Decreased serum angiogenin level in Alzheimer's disease

Kim, Yong Nam; Kim, Do Hoon

doi:10.1016/j.pnpbp.2012.02.010

Cited by 41 publications

(28 citation statements)

References 21 publications

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“…Additionally, an in vitro study showed that VEGF significantly prevented Aβ-induced endothelial apoptosis, and in an AD mouse model it restored the impaired memory behavior by improving vascular survival [88]. Furthermore, low serum levels of angionin, an angiogenesis promoter, were reported in AD patients, and this was found to be related to cognitive decline [89]. The production of thrombin by endothelial cells in AD seems to be another proteomical dysfunction of these cells.…”

Section: Impairment Of Cerebral Microcirculation In Alzheimer's Diseasementioning

confidence: 99%

Dissecting the Contribution of Vascular Alterations and Aging to Alzheimer’s Disease

2015

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Alzheimer's disease (AD) is a neurodegenerative disease characterized by cognitive decline that afflicts as many as 45 % of individuals who survive past the age of 85. AD has been associated with neurovascular dysfunction and brain accumulation of amyloid-β peptide, as well as tau phosphorylation and neurodegeneration, but the pathogenesis of the disease is still somewhat unclear. According to the amyloid cascade hypothesis of AD, accumulation of amyloid-β peptide (Aβ) aggregates initiates a sequence of events leading to neuronal injury and loss, and dementia. Alternatively, the vascular hypothesis of AD incorporates the vascular contribution to the disease, stating that a primary insult to brain microcirculation (e.g., stroke) not only contributes to amyloidopathy but initiates a non-amyloidogenic pathway of vascular-mediated neuronal dysfunction and injury, which involves blood-brain barrier compromise, with increased permeability of blood vessels, leakage of blood-borne components into the brain, and, consequently, neurotoxicity. Vascular dysfunction also includes a diminished brain capillary flow, causing multiple focal ischemic or hypoxic microinjuries, diminished amyloid-β clearance, and formation of neurotoxic oligomers, which lead to neuronal dysfunction. Here we present and discuss relevant findings on the contribution of vascular alterations during aging to AD, with the hope that a better understanding of the players in the "orchestra" of neurodegeneration will be useful in developing therapies to modulate the "symphony".

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Section: Impairment Of Cerebral Microcirculation In Alzheimer's Diseasementioning

confidence: 99%

Dissecting the Contribution of Vascular Alterations and Aging to Alzheimer’s Disease

2015

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“…For instance, the protein exists at high concentrations in motoneurons, where it is involved in the onset of amyotrophic lateral sclerosis (ALS) [24,25]. In addition, Ang is down-regulated in patients affected by Alzheimer’s diseases [26] and in α-synuclein mouse model of Parkinson’s disease [27]. …”

Section: Introductionmentioning

confidence: 99%

Coordination Environment of Cu(II) Ions Bound to N-Terminal Peptide Fragments of Angiogenin Protein

Magrı̀

Munzone

Peana

et al. 2016

IJMS

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Angiogenin (Ang) is a potent angiogenic factor, strongly overexpressed in patients affected by different types of cancers. The specific Ang cellular receptors have not been identified, but it is known that Ang–actin interaction induces changes both in the cell cytoskeleton and in the extracellular matrix. Most in vitro studies use the recombinant form (r-Ang) instead of the form that is normally present in vivo (“wild-type”, wt-Ang). The first residue of r-Ang is a methionine, with a free amino group, whereas wt-Ang has a glutamic acid, whose amino group spontaneously cyclizes in the pyro-glutamate form. The Ang biological activity is influenced by copper ions. To elucidate the role of such a free amino group on the protein–copper binding, we scrutinized the copper(II) complexes with the peptide fragments Ang(1–17) and AcAng(1–17), which encompass the sequence 1–17 of angiogenin (QDNSRYTHFLTQHYDAK-NH2), with free amino and acetylated N-terminus, respectively. Potentiometric, ultraviolet-visible (UV-vis), nuclear magnetic resonance (NMR) and circular dichroism (CD) studies demonstrate that the two peptides show a different metal coordination environment. Confocal microscopy imaging of neuroblastoma cells with the actin staining supports the spectroscopic results, with the finding of different responses in the cytoskeleton organization upon the interaction, in the presence or not of copper ions, with the free amino and the acetylated N-terminus peptides.

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“…In contrast to its upregulation in various cancers, ANG is downregulated in amyotrophic lateral sclerosis (ALS) (McLaughlin et al, 2010), Parkinson's disease (PD) (Steidinger et al, 2011) and Alzheimer's disease (Kim and Kim, 2012). More importantly, loss-of-function mutations have been found in patients with ALS and PD (Conforti et al, 2008;Gellera et al, 2008;Greenway et al, 2006;Paubel et al, 2008;van Es et al, 2009;Wu et al, 2007).…”

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confidence: 99%

Ribonuclease/angiogenin inhibitor 1 regulates stress-induced subcellular localization of angiogenin and controls its growth and survival activities

Pizzo

Sarcinelli

Sheng

et al. 2013

Journal of Cell Science

102

112

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SummaryAngiogenin (ANG) promotes cell growth and survival. Under growth conditions, ANG undergoes nuclear translocation and accumulates in the nucleolus where it stimulates rRNA transcription. When cells are stressed, ANG mediates the production of tRNA-derived stressinduced small RNA (tiRNA), which reprograms protein translation into a survival mechanism. The ribonucleolytic activity of ANG is essential for both processes but how this activity is regulated is unknown. We report here that ribonuclease/angiogenin inhibitor 1 (RNH1) controls both the localization and activity of ANG. Under growth conditions, ANG is located in the nucleus and is not associated with RNH1 so that the ribonucleolytic activity is retained to ensure rRNA transcription. Cytoplasmic ANG is associated with and inhibited by RNH1 so that random cleavage of cellular RNA is prevented. Under stress conditions, ANG is localized to the cytoplasm and is concentrated in stress granules where it is not associated with RNH1 and thus remains enzymatically active for tiRNA production. By contrast, nuclear ANG is associated with RNH1 in stressed cells to ensure that the enzymatic activity is inhibited and no unnecessary rRNA is produced to save anabolic energy. Knockdown of RNH1 abolished stress-induced relocalization of ANG and decreased cell growth and survival.

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Decreased serum angiogenin level in Alzheimer's disease

Cited by 41 publications

References 21 publications

Dissecting the Contribution of Vascular Alterations and Aging to Alzheimer’s Disease

Dissecting the Contribution of Vascular Alterations and Aging to Alzheimer’s Disease

Coordination Environment of Cu(II) Ions Bound to N-Terminal Peptide Fragments of Angiogenin Protein

Ribonuclease/angiogenin inhibitor 1 regulates stress-induced subcellular localization of angiogenin and controls its growth and survival activities

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