Capacity for Creatine Synthesis in the Newborn Spiny Mouse
    2016
    Co-Authors: Hayley Dickinson, Domenic A. Larosa, Stacey J. Ellery, Zoe J. Irel, Bree A. O’connell, Rod Snow, David W. Walker
    Abstract:

    We have previously reported that maternal creatine supplementation protects the neonate from Hypoxic Injury. Here, we investigated whether maternal creatine supplementation altered expression of the creatine synthesis enzymes (arginine:glycine amidinotransferase [AGAT], guanidinoaceteate methyltransferase [GAMT]) and the creatine transporter (solute carrier family 6 [neurotransmitter transporter, creatine] member 8: SLC6A8) in the term offspring. Pregnant spiny mice were fed a 5 % creatine monohydrate diet from midgestation (day 20) to term (39 days). Placentas and neonatal kidney, liver, heart, and brain collected at 24 hours of age underwent quantitative polymerase chain reaction and Western blot analysis. Maternal creatine had no effect on the expression of AGAT and GAMT in neonatal kidney and liver, but mRNA expression of AGAT in brain tissues was significantly decreased in both male and female neonates born to mothers who were fed the creatine diet. SLC6A8 expression was not affected by maternal dietary creatine loading in any tissues. Maternal dietary creatine supplementation from midgestation in the spiny mouse did not alter the capacity for creatine synthesis or transport

  • Maternal Dietary Creatine Supplementation Does Not Alter the Capacity for Creatine Synthesis in the Newborn Spiny Mouse
    Reproductive Sciences, 2013
    Co-Authors: Hayley Dickinson, Z. Ireland, Domenic A. Larosa, Bree Aimee O'connell, Stacey J. Ellery, Rodney J. Snow, David W. Walker
    Abstract:

    We have previously reported that maternal creatine supplementation protects the neonate from Hypoxic Injury. Here, we investigated whether maternal creatine supplementation altered expression of the creatine synthesis enzymes (arginine:glycine amidinotransferase [AGAT], guanidinoaceteate methyltransferase [GAMT]) and the creatine transporter (solute carrier family 6 [neurotransmitter transporter, creatine] member 8: SLC6A8) in the term offspring. Pregnant spiny mice were fed a 5% creatine monohydrate diet from midgestation (day 20) to term (39 days). Placentas and neonatal kidney, liver, heart, and brain collected at 24 hours of age underwent quantitative polymerase chain reaction and Western blot analysis. Maternal creatine had no effect on the expression of AGAT and GAMT in neonatal kidney and liver, but mRNA expression of AGAT in brain tissues was significantly decreased in both male and female neonates born to mothers who were fed the creatine diet. SLC6A8 expression was not affected by maternal dietary creatine loading in any tissues. Maternal dietary creatine supplementation from midgestation in the spiny mouse did not alter the capacity for creatine synthesis or transport.

Takanori Kumagai - One of the best experts on this subject based on the ideXlab platform.

  • the role of glyoxalase system in renal hypoxia
    Advances in Experimental Medicine and Biology, 2010
    Co-Authors: Reiko Inagi, Takanori Kumagai, Toshiro Fujita, Masaomi Nangaku
    Abstract:

    Methylglyoxal (MG), a highly reactive α-oxoaldehyde generated by oxidation of carbohydrate and glycolysis, binds to proteins and forms advanced glycation end products (AGE). MG and MG adducts have been implicated in oxidative stress-related diseases, therefore, MG detoxifying system such as the glyoxalase system (glyoxalase I) also contributes to progression of these diseases. Recent papers have emphasized the pathophysiological effects of MG and the glyoxalase system in acute Hypoxic Injury, which is associated with acute oxidative stress. We investigated the kinetics of MG level and glyoxalase I activity in renal acute Hypoxic Injury induced by ischemia-reperfusion (I/R). I/R induced tubulointerstitial Injury and the histological changes were associated with a significant decrease in renal glyoxalase I activity and an increase in MG level in the damaged tubular cells. Of note, rats over expressing human glyoxalase I showed amelioration of I/R-induced histological and functional damages and it was associated with a decrease in MG level in the lesion resulting in reduction of oxidative stress and tubular cell apoptosis. In conclusion, glyoxalase I has renoprotective effects in renal hypoxia such as I/R Injury via a reduction in cytotoxic MG level in tubular cells.

  • pathophysiological role of the glyoxalase system in renal Hypoxic Injury
    Annals of the New York Academy of Sciences, 2008
    Co-Authors: Takanori Kumagai, Masaomi Nangaku, Reiko Inagi
    Abstract:

    Methylglyoxal (MG), a reactive dicarbonyl compound mainly produced by metabolic pathways, such as glycolysis, binds to proteins or nucleic acids and forms advanced glycation end products. MG is efficiently metabolized by the glyoxalase system where MG is converted by glyoxalase I (GLO I) to S-D-lactoylglutathione. Although the glyoxalase system has been shown to play a pathological role in various diseases, including diabetic complications, its detailed pathophysiological function remains to be elucidated. We are interested in renal Hypoxic diseases, but very little information is available regarding the association between the glyoxalase system and renal Hypoxic diseases. Therefore, we investigated the biological role of GLO I in renal Hypoxic diseases by using the rat ischemia/reperfusion (I/R) Injury model. I/R induced the reduction of renal GLO I activity associated with morphological changes and renal dysfunction. Interestingly, the rats that overexpress human GLO I (GLO I Tg rats) showed amelioration of these manifestations in renal I/R (e.g., improvement of the tubulointerstitial Injury and renal function). Accumulation of renal MG adducts, carboxyethyllysine, induced by I/R also decreased in GLO I Tg rats compared to wild-type rats. These results demonstrate that GLO I has renoprotective effects in I/R Injury via reduction of protein modification by MG.