Soluble form of amyloid precursor protein regulates proliferation of progenitors in the adult subventricular zone

Caillé, Isabelle; Allinquant, Bernadette; Dupont, Edmond; Bouillot, Colette; Langer, Andreas; Müller, Ulrike; Prochiantz, Alain

doi:10.1242/dev.01103

Cited by 322 publications

(260 citation statements)

References 54 publications

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“…Soluble amyloid precursor protein-a increases SVZ cell proliferation, by stimulating the transit-amplifying type-C cells or the type-A SVZ neuroblasts (Caille et al, 2004). We found APP and TACE proteins were not co-localized within SVZ cells in vivo.…”

Section: Discussionmentioning

confidence: 63%

“…Tumor necrosis factor-a-converting enzyme is a protease required for the activation of a variety of growth factors, cytokines, and receptors, some of which have function in maintenance of SVZ neural progenitor cells (Blobel, 2005;Caille et al, 2004;Craig et al, 1996;Wu et al, 2000). Our findings suggest that TACE may be involved in the maintenance of SVZ expansion via an autocrine neurotrophic mechanism.…”

Section: Discussionmentioning

confidence: 70%

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Stroke-Induced Subventricular Zone Proliferation is Promoted by Tumor Necrosis Factor-α-Converting Enzyme Protease Activity

Katakowski¹,

Chen²,

Zhang³

et al. 2006

J Cereb Blood Flow Metab

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Cerebral stroke induces proliferation of subventricular zone (SVZ) neural progenitor cells in adult rodent brain. Tumor necrosis factor-a-converting enzyme (TACE) proteolysis sheds the nonamyloidogenic soluble ectodomain of the amyloid precursor protein (APP) and is a convertase for tumor necrosis factor-a (TNFa). The resulting soluble peptides of APP and TNFa are mitogenic for neural progenitor cells of the SVZ. Therefore, we hypothesized a role for TACE proteolysis in strokeinduced neurogenesis. Using laser-capture microdissection, we found TACE transcription was increased in SVZ cells of ischemic brain. Immunohistochemistry revealed TACE protein was upregulated in SVZ neuroblasts. Intraventricular infusion of tumor necrosis factor-a protease inhibitor-2 (TAPI-2) decreased bromodeoxyuridine incorporation in SVZ cells of rats subjected to middle cerebral artery occlusion. Furthermore, primary culture SVZ neurospheres from ischemic brain overexpress TACE and its substrates APP and TNF-a. These cells proliferated more rapidly, possessed increased TACE protease-dependent a-secretase activity, and released more soluble APP and TNFa compared with nonischemic control. In addition, TAPI-2 reduced SVZ neuroblast migration out of SVZ explants in vitro. These findings indicate TACE proteolysis as a promoter of stroke-induced SVZ progenitor cell neurogenesis, and suggest this protease activity may represent an attractive therapeutic target for stroke recovery.

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Section: Discussionmentioning

confidence: 63%

Section: Discussionmentioning

confidence: 70%

Stroke-Induced Subventricular Zone Proliferation is Promoted by Tumor Necrosis Factor-α-Converting Enzyme Protease Activity

Katakowski¹,

Chen²,

Zhang³

et al. 2006

J Cereb Blood Flow Metab

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“…This effect could be reversed by decreasing APP expression or blocking sAPP secretion. 45 In support of this observation, Lopez-Toledano and Shelanski reported increased proliferation and differentiation of neuronal precursor cells in the dentate gyrus of 3-month-old APP-overexpressing J20 mice. This effect was reverted in an age-dependent manner, coinciding with increasing Ab peptide levels.…”

Section: App Expression and Its Impact On Neurogenesismentioning

confidence: 81%

Altered neurogenesis in mouse models of Alzheimer disease

Wirths

2017

Neurogenesis

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Amyloid-b (Ab) peptides, as well as a variety of other protein fragments, are derived from proteolytical cleavage of the amyloid precursor protein (APP) and have been demonstrated to play a key role in the pathological changes underlying Alzheimer disease (AD). In AD mouse models, altered neurogenesis has been repeatedly reported to be associated with further AD-typical pathological hallmarks such as extracellular plaque deposition, behavioral deficits or neuroinflammation. While a toxic role of Ab in neurodegeneration and impaired neuronal progenitor proliferation is likely and well-accepted, recent findings also suggest an important influence of APP-derived proteolitical fragments like the APP intracellular domain (AICD), as well as of APP itself.

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“…8 This domain, in turn, regulates neuronal excitability 1 and enhances proliferation of progenitor cells in the subventricular zone. 9 Not only is the intracellular domain of APP of functional importance, but the proteolytic fragments derived from the extracellular domain are also of interest. APP is cleaved by secretases, resulting in several fragments, including the Ab-peptide in Alzheimer's disease.…”

Section: Introductionmentioning

confidence: 99%

Amyloid precursor protein and amyloid β-peptide bind to ATP synthase and regulate its activity at the surface of neural cells

et al. 2007

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Amyloid precursor protein (APP) and amyloid b-peptide (Ab) have been implicated in a variety of physiological and pathological processes underlying nervous system functions. APP shares many features with adhesion molecules in that it is involved in neurite outgrowth, neuronal survival and synaptic plasticity. It is, thus, of interest to identify binding partners of APP that influence its functions. Using biochemical cross-linking techniques we have identified ATP synthase subunit a as a binding partner of the extracellular domain of APP and Ab. APP and ATP synthase colocalize at the cell surface of cultured hippocampal neurons and astrocytes. ATP synthase subunit a reaches the cell surface via the secretory pathway and is N-glycosylated during this process. Transfection of APP-deficient neuroblastoma cells with APP results in increased surface localization of ATP synthase subunit a. The extracellular domain of APP and Ab partially inhibit the extracellular generation of ATP by the ATP synthase complex. Interestingly, the binding sequence of APP and Ab is similar in structure to the ATP synthase-binding sequence of the inhibitor of F1 (IF 1 ), a naturally occurring inhibitor of the ATP synthase complex in mitochondria. In hippocampal slices, Ab and IF 1 similarly impair both short-and long-term potentiation via a mechanism that could be suppressed by blockade of GABAergic transmission. These observations indicate that APP and Ab regulate extracellular ATP levels in the brain, thus suggesting a novel mechanism in Ab-mediated Alzheimer's disease pathology.

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Soluble form of amyloid precursor protein regulates proliferation of progenitors in the adult subventricular zone

Cited by 322 publications

References 54 publications

Stroke-Induced Subventricular Zone Proliferation is Promoted by Tumor Necrosis Factor-α-Converting Enzyme Protease Activity

Stroke-Induced Subventricular Zone Proliferation is Promoted by Tumor Necrosis Factor-α-Converting Enzyme Protease Activity

Altered neurogenesis in mouse models of Alzheimer disease

Amyloid precursor protein and amyloid β-peptide bind to ATP synthase and regulate its activity at the surface of neural cells

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