20 S Proteasome from Saccharomyces cerevisiae Is Responsive to Redox Modifications and IsS-Glutathionylated

Demasi, Marilene; Silva, Gustavo Monteiro; Netto, Luís Eduardo Soares

doi:10.1074/jbc.m209282200

Cited by 115 publications

(96 citation statements)

References 40 publications

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“…In fact, recent data suggests that the reversible S-glutathionylation of cysteine may be an important physiological regulator of the chymotrypsin-like activity (Demasi et al, 2001;Demasi et al, 2003). The current results further implicate the importance of cysteine residues for chymotrypsin-like activity by showing that the sulfhydryl-reactive compound NEM reduced degradation of both the LLVY peptide and the model substrate.…”

Section: Mechanisms Of Chymotrypsin-like Inhibitionsupporting

confidence: 74%

“…Evidence from previous studies showing partial reversal of peroxide-induced inhibition of chymotrypsin-like activity by DTT and the inhibition of chymotrypsin-like activity by sulfhydryl blocking compounds (Demasi et al, 2003;Andersson et al, 1999), suggest that at least one of the sites critical for maintenance of chymotrypsin-like activity is a cysteine residue. In fact, recent data suggests that the reversible S-glutathionylation of cysteine may be an important physiological regulator of the chymotrypsin-like activity (Demasi et al, 2001;Demasi et al, 2003).…”

Section: Mechanisms Of Chymotrypsin-like Inhibitionmentioning

confidence: 91%

“…Previous studies have shown oxidation or modification of a reactive cysteine residue can inhibit the chymotrypsin-like activity (Andersson et al, 1999;Demasi et al, 2003). To determine if there were age-dependent differences in the extent of reversible cysteine modification, we measured the chymotrypsin-like activity in the absence and presence of DTT.…”

Section: Inhibition Of Proteasome Activity With N-ethylmaleimidementioning

confidence: 99%

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Age-dependent inhibition of proteasome chymotrypsin-like activity in the retina

Kapphahn

Bigelow

Ferrington

2007

Experimental Eye Research

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The proteasome plays a fundamental role in processes essential for cell viability. A loss in proteasome function has been associated with aging, as well as a number of age-related diseases. Defining the mechanism(s) behind this loss in function will add important information regarding the molecular basis for aging. In the current study, we performed an age-based comparison of proteasome function and composition of subunits and regulatory proteins in the neural retina and retinal pigment epithelium (RPE) in Fischer 344 rats. In the RPE, there was no age-dependent difference in activity, subunit composition, or content of proteasome regulators, PA28 and PA700. In contrast, the aged neural retina demonstrated a significant reduction in the chymotrypsin-like activity and decreased degradation of both casein and casein modified by 4-hydroxynonenal. This loss in function could not be explained by differences in subunit composition, content of PA28 and PA700, or reversible modification of cysteine residues. To begin investigating the molecular basis for the age-associated decrement in proteasome function, we modified the cysteine residues in proteasome from young rats with the sulfhydryl reactive chemical N-ethylmaleimide. We observed inhibition of the chymotrypsin-like activity and decreased degradation of casein that was comparable to that seen in aged retinas. Thus, chemical modification of cysteine provides an in vitro method that partially recapitulates aging proteasome. Further studies are required to confirm irreversible modification of functionally significant cysteine as a potential mechanism behind the age-related loss in proteasome function.

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Section: Mechanisms Of Chymotrypsin-like Inhibitionsupporting

confidence: 74%

Section: Mechanisms Of Chymotrypsin-like Inhibitionmentioning

confidence: 91%

Section: Inhibition Of Proteasome Activity With N-ethylmaleimidementioning

confidence: 99%

See 1 more Smart Citation

Age-dependent inhibition of proteasome chymotrypsin-like activity in the retina

Kapphahn

Bigelow

Ferrington

2007

Experimental Eye Research

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“…Proteins related to cell control were also found in our study, as two clones of a proteasome component, proteolytic complexes responsible for the degradation of many cellular proteins (Demasi et al, 2003) that play an important role in regulating the cell cycle and signalling, including apoptosis and the elimination of abnormal proteins generated by mutation and oxidative damage (Berlett & Stadtman, 1997;Bochtler et al, 1999;Coux et al, 1996;Demasi et al, 2003;Giulivi et al, 1994;Ullrich et al, 1999). Moreover, proteasomes are controlled by glutathione S-transferase and the related control of oxidation-reduction reactions and production of transcription factors (Demasi et al, 2003;Silva et al, 2008).…”

Section: R Peres Da Silva and Othersmentioning

confidence: 85%

Differential gene expression analysis of Paracoccidioides brasiliensis during keratinocyte infection

Silva

Matsumoto

Braz

et al. 2011

Journal of Medical Microbiology

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Paracoccidioides brasiliensis is the agent of paracoccidioidomycosis, one of the most important systemic fungal diseases in Latin America. This initiates in lung tissue and can subsequently disseminate to other tissues. Clinical manifestations range from localized forms to disseminated disease that can progress to lethality, probably depending on the relationships among the virulence of the fungus, the immune response and the ability to interact with the surface structures and invade epithelial cells and mononuclear cells of the host. It is generally regarded as a multifocal disease, with oral lesions as the prominent feature. The aim of this study was to evaluate P. brasiliensis yeast infection in normal oral keratinocytes (NOKs). The differential expression of mRNAs and proteins was also determined when the fungus was placed in contact with the cell in order to characterize differentially expressed genes and proteins during P. brasiliensis infection. After contact with NOKs, the fungus appeared to induce alterations in the cells, which showed cellular extensions and cavitations, probably resulting from changes in the actin cytoskeleton seen at 5 and 8 h after infection. Levels of protein expression were higher after reisolation of the fungus from infected NOK culture compared with culture of the fungus in medium. The analysis identified transcripts related to 19 proteins involved in different biological processes. Transcripts were found with multiple functions including induction of cytokines, protein metabolism, alternative carbon metabolism, zinc transport and the stress response during contact with NOKs. The proteins found suggested that the yeast was in a stress situation, as indicated by the presence of RDS1. Nevertheless, the yeast seemed to be proliferating and metabolically active, as shown by the presence of a proteasome, short-chain acetylator, glucosamine-6-phosphate isomerase and ADP/ATP carrier transcripts. Additionally, metabolic pathways may have been activated in order to eliminate toxic substances from the cell as a zinc transporter was detected, which is a potential target for the development of future drugs. INTRODUCTIONParacoccidioides brasiliensis is a thermodimorphic pathogenic fungus, the aetiological agent of paracoccidioidomycosis (PCM), an endemic disease geographically limited to Latin America and one of the most prevalent human deep systemic mycoses found in Brazil, Colombia and Venezuela (San-Blas et al., 2002). The transition from mycelium at 25 u C to yeast at 37 u C is essential for P. brasiliensis to establish the disease (Franco et al., 1997). P. brasiliensis may be inhaled and, once in the lungs, the fungus initiates a process of morphological transition into the pathogenic yeast form (San-Blas et al., 2002).PCM has a multiplicity of clinical presentations, from cutaneous to systemic forms, and can attack various tissues, especially the lungs (Benard & Franco, 2007). Oral mucosal lesions are commonly multiple, with a granular, mulberry-like surface and microulcerations, and ...

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“…In addition, it was shown that reversible S-thiolation of E1 and E2 enzymes regulates the ubiquitin-dependent proteolysis in response to altered redox environment (Obin et al, 1998). Furthermore, the 20S proteasome activity in S. cerevisiae was also reported to be inhibited by S-glutathionylation following H 2 O 2 treatment (Demasi et al, 2003). These observations suggest redox regulation of the proteasome degradation machinery could regulate cyclin D1 levels.…”

Section: Intracellular Redox State and Cell Cycle Proteinsmentioning

confidence: 97%

A redox cycle within the cell cycle: ring in the old with the new

2006

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In recent years, the intracellular oxidation-reduction (redox) state has gained increasing attention as a critical mediator of cell signaling, gene expression changes and proliferation. This review discusses the evidence for a redox cycle (i.e., fluctuation in the cellular redox state) regulating the cell cycle. The presence of redox-sensitive motifs (cysteine residues, metal co-factors in kinases and phosphatases) in several cell cycle regulatory proteins indicate periodic oscillations in intracellular redox state could play a central role in regulating progression from G 0 /G 1 to S to G 2 and M cell cycle phases. Fluctuations in the intracellular redox state during cell cycle progression could represent a fundamental mechanism linking oxidative metabolic processes to cell cycle regulatory processes. Proliferative disorders are central to a variety of human pathophysiological conditions thought to involve oxidative stress. Therefore, a more complete understanding of redox control of the cell cycle could provide a biochemical rationale for manipulating aberrant cell proliferation.

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20 S Proteasome from Saccharomyces cerevisiae Is Responsive to Redox Modifications and IsS-Glutathionylated

Cited by 115 publications

References 40 publications

Age-dependent inhibition of proteasome chymotrypsin-like activity in the retina

Age-dependent inhibition of proteasome chymotrypsin-like activity in the retina

Differential gene expression analysis of Paracoccidioides brasiliensis during keratinocyte infection

A redox cycle within the cell cycle: ring in the old with the new

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