Peroxynitrite-induced oxidation and its effects on isolated proteasomal systems

Amici, Manila

doi:10.1016/s0891-5849(02)01369-2

Cited by 53 publications

(36 citation statements)

References 50 publications

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“…The absence of a significant increase of ROS after EtOH treatment in HIV-1 infected MDM may explain why IPR activity was not altered in infected cells after alcohol exposure. It was shown that IPR are more susceptible to ROS-mediated inhibition compared with constitutive PR [39]. Indeed, we were able to completely restore the IPR activity in EtOH-treated and IFN-c stimulated MDM by anti-oxidant.…”

Section: Discussionmentioning

confidence: 55%

“…6C). These data were substantiated by Western blot detection of 215 kDa nitrated protein, an established marker of peroxynitrite oxidation [39]. As positive controls we used three nitrated proteins of molecular weight 16 kDa (nitrated bovine superoxide dismutase), 66 kDa (nitrated bovine serum albumin) and 215 kDa (nitrated rabbit muscle myosin).…”

Section: Etoh Metabolism By Cyp2e1 Leads To Ros Production In Mdmmentioning

confidence: 96%

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Alcohol and HIV decrease proteasome and immunoproteasome function in macrophages: implications for impaired immune function during disease

Haorah

Heilman

Diekmann

et al. 2004

Cellular Immunology

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Proteasomes (proteinase complexes, PR) and immunoproteasomes (IPR) degrade damaged proteins and affect protein processing required for antigen presentation by mononuclear phagocytes. These critical immune processes are attenuated during progressive HIV-1 infection and are affected by alcohol abuse. To investigate the mechanisms underlying these functional changes, we measured PR and CYP2E1 activities [an ethanol (EtOH) metabolizing enzyme] and reactive oxygen species (ROS) in human monocyte-derived macrophages (MDM) following HIV-1 infection and EtOH treatment. We observed progressive declines of PR activity and PR/IPR contents in HIV-1-infected MDM. PR activity and IPR expression increased after IFN-c stimulation but reduced after HIV-1 infection. EtOH inhibited both IFN-c-induced PR and IPR. Paradoxically, EtOH attenuated PR catalytic activity in infected MDM and suppressed viral replication. Elevated ROS followed EtOH exposure and paralleled decreased PR activity. The latter was restored by anti-oxidant. The data support the notion that HIV-1 infection and EtOH may work in concert to affect immune function including antigen presentation and thereby affect disease progression.

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Section: Discussionmentioning

confidence: 55%

Section: Etoh Metabolism By Cyp2e1 Leads To Ros Production In Mdmmentioning

confidence: 96%

Alcohol and HIV decrease proteasome and immunoproteasome function in macrophages: implications for impaired immune function during disease

Haorah

Heilman

Diekmann

et al. 2004

Cellular Immunology

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“…Furthermore, exposure of isolated proteasome to oxidants, such as ONOO Ϫ , leads to alteration of proteasome activation, 44 whereas exposure of certain cellular proteins to ONOO Ϫ leads to increased oxidation followed by preferential degradation by the proteasomal system. 45 The mechanism of preferential degradation of GTPCH in diabetes mellitus, however, remains unknown.…”

Section: Discussionmentioning

confidence: 99%

Proteasome-Dependent Degradation of Guanosine 5′-Triphosphate Cyclohydrolase I Causes Tetrahydrobiopterin Deficiency in Diabetes Mellitus

et al. 2007

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Background-Tetrahydrobiopterin (BH4) deficiency is reported to uncouple the enzymatic activity of endothelial nitric oxide synthase in diabetes mellitus. The mechanism by which diabetes actually leads to BH4 deficiency remains elusive. Here, we demonstrate that diabetes reduced BH4 by increasing 26S proteasome-dependent degradation of guanosine 5Ј-triphosphate cyclohydrolase I (GTPCH), a rate-limiting enzyme in the synthesis of BH4, in parallel with increased formation of both superoxide and peroxynitrite (ONOO Ϫ ). Methods and Results-Exposure

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“…58,59 IPR activity is susceptible to inhibition by reactive oxygen species. 60 Re-active oxygen species generation was linked to ethanol metabolism in neural cells 61 and macrophages resulting in IPR dysfunction. 22 Indeed, brain tissue of ethanol-fed mice featured higher levels of nitrotyrosine indicating enhanced oxidative damage.…”

Section: Discussionmentioning

confidence: 99%

Alcohol Abuse Enhances Neuroinflammation and Impairs Immune Responses in an Animal Model of Human Immunodeficiency Virus-1 Encephalitis

Potula

Haorah

Knipe

et al. 2006

The American Journal of Pathology

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Peroxynitrite-induced oxidation and its effects on isolated proteasomal systems

Cited by 53 publications

References 50 publications

Alcohol and HIV decrease proteasome and immunoproteasome function in macrophages: implications for impaired immune function during disease

Alcohol and HIV decrease proteasome and immunoproteasome function in macrophages: implications for impaired immune function during disease

Proteasome-Dependent Degradation of Guanosine 5′-Triphosphate Cyclohydrolase I Causes Tetrahydrobiopterin Deficiency in Diabetes Mellitus

Alcohol Abuse Enhances Neuroinflammation and Impairs Immune Responses in an Animal Model of Human Immunodeficiency Virus-1 Encephalitis

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