Impairment of glyoxalase-1, an advanced glycation end-product detoxifying enzyme, induced by inflammation in age-related osteoarthritis

Background Accumulation of advanced glycation end-products (AGEs) is involved in age-related osteoarthritis (OA). Glyoxalase (Glo)-1 is the main enzyme involved in the removal of AGE precursors, especially carboxymethyl-lysine (CML). We aimed to investigate the expression of several AGEs and Glo-1 i...
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Autor*in:	Trellu, Sabine [verfasserIn] Courties, Alice Jaisson, Stéphane Gorisse, Laëtitia Gillery, Philippe Kerdine-Römer, Saadia Vaamonde-Garcia, Carlos Houard, Xavier Ekhirch, François-Paul Sautet, Alain Friguet, Bertrand Jacques, Claire Berenbaum, Francis Sellam, Jérémie

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2019

Schlagwörter:	Aging Advanced glycation end-product Chondrocyte Osteoarthritis Glyoxalase Carboxymethyl-lysine

Anmerkung:	© The Author(s). 2019

Übergeordnetes Werk:	Enthalten in: Arthritis Research & Therapy - London : BioMed Central, 1999, 21(2019), 1 vom: 11. Jan.
Übergeordnetes Werk:	volume:21 ; year:2019 ; number:1 ; day:11 ; month:01

Links:	Volltext

DOI / URN:	10.1186/s13075-018-1801-y

Katalog-ID:	SPR030229731

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520			\|a Background Accumulation of advanced glycation end-products (AGEs) is involved in age-related osteoarthritis (OA). Glyoxalase (Glo)-1 is the main enzyme involved in the removal of AGE precursors, especially carboxymethyl-lysine (CML). We aimed to investigate the expression of several AGEs and Glo-1 in human OA cartilage and to study chondrocytic Glo-1 regulation by inflammation, mediated by interleukin (IL)-1β. Methods Ex vivo, we quantified AGEs (pentosidine, CML, methylglyoxal-hydroimidazolone-1) in knee cartilage from 30 OA patients. Explants were also incubated with and without IL-1β, and we assessed Glo-1 protein expression and enzymatic activity. In vitro, primary cultured murine chondrocytes were stimulated with increasing concentrations of IL-1β to assess Glo-1 enzymatic activity and expression. To investigate the role of oxidative stress in the IL-1β effect, cells were also treated with inhibitors of mitochondrial oxidative stress or nitric oxide synthase. Results Ex vivo, only the human cartilage CML content was correlated with patient age (r = 0.78, p = 0.0031). No statistically significant correlation was found between Glo-1 protein expression and enzymatic activity in human cartilage and patient age. We observed that cartilage explant stimulation with IL-1β decreased Glo-1 protein expression and enzymatic activity. In vitro, we observed a dose-dependent decrease in Glo-1 mRNA, protein quantity, and enzymatic activity in response to IL-1β in murine chondrocytes. Inhibitors of oxidative stress blunted this downregulation. Conclusion Glo-1 is impaired by inflammation mediated by IL-1β in chondrocytes through oxidative stress pathways and may explain age-dependent accumulation of the AGE CML in OA cartilage.
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allfields	10.1186/s13075-018-1801-y doi (DE-627)SPR030229731 (SPR)s13075-018-1801-y-e DE-627 ger DE-627 rakwb eng Trellu, Sabine verfasserin aut Impairment of glyoxalase-1, an advanced glycation end-product detoxifying enzyme, induced by inflammation in age-related osteoarthritis 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s). 2019 Background Accumulation of advanced glycation end-products (AGEs) is involved in age-related osteoarthritis (OA). Glyoxalase (Glo)-1 is the main enzyme involved in the removal of AGE precursors, especially carboxymethyl-lysine (CML). We aimed to investigate the expression of several AGEs and Glo-1 in human OA cartilage and to study chondrocytic Glo-1 regulation by inflammation, mediated by interleukin (IL)-1β. Methods Ex vivo, we quantified AGEs (pentosidine, CML, methylglyoxal-hydroimidazolone-1) in knee cartilage from 30 OA patients. Explants were also incubated with and without IL-1β, and we assessed Glo-1 protein expression and enzymatic activity. In vitro, primary cultured murine chondrocytes were stimulated with increasing concentrations of IL-1β to assess Glo-1 enzymatic activity and expression. To investigate the role of oxidative stress in the IL-1β effect, cells were also treated with inhibitors of mitochondrial oxidative stress or nitric oxide synthase. Results Ex vivo, only the human cartilage CML content was correlated with patient age (r = 0.78, p = 0.0031). No statistically significant correlation was found between Glo-1 protein expression and enzymatic activity in human cartilage and patient age. We observed that cartilage explant stimulation with IL-1β decreased Glo-1 protein expression and enzymatic activity. In vitro, we observed a dose-dependent decrease in Glo-1 mRNA, protein quantity, and enzymatic activity in response to IL-1β in murine chondrocytes. Inhibitors of oxidative stress blunted this downregulation. Conclusion Glo-1 is impaired by inflammation mediated by IL-1β in chondrocytes through oxidative stress pathways and may explain age-dependent accumulation of the AGE CML in OA cartilage. Aging (dpeaa)DE-He213 Advanced glycation end-product (dpeaa)DE-He213 Chondrocyte (dpeaa)DE-He213 Osteoarthritis (dpeaa)DE-He213 Glyoxalase (dpeaa)DE-He213 Carboxymethyl-lysine (dpeaa)DE-He213 Courties, Alice aut Jaisson, Stéphane aut Gorisse, Laëtitia aut Gillery, Philippe aut Kerdine-Römer, Saadia aut Vaamonde-Garcia, Carlos aut Houard, Xavier aut Ekhirch, François-Paul aut Sautet, Alain aut Friguet, Bertrand aut Jacques, Claire aut Berenbaum, Francis aut Sellam, Jérémie aut Enthalten in Arthritis Research & Therapy London : BioMed Central, 1999 21(2019), 1 vom: 11. Jan. (DE-627)326646418 (DE-600)2041668-4 1478-6354 nnns volume:21 year:2019 number:1 day:11 month:01 https://dx.doi.org/10.1186/s13075-018-1801-y kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2019 1 11 01
spelling	10.1186/s13075-018-1801-y doi (DE-627)SPR030229731 (SPR)s13075-018-1801-y-e DE-627 ger DE-627 rakwb eng Trellu, Sabine verfasserin aut Impairment of glyoxalase-1, an advanced glycation end-product detoxifying enzyme, induced by inflammation in age-related osteoarthritis 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s). 2019 Background Accumulation of advanced glycation end-products (AGEs) is involved in age-related osteoarthritis (OA). Glyoxalase (Glo)-1 is the main enzyme involved in the removal of AGE precursors, especially carboxymethyl-lysine (CML). We aimed to investigate the expression of several AGEs and Glo-1 in human OA cartilage and to study chondrocytic Glo-1 regulation by inflammation, mediated by interleukin (IL)-1β. Methods Ex vivo, we quantified AGEs (pentosidine, CML, methylglyoxal-hydroimidazolone-1) in knee cartilage from 30 OA patients. Explants were also incubated with and without IL-1β, and we assessed Glo-1 protein expression and enzymatic activity. In vitro, primary cultured murine chondrocytes were stimulated with increasing concentrations of IL-1β to assess Glo-1 enzymatic activity and expression. To investigate the role of oxidative stress in the IL-1β effect, cells were also treated with inhibitors of mitochondrial oxidative stress or nitric oxide synthase. Results Ex vivo, only the human cartilage CML content was correlated with patient age (r = 0.78, p = 0.0031). No statistically significant correlation was found between Glo-1 protein expression and enzymatic activity in human cartilage and patient age. We observed that cartilage explant stimulation with IL-1β decreased Glo-1 protein expression and enzymatic activity. In vitro, we observed a dose-dependent decrease in Glo-1 mRNA, protein quantity, and enzymatic activity in response to IL-1β in murine chondrocytes. Inhibitors of oxidative stress blunted this downregulation. Conclusion Glo-1 is impaired by inflammation mediated by IL-1β in chondrocytes through oxidative stress pathways and may explain age-dependent accumulation of the AGE CML in OA cartilage. Aging (dpeaa)DE-He213 Advanced glycation end-product (dpeaa)DE-He213 Chondrocyte (dpeaa)DE-He213 Osteoarthritis (dpeaa)DE-He213 Glyoxalase (dpeaa)DE-He213 Carboxymethyl-lysine (dpeaa)DE-He213 Courties, Alice aut Jaisson, Stéphane aut Gorisse, Laëtitia aut Gillery, Philippe aut Kerdine-Römer, Saadia aut Vaamonde-Garcia, Carlos aut Houard, Xavier aut Ekhirch, François-Paul aut Sautet, Alain aut Friguet, Bertrand aut Jacques, Claire aut Berenbaum, Francis aut Sellam, Jérémie aut Enthalten in Arthritis Research & Therapy London : BioMed Central, 1999 21(2019), 1 vom: 11. Jan. (DE-627)326646418 (DE-600)2041668-4 1478-6354 nnns volume:21 year:2019 number:1 day:11 month:01 https://dx.doi.org/10.1186/s13075-018-1801-y kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2019 1 11 01
allfields_unstemmed	10.1186/s13075-018-1801-y doi (DE-627)SPR030229731 (SPR)s13075-018-1801-y-e DE-627 ger DE-627 rakwb eng Trellu, Sabine verfasserin aut Impairment of glyoxalase-1, an advanced glycation end-product detoxifying enzyme, induced by inflammation in age-related osteoarthritis 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s). 2019 Background Accumulation of advanced glycation end-products (AGEs) is involved in age-related osteoarthritis (OA). Glyoxalase (Glo)-1 is the main enzyme involved in the removal of AGE precursors, especially carboxymethyl-lysine (CML). We aimed to investigate the expression of several AGEs and Glo-1 in human OA cartilage and to study chondrocytic Glo-1 regulation by inflammation, mediated by interleukin (IL)-1β. Methods Ex vivo, we quantified AGEs (pentosidine, CML, methylglyoxal-hydroimidazolone-1) in knee cartilage from 30 OA patients. Explants were also incubated with and without IL-1β, and we assessed Glo-1 protein expression and enzymatic activity. In vitro, primary cultured murine chondrocytes were stimulated with increasing concentrations of IL-1β to assess Glo-1 enzymatic activity and expression. To investigate the role of oxidative stress in the IL-1β effect, cells were also treated with inhibitors of mitochondrial oxidative stress or nitric oxide synthase. Results Ex vivo, only the human cartilage CML content was correlated with patient age (r = 0.78, p = 0.0031). No statistically significant correlation was found between Glo-1 protein expression and enzymatic activity in human cartilage and patient age. We observed that cartilage explant stimulation with IL-1β decreased Glo-1 protein expression and enzymatic activity. In vitro, we observed a dose-dependent decrease in Glo-1 mRNA, protein quantity, and enzymatic activity in response to IL-1β in murine chondrocytes. Inhibitors of oxidative stress blunted this downregulation. Conclusion Glo-1 is impaired by inflammation mediated by IL-1β in chondrocytes through oxidative stress pathways and may explain age-dependent accumulation of the AGE CML in OA cartilage. Aging (dpeaa)DE-He213 Advanced glycation end-product (dpeaa)DE-He213 Chondrocyte (dpeaa)DE-He213 Osteoarthritis (dpeaa)DE-He213 Glyoxalase (dpeaa)DE-He213 Carboxymethyl-lysine (dpeaa)DE-He213 Courties, Alice aut Jaisson, Stéphane aut Gorisse, Laëtitia aut Gillery, Philippe aut Kerdine-Römer, Saadia aut Vaamonde-Garcia, Carlos aut Houard, Xavier aut Ekhirch, François-Paul aut Sautet, Alain aut Friguet, Bertrand aut Jacques, Claire aut Berenbaum, Francis aut Sellam, Jérémie aut Enthalten in Arthritis Research & Therapy London : BioMed Central, 1999 21(2019), 1 vom: 11. Jan. (DE-627)326646418 (DE-600)2041668-4 1478-6354 nnns volume:21 year:2019 number:1 day:11 month:01 https://dx.doi.org/10.1186/s13075-018-1801-y kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2019 1 11 01
allfieldsGer	10.1186/s13075-018-1801-y doi (DE-627)SPR030229731 (SPR)s13075-018-1801-y-e DE-627 ger DE-627 rakwb eng Trellu, Sabine verfasserin aut Impairment of glyoxalase-1, an advanced glycation end-product detoxifying enzyme, induced by inflammation in age-related osteoarthritis 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s). 2019 Background Accumulation of advanced glycation end-products (AGEs) is involved in age-related osteoarthritis (OA). Glyoxalase (Glo)-1 is the main enzyme involved in the removal of AGE precursors, especially carboxymethyl-lysine (CML). We aimed to investigate the expression of several AGEs and Glo-1 in human OA cartilage and to study chondrocytic Glo-1 regulation by inflammation, mediated by interleukin (IL)-1β. Methods Ex vivo, we quantified AGEs (pentosidine, CML, methylglyoxal-hydroimidazolone-1) in knee cartilage from 30 OA patients. Explants were also incubated with and without IL-1β, and we assessed Glo-1 protein expression and enzymatic activity. In vitro, primary cultured murine chondrocytes were stimulated with increasing concentrations of IL-1β to assess Glo-1 enzymatic activity and expression. To investigate the role of oxidative stress in the IL-1β effect, cells were also treated with inhibitors of mitochondrial oxidative stress or nitric oxide synthase. Results Ex vivo, only the human cartilage CML content was correlated with patient age (r = 0.78, p = 0.0031). No statistically significant correlation was found between Glo-1 protein expression and enzymatic activity in human cartilage and patient age. We observed that cartilage explant stimulation with IL-1β decreased Glo-1 protein expression and enzymatic activity. In vitro, we observed a dose-dependent decrease in Glo-1 mRNA, protein quantity, and enzymatic activity in response to IL-1β in murine chondrocytes. Inhibitors of oxidative stress blunted this downregulation. Conclusion Glo-1 is impaired by inflammation mediated by IL-1β in chondrocytes through oxidative stress pathways and may explain age-dependent accumulation of the AGE CML in OA cartilage. Aging (dpeaa)DE-He213 Advanced glycation end-product (dpeaa)DE-He213 Chondrocyte (dpeaa)DE-He213 Osteoarthritis (dpeaa)DE-He213 Glyoxalase (dpeaa)DE-He213 Carboxymethyl-lysine (dpeaa)DE-He213 Courties, Alice aut Jaisson, Stéphane aut Gorisse, Laëtitia aut Gillery, Philippe aut Kerdine-Römer, Saadia aut Vaamonde-Garcia, Carlos aut Houard, Xavier aut Ekhirch, François-Paul aut Sautet, Alain aut Friguet, Bertrand aut Jacques, Claire aut Berenbaum, Francis aut Sellam, Jérémie aut Enthalten in Arthritis Research & Therapy London : BioMed Central, 1999 21(2019), 1 vom: 11. Jan. (DE-627)326646418 (DE-600)2041668-4 1478-6354 nnns volume:21 year:2019 number:1 day:11 month:01 https://dx.doi.org/10.1186/s13075-018-1801-y kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2019 1 11 01
allfieldsSound	10.1186/s13075-018-1801-y doi (DE-627)SPR030229731 (SPR)s13075-018-1801-y-e DE-627 ger DE-627 rakwb eng Trellu, Sabine verfasserin aut Impairment of glyoxalase-1, an advanced glycation end-product detoxifying enzyme, induced by inflammation in age-related osteoarthritis 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s). 2019 Background Accumulation of advanced glycation end-products (AGEs) is involved in age-related osteoarthritis (OA). Glyoxalase (Glo)-1 is the main enzyme involved in the removal of AGE precursors, especially carboxymethyl-lysine (CML). We aimed to investigate the expression of several AGEs and Glo-1 in human OA cartilage and to study chondrocytic Glo-1 regulation by inflammation, mediated by interleukin (IL)-1β. Methods Ex vivo, we quantified AGEs (pentosidine, CML, methylglyoxal-hydroimidazolone-1) in knee cartilage from 30 OA patients. Explants were also incubated with and without IL-1β, and we assessed Glo-1 protein expression and enzymatic activity. In vitro, primary cultured murine chondrocytes were stimulated with increasing concentrations of IL-1β to assess Glo-1 enzymatic activity and expression. To investigate the role of oxidative stress in the IL-1β effect, cells were also treated with inhibitors of mitochondrial oxidative stress or nitric oxide synthase. Results Ex vivo, only the human cartilage CML content was correlated with patient age (r = 0.78, p = 0.0031). No statistically significant correlation was found between Glo-1 protein expression and enzymatic activity in human cartilage and patient age. We observed that cartilage explant stimulation with IL-1β decreased Glo-1 protein expression and enzymatic activity. In vitro, we observed a dose-dependent decrease in Glo-1 mRNA, protein quantity, and enzymatic activity in response to IL-1β in murine chondrocytes. Inhibitors of oxidative stress blunted this downregulation. Conclusion Glo-1 is impaired by inflammation mediated by IL-1β in chondrocytes through oxidative stress pathways and may explain age-dependent accumulation of the AGE CML in OA cartilage. Aging (dpeaa)DE-He213 Advanced glycation end-product (dpeaa)DE-He213 Chondrocyte (dpeaa)DE-He213 Osteoarthritis (dpeaa)DE-He213 Glyoxalase (dpeaa)DE-He213 Carboxymethyl-lysine (dpeaa)DE-He213 Courties, Alice aut Jaisson, Stéphane aut Gorisse, Laëtitia aut Gillery, Philippe aut Kerdine-Römer, Saadia aut Vaamonde-Garcia, Carlos aut Houard, Xavier aut Ekhirch, François-Paul aut Sautet, Alain aut Friguet, Bertrand aut Jacques, Claire aut Berenbaum, Francis aut Sellam, Jérémie aut Enthalten in Arthritis Research & Therapy London : BioMed Central, 1999 21(2019), 1 vom: 11. Jan. (DE-627)326646418 (DE-600)2041668-4 1478-6354 nnns volume:21 year:2019 number:1 day:11 month:01 https://dx.doi.org/10.1186/s13075-018-1801-y kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2019 1 11 01
language	English
source	Enthalten in Arthritis Research & Therapy 21(2019), 1 vom: 11. Jan. volume:21 year:2019 number:1 day:11 month:01
sourceStr	Enthalten in Arthritis Research & Therapy 21(2019), 1 vom: 11. Jan. volume:21 year:2019 number:1 day:11 month:01
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Aging Advanced glycation end-product Chondrocyte Osteoarthritis Glyoxalase Carboxymethyl-lysine
isfreeaccess_bool	true
container_title	Arthritis Research & Therapy
authorswithroles_txt_mv	Trellu, Sabine @@aut@@ Courties, Alice @@aut@@ Jaisson, Stéphane @@aut@@ Gorisse, Laëtitia @@aut@@ Gillery, Philippe @@aut@@ Kerdine-Römer, Saadia @@aut@@ Vaamonde-Garcia, Carlos @@aut@@ Houard, Xavier @@aut@@ Ekhirch, François-Paul @@aut@@ Sautet, Alain @@aut@@ Friguet, Bertrand @@aut@@ Jacques, Claire @@aut@@ Berenbaum, Francis @@aut@@ Sellam, Jérémie @@aut@@
publishDateDaySort_date	2019-01-11T00:00:00Z
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Glyoxalase (Glo)-1 is the main enzyme involved in the removal of AGE precursors, especially carboxymethyl-lysine (CML). We aimed to investigate the expression of several AGEs and Glo-1 in human OA cartilage and to study chondrocytic Glo-1 regulation by inflammation, mediated by interleukin (IL)-1β. Methods Ex vivo, we quantified AGEs (pentosidine, CML, methylglyoxal-hydroimidazolone-1) in knee cartilage from 30 OA patients. Explants were also incubated with and without IL-1β, and we assessed Glo-1 protein expression and enzymatic activity. In vitro, primary cultured murine chondrocytes were stimulated with increasing concentrations of IL-1β to assess Glo-1 enzymatic activity and expression. To investigate the role of oxidative stress in the IL-1β effect, cells were also treated with inhibitors of mitochondrial oxidative stress or nitric oxide synthase. Results Ex vivo, only the human cartilage CML content was correlated with patient age (r = 0.78, p = 0.0031). 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author	Trellu, Sabine
spellingShingle	Trellu, Sabine misc Aging misc Advanced glycation end-product misc Chondrocyte misc Osteoarthritis misc Glyoxalase misc Carboxymethyl-lysine Impairment of glyoxalase-1, an advanced glycation end-product detoxifying enzyme, induced by inflammation in age-related osteoarthritis
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topic_title	Impairment of glyoxalase-1, an advanced glycation end-product detoxifying enzyme, induced by inflammation in age-related osteoarthritis Aging (dpeaa)DE-He213 Advanced glycation end-product (dpeaa)DE-He213 Chondrocyte (dpeaa)DE-He213 Osteoarthritis (dpeaa)DE-He213 Glyoxalase (dpeaa)DE-He213 Carboxymethyl-lysine (dpeaa)DE-He213
topic	misc Aging misc Advanced glycation end-product misc Chondrocyte misc Osteoarthritis misc Glyoxalase misc Carboxymethyl-lysine
topic_unstemmed	misc Aging misc Advanced glycation end-product misc Chondrocyte misc Osteoarthritis misc Glyoxalase misc Carboxymethyl-lysine
topic_browse	misc Aging misc Advanced glycation end-product misc Chondrocyte misc Osteoarthritis misc Glyoxalase misc Carboxymethyl-lysine
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title	Impairment of glyoxalase-1, an advanced glycation end-product detoxifying enzyme, induced by inflammation in age-related osteoarthritis
ctrlnum	(DE-627)SPR030229731 (SPR)s13075-018-1801-y-e
title_full	Impairment of glyoxalase-1, an advanced glycation end-product detoxifying enzyme, induced by inflammation in age-related osteoarthritis
author_sort	Trellu, Sabine
journal	Arthritis Research & Therapy
journalStr	Arthritis Research & Therapy
lang_code	eng
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author_browse	Trellu, Sabine Courties, Alice Jaisson, Stéphane Gorisse, Laëtitia Gillery, Philippe Kerdine-Römer, Saadia Vaamonde-Garcia, Carlos Houard, Xavier Ekhirch, François-Paul Sautet, Alain Friguet, Bertrand Jacques, Claire Berenbaum, Francis Sellam, Jérémie
container_volume	21
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author-letter	Trellu, Sabine
doi_str_mv	10.1186/s13075-018-1801-y
title_sort	impairment of glyoxalase-1, an advanced glycation end-product detoxifying enzyme, induced by inflammation in age-related osteoarthritis
title_auth	Impairment of glyoxalase-1, an advanced glycation end-product detoxifying enzyme, induced by inflammation in age-related osteoarthritis
abstract	Background Accumulation of advanced glycation end-products (AGEs) is involved in age-related osteoarthritis (OA). Glyoxalase (Glo)-1 is the main enzyme involved in the removal of AGE precursors, especially carboxymethyl-lysine (CML). We aimed to investigate the expression of several AGEs and Glo-1 in human OA cartilage and to study chondrocytic Glo-1 regulation by inflammation, mediated by interleukin (IL)-1β. Methods Ex vivo, we quantified AGEs (pentosidine, CML, methylglyoxal-hydroimidazolone-1) in knee cartilage from 30 OA patients. Explants were also incubated with and without IL-1β, and we assessed Glo-1 protein expression and enzymatic activity. In vitro, primary cultured murine chondrocytes were stimulated with increasing concentrations of IL-1β to assess Glo-1 enzymatic activity and expression. To investigate the role of oxidative stress in the IL-1β effect, cells were also treated with inhibitors of mitochondrial oxidative stress or nitric oxide synthase. Results Ex vivo, only the human cartilage CML content was correlated with patient age (r = 0.78, p = 0.0031). No statistically significant correlation was found between Glo-1 protein expression and enzymatic activity in human cartilage and patient age. We observed that cartilage explant stimulation with IL-1β decreased Glo-1 protein expression and enzymatic activity. In vitro, we observed a dose-dependent decrease in Glo-1 mRNA, protein quantity, and enzymatic activity in response to IL-1β in murine chondrocytes. Inhibitors of oxidative stress blunted this downregulation. Conclusion Glo-1 is impaired by inflammation mediated by IL-1β in chondrocytes through oxidative stress pathways and may explain age-dependent accumulation of the AGE CML in OA cartilage. © The Author(s). 2019
abstractGer	Background Accumulation of advanced glycation end-products (AGEs) is involved in age-related osteoarthritis (OA). Glyoxalase (Glo)-1 is the main enzyme involved in the removal of AGE precursors, especially carboxymethyl-lysine (CML). We aimed to investigate the expression of several AGEs and Glo-1 in human OA cartilage and to study chondrocytic Glo-1 regulation by inflammation, mediated by interleukin (IL)-1β. Methods Ex vivo, we quantified AGEs (pentosidine, CML, methylglyoxal-hydroimidazolone-1) in knee cartilage from 30 OA patients. Explants were also incubated with and without IL-1β, and we assessed Glo-1 protein expression and enzymatic activity. In vitro, primary cultured murine chondrocytes were stimulated with increasing concentrations of IL-1β to assess Glo-1 enzymatic activity and expression. To investigate the role of oxidative stress in the IL-1β effect, cells were also treated with inhibitors of mitochondrial oxidative stress or nitric oxide synthase. Results Ex vivo, only the human cartilage CML content was correlated with patient age (r = 0.78, p = 0.0031). No statistically significant correlation was found between Glo-1 protein expression and enzymatic activity in human cartilage and patient age. We observed that cartilage explant stimulation with IL-1β decreased Glo-1 protein expression and enzymatic activity. In vitro, we observed a dose-dependent decrease in Glo-1 mRNA, protein quantity, and enzymatic activity in response to IL-1β in murine chondrocytes. Inhibitors of oxidative stress blunted this downregulation. Conclusion Glo-1 is impaired by inflammation mediated by IL-1β in chondrocytes through oxidative stress pathways and may explain age-dependent accumulation of the AGE CML in OA cartilage. © The Author(s). 2019
abstract_unstemmed	Background Accumulation of advanced glycation end-products (AGEs) is involved in age-related osteoarthritis (OA). Glyoxalase (Glo)-1 is the main enzyme involved in the removal of AGE precursors, especially carboxymethyl-lysine (CML). We aimed to investigate the expression of several AGEs and Glo-1 in human OA cartilage and to study chondrocytic Glo-1 regulation by inflammation, mediated by interleukin (IL)-1β. Methods Ex vivo, we quantified AGEs (pentosidine, CML, methylglyoxal-hydroimidazolone-1) in knee cartilage from 30 OA patients. Explants were also incubated with and without IL-1β, and we assessed Glo-1 protein expression and enzymatic activity. In vitro, primary cultured murine chondrocytes were stimulated with increasing concentrations of IL-1β to assess Glo-1 enzymatic activity and expression. To investigate the role of oxidative stress in the IL-1β effect, cells were also treated with inhibitors of mitochondrial oxidative stress or nitric oxide synthase. Results Ex vivo, only the human cartilage CML content was correlated with patient age (r = 0.78, p = 0.0031). No statistically significant correlation was found between Glo-1 protein expression and enzymatic activity in human cartilage and patient age. We observed that cartilage explant stimulation with IL-1β decreased Glo-1 protein expression and enzymatic activity. In vitro, we observed a dose-dependent decrease in Glo-1 mRNA, protein quantity, and enzymatic activity in response to IL-1β in murine chondrocytes. Inhibitors of oxidative stress blunted this downregulation. Conclusion Glo-1 is impaired by inflammation mediated by IL-1β in chondrocytes through oxidative stress pathways and may explain age-dependent accumulation of the AGE CML in OA cartilage. © The Author(s). 2019
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container_issue	1
title_short	Impairment of glyoxalase-1, an advanced glycation end-product detoxifying enzyme, induced by inflammation in age-related osteoarthritis
url	https://dx.doi.org/10.1186/s13075-018-1801-y
remote_bool	true
author2	Courties, Alice Jaisson, Stéphane Gorisse, Laëtitia Gillery, Philippe Kerdine-Römer, Saadia Vaamonde-Garcia, Carlos Houard, Xavier Ekhirch, François-Paul Sautet, Alain Friguet, Bertrand Jacques, Claire Berenbaum, Francis Sellam, Jérémie
author2Str	Courties, Alice Jaisson, Stéphane Gorisse, Laëtitia Gillery, Philippe Kerdine-Römer, Saadia Vaamonde-Garcia, Carlos Houard, Xavier Ekhirch, François-Paul Sautet, Alain Friguet, Bertrand Jacques, Claire Berenbaum, Francis Sellam, Jérémie
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up_date	2024-07-03T14:49:25.210Z
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