We are analyzing https://link.springer.com/article/10.1007/pl00000660.

Title:
4-Hydroxynonenal-modified amyloid-β peptide inhibits the proteasome: possible importance in Alzheimer’s disease* | Cellular and Molecular Life Sciences
Description:
The amyloid β-peptide (Aβ) is a 4-kDa species derived from the amyloid precursor protein, which accumulates in the brains of patients with Alzheimer’s disease. Although we lack full understanding of the etiology and pathogenesis of selective neuron death, considerable data do imply roles for both the toxic Aβ and increased oxidative stress. Another significant observation is the accumulation of abnormal, ubiquitin-conjugated proteins in affected neurons, suggesting dysfunction of the proteasome proteolytic system in these cells. Recent reports have indicated that Aβ can bind and inhibit the proteasome, the major cytoslic protease for degrading damaged and ubiquitin-conjugated proteins. Earlier results from our laboratory showed that moderately oxidized proteins are preferentially recognized and degraded by the proteasome; however, severely oxidized proteins cannot be easily degraded and, instead, inhibit the proteasome. We hypothesized that oxidatively modified Aβ might have a stronger (or weaker) inhibitory effect on the proteasome than does native Aβ. We therefore also investigated the proteasome inhibitory action of Aβ 1–40 (a peptide comprising the first 40 residues of Aβ) modified by the intracellular oxidant hydrogen peroxide, and by the lipid peroxidation product 4-hydroxynonenal (HNE). H2O2 modification of Aβ 1–40 generates a progressively poorer inhibitor of the purified human 20S proteasome. In contrast, HNE modification of Aβ 1–40 generates a progressively more selective and efficient inhibitor of the degradation of fluorogenic peptides and oxidized protein substrates by human 20S proteasome. This interaction may contribute to certain pathological manifestations of Alzheimer’s disease
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Keywords {🔍}

proteasome, article, alzheimers, disease, proteins, access, privacy, cookies, content, data, information, publish, search, molecular, amyloidβ, peptide, protein, log, journal, research, life, cmls, shringarpure, grune, sitte, amyloid, oxidized, human, open, discover, springer, optional, personal, parties, policy, find, track, cellular, sciences, hydroxynonenalmodified, inhibits, importance, october, cite, davies, explore, full, selective, oxidative, stress,

Topics {✒️}

month download article/chapter amyloid β-peptide amyloid-β proteoforms amyloid beta peptide ubiquitin-conjugated proteins moderately oxidized proteins severely oxidized proteins 4-kda species derived privacy choices/manage cookies human 20s proteasome full article pdf related subjects amyloid precursor protein oxidatively modified aβ european economic area scope submit manuscript lack full understanding major cytoslic protease conditions privacy policy oxidized protein substrates proteasome proteolytic system proteasome inhibitory action accepting optional cookies article cellular selective neuron death increased oxidative stress life sci molecular biology october 2000 volume 57 progressively poorer inhibitor journal finder publish rapidly progressive alzheimer affected neurons peptide comprising article log check access instant access article cite disease published article shringarpure privacy policy cmls personal data 4-hydroxynonenal books a modified optional cookies manage preferences davies clinics oxidative stress

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         headline:4-Hydroxynonenal-modified amyloid-β peptide inhibits the proteasome: possible importance in Alzheimer’s disease*
         description: The amyloid β-peptide (Aβ) is a 4-kDa species derived from the amyloid precursor protein, which accumulates in the brains of patients with Alzheimer’s disease. Although we lack full understanding of the etiology and pathogenesis of selective neuron death, considerable data do imply roles for both the toxic Aβ and increased oxidative stress. Another significant observation is the accumulation of abnormal, ubiquitin-conjugated proteins in affected neurons, suggesting dysfunction of the proteasome proteolytic system in these cells. Recent reports have indicated that Aβ can bind and inhibit the proteasome, the major cytoslic protease for degrading damaged and ubiquitin-conjugated proteins. Earlier results from our laboratory showed that moderately oxidized proteins are preferentially recognized and degraded by the proteasome; however, severely oxidized proteins cannot be easily degraded and, instead, inhibit the proteasome. We hypothesized that oxidatively modified Aβ might have a stronger (or weaker) inhibitory effect on the proteasome than does native Aβ. We therefore also investigated the proteasome inhibitory action of Aβ 1–40 (a peptide comprising the first 40 residues of Aβ) modified by the intracellular oxidant hydrogen peroxide, and by the lipid peroxidation product 4-hydroxynonenal (HNE). H2O2 modification of Aβ 1–40 generates a progressively poorer inhibitor of the purified human 20S proteasome. In contrast, HNE modification of Aβ 1–40 generates a progressively more selective and efficient inhibitor of the degradation of fluorogenic peptides and oxidized protein substrates by human 20S proteasome. This interaction may contribute to certain pathological manifestations of Alzheimer’s disease
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      headline:4-Hydroxynonenal-modified amyloid-β peptide inhibits the proteasome: possible importance in Alzheimer’s disease*
      description: The amyloid β-peptide (Aβ) is a 4-kDa species derived from the amyloid precursor protein, which accumulates in the brains of patients with Alzheimer’s disease. Although we lack full understanding of the etiology and pathogenesis of selective neuron death, considerable data do imply roles for both the toxic Aβ and increased oxidative stress. Another significant observation is the accumulation of abnormal, ubiquitin-conjugated proteins in affected neurons, suggesting dysfunction of the proteasome proteolytic system in these cells. Recent reports have indicated that Aβ can bind and inhibit the proteasome, the major cytoslic protease for degrading damaged and ubiquitin-conjugated proteins. Earlier results from our laboratory showed that moderately oxidized proteins are preferentially recognized and degraded by the proteasome; however, severely oxidized proteins cannot be easily degraded and, instead, inhibit the proteasome. We hypothesized that oxidatively modified Aβ might have a stronger (or weaker) inhibitory effect on the proteasome than does native Aβ. We therefore also investigated the proteasome inhibitory action of Aβ 1–40 (a peptide comprising the first 40 residues of Aβ) modified by the intracellular oxidant hydrogen peroxide, and by the lipid peroxidation product 4-hydroxynonenal (HNE). H2O2 modification of Aβ 1–40 generates a progressively poorer inhibitor of the purified human 20S proteasome. In contrast, HNE modification of Aβ 1–40 generates a progressively more selective and efficient inhibitor of the degradation of fluorogenic peptides and oxidized protein substrates by human 20S proteasome. This interaction may contribute to certain pathological manifestations of Alzheimer’s disease
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      dateModified:
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         Cell Biology
         Biomedicine
         general
         Life Sciences
         Biochemistry
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