Presenilins Regulate Neurotrypsin Gene Expression and Neurotrypsin-dependent Agrin Cleavage via Cyclic AMP Response Element-binding Protein (CREB) Modulation

Almenar-Queralt, Angels; Kim, Sonia N.; Benner, Chris; Herrera, Cheryl; Kang, David E.; García-Bassets, Ivan; Goldstein, Lawrence S.B.

doi:10.1074/jbc.m113.513705

Cited by 14 publications

(10 citation statements)

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“…The exact relationship between cAMP and Notch in endothelial cell differentiation remains unknown, but cAMP has been shown to modulate presenilin-1 (a component of γ-secretase) in neurons [72]. …”

Section: Ve-cadherin-dependent and Independent Signaling In Vmmentioning

confidence: 99%

Vasculogenic mimicry signaling revisited: focus on non-vascular VE-cadherin

et al. 2017

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Vasculogenic mimicry (VM) is a blood supply system independent of endothelial vessels in tumor cells from different origins. It reflects the plasticity of aggressive tumor cells that express vascular cell markers and line tumor vasculature. The presence of VM is associated with a high tumor grade, short survival, invasion and metastasis. Endothelial cells (ECs) express various members of the cadherin superfamily, in particular vascular endothelial (VE-) cadherin, which is the main adhesion receptor of endothelial adherent junctions. Aberrant extra-vascular expression of VE-cadherin has been observed in certain cancer types associated with VM. In this review we focus on non-endothelial VE-cadherin as a prominent factor involved in the acquisition of tubules-like structures by aggressive tumor cells and we summarize the specific signaling pathways, the association with trans-differentiation and stem-like phenotype and the therapeutic opportunities derived from the in-depth knowledge of the peculiarities of the biology of VE-cadherin and other key components of VM.

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Section: Ve-cadherin-dependent and Independent Signaling In Vmmentioning

confidence: 99%

Vasculogenic mimicry signaling revisited: focus on non-vascular VE-cadherin

et al. 2017

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“…For ChIP-seq, hiPSCs/hESCs seeded on γ-irradiated MEFs were grown to confluency, and mESCs were grown before reaching confluency. ChIPs were conducted as previously 72,73 . Briefly, cells were crosslinked for 45 minutes with 2 mM DSG (ProteoChem) diluted in 1xPBS buffer followed by 15 minutes treatment with 1% formaldehyde diluted in 1xPBS buffer (Sigma) for protein-based ChIPs.…”

Section: Chip-seq Analysismentioning

confidence: 99%

Chromatin establishes an immature version of neuronal protocadherin selection during the naive-to-primed conversion of pluripotent stem cells

et al. 2019

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The sequencing datasets generated in this study have been deposited in GEO under accession number GSE106872. COMPETING INTERESTS STATEMENT Martin Marsala is the scientific founder of Neurgain Technologies, Inc. and has an equity interest in the company. In addition, Martin Marsala serves as a consultant to Neurgain Technologies, Inc., and receives compensation for these services. The terms of this arrangement have been reviewed and approved by the University of California, San Diego in accordance with its conflict of interest policies.

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“…First, while Anderson et al [112] went to considerable lengths to control for penetration artifacts that might lead to inconsistent staining of agrin deposits, technical difficulties, whether reflecting issues of penetration or local proteolytic action on specific epitopes, can never be excluded definitively. For example, focal proteolysis of matrix constituents is a constant feature attending synaptogenesis in the amphibian culture system [14,115] and agrin is known to be subject to hydrolysis by several metalloproteinases [116,117], as well as by neurotrypsin, a serine proteinase [118,119]. More generally, in a context where staining is, in the words of Anderson et al, “erratic” [112], definitive conclusions will require a complete description that can account for the presence of agrin at some synapses and its absence in others.…”

Section: Synapse Formation: Two Mechanisms—agrin and Prepatterningmentioning

confidence: 99%

Nerve, Muscle, and Synaptogenesis

Swenarchuk

2019

Cells

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The vertebrate skeletal neuromuscular junction (NMJ) has long served as a model system for studying synapse structure, function, and development. Over the last several decades, a neuron-specific isoform of agrin, a heparan sulfate proteoglycan, has been identified as playing a central role in synapse formation at all vertebrate skeletal neuromuscular synapses. While agrin was initially postulated to be the inductive molecule that initiates synaptogenesis, this model has been modified in response to work showing that postsynaptic differentiation can develop in the absence of innervation, and that synapses can form in transgenic mice in which the agrin gene is ablated. In place of a unitary mechanism for neuromuscular synapse formation, studies in both mice and zebrafish have led to the proposal that two mechanisms mediate synaptogenesis, with some synapses being induced by nerve contact while others involve the incorporation of prepatterned postsynaptic structures. Moreover, the current model also proposes that agrin can serve two functions, to induce synaptogenesis and to stabilize new synapses, once these are formed. This review examines the evidence for these propositions, and concludes that it remains possible that a single molecular mechanism mediates synaptogenesis at all NMJs, and that agrin acts as a stabilizer, while its role as inducer is open to question. Moreover, if agrin does not act to initiate synaptogenesis, it follows that as yet uncharacterized molecular interactions are required to play this essential inductive role. Several alternatives to agrin for this function are suggested, including focal pericellular proteolysis and integrin signaling, but all require experimental validation.

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Presenilins Regulate Neurotrypsin Gene Expression and Neurotrypsin-dependent Agrin Cleavage via Cyclic AMP Response Element-binding Protein (CREB) Modulation

Cited by 14 publications

References 84 publications

Vasculogenic mimicry signaling revisited: focus on non-vascular VE-cadherin

Vasculogenic mimicry signaling revisited: focus on non-vascular VE-cadherin

Chromatin establishes an immature version of neuronal protocadherin selection during the naive-to-primed conversion of pluripotent stem cells

Nerve, Muscle, and Synaptogenesis

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