Possible roles of amyloid intracellular domain of amyloid precursor protein

Chang, Keun-A; Suh, Yoo‐Hun

doi:10.3858/bmbrep.2010.43.10.656

Cited by 6 publications

(10 citation statements)

References 88 publications

(105 reference statements)

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“…Thus, members of the JIP family (c-jun-N-terminal kinase interacting protein, JIP1b and JIP2) activate AICD-mediated signaling but interestingly, do not modulate transcription associated with ICDs of other members of the bAPP family (Scheinfeld et al 2003). Briefly, members of the Shc family (ShcA and ShcB), mammalian disabled (mDab1), Numb, Abl, and Grb2 also interact with the YENPTY domain of AICD in both phosphorylation-dependent and -independent mechanism (Raychaudhuri and Mukhopadhyay 2007;Müller et al 2008;Chang and Suh 2010).…”

Section: Regulation Of Aicd Production and Functionmentioning

confidence: 99%

“…AICD function: focus on the control of cell death and neprilysin-mediated Ab degradation AICD has been implicated in various cellular functions that have been reviewed recently (Müller et al 2008;Chang and Suh 2010). Briefly, AICD modulates the intracellular homeostasis of calcium and ATP (Hamid et al 2007) and can control neuronal networks (Vogt et al 2011).…”

Section: Aicd As a Transcription Factor: No Longer Controversialmentioning

confidence: 99%

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The physiology of the β‐amyloid precursor protein intracellular domain AICD

Pardossi‐Piquard

Checler

2011

Journal of Neurochemistry

139

136

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The amyloid-b precursor protein (bAPP) undergoes several cleavages by enzymatic activities called secretases. Numerous studies aimed at studying the biogenesis and catabolic fate of Ab peptides, the proteinaceous component of the senile plaques that accumulate in Alzheimer's disease-affected brains. Relatively recently, another secretase-mediated b-APP-derived catabolite called APP IntraCellular Domain (AICD) entered the game. Whether AICD corresponded to a biologically inert by-pass product of bAPP processing or whether it could harbor its own function remained questionable. In this study, we review the mechanisms by which AICD is generated and how its production is regulated. Furthermore, we discuss the degradation mechanism underlying its rapid catabolic fate. Finally, we review putative AICD-related functions and more particularly, the numerous studies indicating that AICD could translocate to the nucleus and control at a transcriptional level, the expression of a series of proteins involved in various functions including the control of cell death and Ab degradation.

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Section: Regulation Of Aicd Production and Functionmentioning

confidence: 99%

Section: Aicd As a Transcription Factor: No Longer Controversialmentioning

confidence: 99%

The physiology of the β‐amyloid precursor protein intracellular domain AICD

Pardossi‐Piquard

Checler

2011

Journal of Neurochemistry

139

136

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“…It is important to note that beside Aβ, an increasing level of AICD peptide could also mediate several processes in APP/PS1 mice. Although AICD can be generated by both α-γ and β-γ-secretase cleavages, its exact role remains controversial [73]. The AICD-mediated nuclear signaling occurs predominantly through the amyloidogenic processing pathway [74].…”

Section: Discussionmentioning

confidence: 99%

Mitochondrial Proteome Changes Correlating with β-Amyloid Accumulation

et al. 2016

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Alzheimer's disease (AD) is a multifactorial disease of wide clinical heterogenity. Overproduction of amyloid precursor protein (APP) and accumulation of β-amyloid (Aβ) and tau proteins are important hallmarks of AD. The identification of early pathomechanisms of AD is critically important for discovery of early diagnosis markers. Decreased brain metabolism is one of the earliest clinical symptoms of AD that indicate mitochondrial dysfunction in the brain. We performed the first comprehensive study integrating synaptic and non-synaptic mitochondrial proteome analysis (two-dimensional differential gel electrophoresis (2D-DIGE) and mass spectrometry) in correlation with Aβ progression in APP/PS1 mice (3, 6, and 9 months of age). We identified changes of 60 mitochondrial proteins that reflect the progressive effect of APP overproduction and Aβ accumulation on mitochondrial processes. Most of the significantly affected proteins play role in the mitochondrial electron transport chain, citric acid cycle, oxidative stress, or apoptosis. Altered expression levels of Htra2 and Ethe1, which showed parallel changes in different age groups, were confirmed also by Western blot. The common regulator bioinformatical analysis suggests the regulatory role of tumor necrosis factor (TNF) in Aβ-mediated mitochondrial protein changes. Our results are in accordance with the previous postmortem human brain proteomic studies in AD in the case of many proteins. Our results could open a new path of research aiming early mitochondrial molecular mechanisms of Aβ accumulation as a prodromal stage of human AD.

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“…The other secretome proteins investigated in our selected panel of candidates have also been shown to have important biological functions relating to cancer . APP is known for its role in the development of Alzheimer's disease, yet recent studies have shown that the proteolytic cleavage of APP is associated with growth factors and NF‐κB pathway activation, and alteration of calcium signaling and cytoskeletal dynamics, all of which suggest a role for APP in cancer development . Overexpression of APP has been reported in pancreatic, prostate, colon, and oral squamous cell carcinoma tissues .…”

Section: Discussionmentioning

confidence: 99%

Secretome proteins as candidate biomarkers for aggressive thyroid carcinomas

et al. 2013

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Using proteomics in tandem with bioinformatics, the secretomes of nonaggressive and aggressive thyroid carcinoma (TC) cell lines were analyzed to detect potential biomarkers for tumor aggressiveness. A panel of nine proteins, activated leukocyte cell adhesion molecule (ALCAM/CD166), tyrosine-protein kinase receptor (AXL), amyloid beta A4 protein, amyloid-like protein 2, heterogeneous nuclear ribonucleoprotein K, phosphoglycerate kinase 1, pyruvate kinase isozyme M2, phosphatase 2A inhibitor (SET), and protein kinase C inhibitor protein 1 (14-3-3 zeta) was chosen to confirm their expression in TC patients' sera and tissues. Increased presurgical circulating levels of ALCAM were associated with aggressive tumors (p = 0.04) and presence of lymph node metastasis (p = 0.018). Increased serum AXL levels were associated with extrathyroidal extension (p = 0.027). Furthermore, differential expression of amyloid beta A4 protein, AXL, heterogeneous nuclear ribonucleoprotein K, phosphoglycerate kinase 1, pyruvate kinase muscle isozyme M2, and SET was observed in TC tissues compared to benign nodules. Decreased nuclear expression of AXL can detect malignancy with 90% specificity and 100% sensitivity (AUC = 0.995, p < 0.001). In conclusion, some of these proteins show potential for future development as serum and/or tissue-based biomarkers for TC and warrant further investigation in a large cohort of patients.

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Possible roles of amyloid intracellular domain of amyloid precursor protein

Cited by 6 publications

References 88 publications

The physiology of the β‐amyloid precursor protein intracellular domain AICD

The physiology of the β‐amyloid precursor protein intracellular domain AICD

Mitochondrial Proteome Changes Correlating with β-Amyloid Accumulation

Secretome proteins as candidate biomarkers for aggressive thyroid carcinomas

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