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the expression of APLP2 might correlate with tumor development and be a prognostic factor for patients with glioblastoma
These findings suggest that the identified APLP2, RRM2, and PRC1 signature could be useful for distinguishing between benign (follicular adenoma) and malignant (follicular carcionma and follicular variant of papillary carcinoma) tumors of the thyroid follicular epithelium.
This paper demonstrates an important role for APLP2 in refractive development in mice and humans, suggesting a high level of evolutionary conservation of the signaling pathways underlying refractive eye development.
Data show that amyloid precursor-like protein 2 (APLP2) expression is elevated in pancreatic cancer metastases.
We conclude that PCSK9 enhances the degradation of the LDLR independently of either APLP2 or sortilin both ex vivo and in mice.
APLP1 and APLP2, behave similarly to APP in that they both associate with assembled NMDA receptors in the endoplasmic reticulum
our discoveries establish a role for APLP2 in the growth of pancreatic cancer cells and show that inhibitors preventing APLP2 cleavage reduce the viability of pancreatic cancer cells.
amyloid precursor protein-like protein-2, but not amyloid precursor protein, is involved in mediating postendocytic delivery of PCSK9 to lysosomes and is therefore important for PCSK9 function
Aberrant enhancement of YWK-II/APLP2 by nuclear export of Bat3 may play a role in cancer development by inhibiting cell apoptosis.
APP and its mammalian homologs, amyloid precursor-like proteins APLP1 and APLP2, participate under physiological conditions via trans-cellular dimerization in synaptogenesis.
APLP-2 (and APLP1) are capable of activating gene transcription via binding to Mint3.
Regulation of major histocompatibility complex class I molecule expression on cancer cells by amyloid precursor-like protein 2.
proteolytic cleavage sites of the amyloid precursor-like protein 2 by the proteases ADAM10, BACE1 and gamma-secretase
The interaction between APLP2 and ataxin-7 and proteolytic processing of APLP2 may contribute to the pathogenesis of spinocerebellar ataxia type 7.
APLP1 and APLP2 are processed by the gamma-secretase in a Presenilin 1-dependent manner and the extreme carboxyl-terminal fragments produced by this processing (APP-like Intracellular Domain are able to enhance Fe65-dependent gene activation
crystals of extracellular fragment X3 of a human sperm membrane protein YWK-II/APPH have been grow by the vapour-diffusion method [YWK-II PROTEIN]
Sustained levels of APP and the elevated levels of APLP2, in spite of the reduced mRNA expression, are due to altered proteolytic processing of these proteins.
APLP1 and APLP2 and APP are processed similarly to act via the same nuclear target and are regulated by BACE 1 in neurons
APLP-1 and APLP-2 are processed by alpha- and gamma-secretase-like cleavages, and their intracellular domains can be released by cleavage at epsilon-sites. APLP-2 processing appears to be the most elaborate and to involve alternative cleavage sites.
The APLP2 gene has no CAGA box, but it does have a GAGA sequence in a location similar to that of the CAGA box in the APP gene.
These data identified APP and APLP2 as modulators of normal myelination and demyelination/remyelination conditions.
APLP2 couples retina development and synaptic genes and present the first evidence that APLP2 expression may be linked to synaptic disease.
These data support the notion that APP and APLP2 facilitate transmitter release, likely through the interaction with the neurotransmitter release machinery.
Study provides compelling evidence for an essential role of both APP and APLP2 for neuronal and synaptic morphology as well as hippocampal function and suggest an acute and specific function of endogenous APPsalpha to facilitate synaptic plasticity
The study investigates the subcellular distribution patterns of the metal ions Cu, Zn, Fe, and Ca in individual neurons derived from APP and APLP2 knockout mice brains to further define their role in metal homeostasis.
This study further highlights the distinct and essential role of APLP2 at NMJ synapses that cannot be compensated by APP.
Amyloid precursor protein (APP)/APP-like protein 2 (APLP2) expression is required to initiate endosome-nucleus-autophagosome
The study investigated copper, iron, zinc and manganese levels in APP and APLP-2 single knockout mice as well as homozygous:hemizygous knockout mice at 3, 12 and 18 plus months of age.
Data reveal that APLP2 is specifically required for proper cell cycle exit of neuronal progenitors, and thus has a distinct role in priming cortical progenitors for neuronal differentiation.
APLP2 and the intracellular domain of APP are not essential for coherent activity patterns in the hippocampus, but have subtle effects on synaptic plasticity and fine-tuning of network oscillations.
Gain and loss of function experiments demonstrate that miR-153 suppresses expression of amyloid precursor protein (APP) and APLP2.
These studies highlight the so far underestimated functional importance of APLP2 for CNS physiology.
[review] Studies of protein expression in knock-out mice demonstrate that APP and APLP2 do indeed play an important role in synaptic plasticity.
APLP2 appears not to be essential for maintenance of dendritic structure, spine density, or synaptic function
Collectively, these data show that APLP2 and APP are synergistically required to mediate neuromuscular transmission, spatial learning and synaptic plasticity.
Data show there were no differences in expression were detectable between wt and floxed alleles.
role in inducing neuronal death is mediated by impairment of the neuroprotective calcium/calmodulin protein kinase IV-dependent signaling pathway
The levels of APLP2 proteolytic products were decreased in BACE KO mice, but increased in BACE transgenic mice. Overexpression of BACE in cultured cells led to increased APLP2 processing.
these results indicate the Appa-RFP and Aplp2 fusion proteins are likely secreted from the central nervous system and accumulate in the embryonic veins independent of blood flow.
This gene encodes amyloid precursor- like protein 2 (APLP2), which is a member of the APP (amyloid precursor protein) family including APP, APLP1 and APLP2. This protein is ubiquitously expressed. It contains heparin-, copper- and zinc- binding domains at the N-terminus, BPTI/Kunitz inhibitor and E2 domains in the middle region, and transmembrane and intracellular domains at the C-terminus. This protein interacts with major histocompatibility complex (MHC) class I molecules. The synergy of this protein and the APP is required to mediate neuromuscular transmission, spatial learning and synaptic plasticity. This protein has been implicated in the pathogenesis of Alzheimer's disease. Multiple alternatively spliced transcript variants encoding different isoforms have been identified.
CDEI box-binding protein
, amyloid precursor protein homolog HSD-2
, amyloid-like protein 2
, Amyloid protein precursor-like protein 2
, amyloid beta (A4) precursor-like protein 2-like
, sperm membrane protein (YWK-II)
, sperm membrane protein YWK-II
, amyloid beta (A4) precursor-like protein 2
, amyloid-beta-like protein B
, suppression of tumorigenicity 14
, amyloid-like protein 2-like
, amyloid-beta-like protein A