Neurochemical enzyme changes in Alzheimer's and Pick's disease

Meier‐Ruge, W.; Iwangoff, P.; K, Reichlmeier

doi:10.1016/0167-4943(84)90007-4

Cited by 146 publications

(66 citation statements)

References 11 publications

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“…This glycolytic enzymes demonstrates increased oxidation in AD and models of AD (50,74,77). Lowered enzymatic activity of enolase has been previously established in the brain of subjects with MCI (76) and subjects with AD (271,363). Carbonylation of this protein supports the hypothesis of altered energy metabolism as a common theme in neurodegenerative disease.…”

Section: Identification Of Carbonylated Proteins In Brainsupporting

confidence: 57%

“…As just noted, ATP is essential in maintaining ATPases, ion-motive pumps, and potential gradients. In the AD brain, TPI is oxidatively modified as shown by our group in late-stage AD (363), but there is no significant reduction in its activity in AD (271).…”

Section: Identification Of Carbonylated Proteins In Brainmentioning

confidence: 99%

“…These results support the notion that energy metabolism is a key feature in the progression of AD pathogenesis. Since glycolysis is the main source of ATP production in brain, impairment of glycolysis may lead to shortage of ATP in brains, thus to cellular dysfunction (74,271). Moreover, decreased ATP shortage can also induce hypothermia, causing abnormal tau phosphorylation through differential inhibition of kinases and phosphatases (311).…”

Section: Identification Of Carbonylated Proteins In Brainmentioning

confidence: 99%

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Redox Proteomics in Selected Neurodegenerative Disorders: From Its Infancy to Future Applications

Butterfield

Perluigi

Reed

et al. 2012

Antioxidants & Redox Signaling

157

142

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Several studies demonstrated that oxidative damage is a characteristic feature of many neurodegenerative diseases. The accumulation of oxidatively modified proteins may disrupt cellular functions by affecting protein expression, protein turnover, cell signaling, and induction of apoptosis and necrosis, suggesting that protein oxidation could have both physiological and pathological significance. For nearly two decades, our laboratory focused particular attention on studying oxidative damage of proteins and how their chemical modifications induced by reactive oxygen species/reactive nitrogen species correlate with pathology, biochemical alterations, and clinical presentations of Alzheimer's disease. This comprehensive article outlines basic knowledge of oxidative modification of proteins and lipids, followed by the principles of redox proteomics analysis, which also involve recent advances of mass spectrometry technology, and its application to selected age-related neurodegenerative diseases. Redox proteomics results obtained in different diseases and animal models thereof may provide new insights into the main mechanisms involved in the pathogenesis and progression of oxidativestress-related neurodegenerative disorders. Redox proteomics can be considered a multifaceted approach that has the potential to provide insights into the molecular mechanisms of a disease, to find disease markers, as well as to identify potential targets for drug therapy. Considering the importance of a better understanding of the cause/effect of protein dysfunction in the pathogenesis and progression of neurodegenerative disorders, this article provides an overview of the intrinsic power of the redox proteomics approach together with the most significant results obtained by our laboratory and others during almost 10 years of research on neurodegenerative disorders since we initiated the field of redox proteomics. Antioxid. Redox Signal. 17, 1610-1655.

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Section: Identification Of Carbonylated Proteins In Brainsupporting

confidence: 57%

Section: Identification Of Carbonylated Proteins In Brainmentioning

confidence: 99%

Section: Identification Of Carbonylated Proteins In Brainmentioning

confidence: 99%

See 1 more Smart Citation

Redox Proteomics in Selected Neurodegenerative Disorders: From Its Infancy to Future Applications

Butterfield

Perluigi

Reed

et al. 2012

Antioxidants & Redox Signaling

157

142

View full text Add to dashboard Cite

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“…Peroxiredoxins 1 and 2 protect against huntingtin neurotoxicity (Pitts et al ., 2012) and dopaminergic neurodegeneration (Hu et al ., 2011). Phosphoglycerate mutase activity in brain decreases with aging and especially with AD (Meier‐Ruge et al ., 1984), perhaps explained by its AD‐specific accumulation in aggregates. Secernin‐1 was identified as an early marker of neurodegeneration in a transgenic mouse overexpressing human tau (Chang et al ., 2013b).…”

Section: Discussionmentioning

confidence: 99%

Proteins that mediate protein aggregation and cytotoxicity distinguish Alzheimer's hippocampus from normal controls

et al. 2016

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SummaryNeurodegenerative diseases are distinguished by characteristic protein aggregates initiated by disease‐specific ‘seed’ proteins; however, roles of other co‐aggregated proteins remain largely unexplored. Compact hippocampal aggregates were purified from Alzheimer's and control‐subject pools using magnetic‐bead immunoaffinity pulldowns. Their components were fractionated by electrophoretic mobility and analyzed by high‐resolution proteomics. Although total detergent‐insoluble aggregates from Alzheimer's and controls had similar protein content, within the fractions isolated by tau or Aβ1–42 pulldown, the protein constituents of Alzheimer‐derived aggregates were more abundant, diverse, and post‐translationally modified than those from controls. Tau‐ and Aβ‐containing aggregates were distinguished by multiple components, and yet shared >90% of their protein constituents, implying similar accretion mechanisms. Alzheimer‐specific protein enrichment in tau‐containing aggregates was corroborated for individuals by three analyses. Five proteins inferred to co‐aggregate with tau were confirmed by precise in situ methods, including proximity ligation amplification that requires co‐localization within 40 nm. Nematode orthologs of 21 proteins, which showed Alzheimer‐specific enrichment in tau‐containing aggregates, were assessed for aggregation‐promoting roles in C. elegans by RNA‐interference ‘knockdown’. Fifteen knockdowns (71%) rescued paralysis of worms expressing muscle Aβ, and 12 (57%) rescued chemotaxis disrupted by neuronal Aβ expression. Proteins identified in compact human aggregates, bound by antibody to total tau, were thus shown to play causal roles in aggregation based on nematode models triggered by Aβ1–42. These observations imply shared mechanisms driving both types of aggregation, and/or aggregate‐mediated cross‐talk between tau and Aβ. Knowledge of protein components that promote protein accrual in diverse aggregate types implicates common mechanisms and identifies novel targets for drug intervention.

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“…6 Moreover, in the neurodegenerative disorder of memory and cognitive function, Alzheimer's disease, the level of CA is significantly diminished. 7 A similar decrease in the expression level of CA was observed in the brain of older rats relative to young animals, 8 being associated with a reduced resistance to dehydration, alteration in choroidal control of brain homeostasis, and reduced cerebrospinal fluid production. Therefore, activation of the CAs present in the brain represents a promising and rather unexplored approach to increase brain activity, especially memory and learning, with significant potential benefits in older individuals or in patients affected by Alzheimer's disease and other forms of dementia.…”

mentioning

confidence: 60%

Ethylene bis-imidazoles are highly potent and selective activators for isozymes VA and VII of carbonic anhydrase, with a potential nootropic effect

et al. 2014

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Neurochemical enzyme changes in Alzheimer's and Pick's disease

Cited by 146 publications

References 11 publications

Redox Proteomics in Selected Neurodegenerative Disorders: From Its Infancy to Future Applications

Redox Proteomics in Selected Neurodegenerative Disorders: From Its Infancy to Future Applications

Proteins that mediate protein aggregation and cytotoxicity distinguish Alzheimer's hippocampus from normal controls

Ethylene bis-imidazoles are highly potent and selective activators for isozymes VA and VII of carbonic anhydrase, with a potential nootropic effect

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