Amyloid beta A4 (Phospho-Thr743/668) ELISA Kit

Alzheimer's disease (AD) is one of the most common neurodegenerative disorders in recent world, characterized by increased production of amyloid beta in the nervous system with an ultimate effect of apoptotic neurodegeneration. This study was aimed to investigate the neuroprotective effect of black soybean anthocyanins in a neurodegenerative model of amyloid beta 1-42 (A beta(1-42)). A beta(1-42) was treated to HT22 cell lines or adult male rats via intra-cerebro-ventricular injection to induce neurotoxicity in these experimental models. Anthocyanins were treated 0.2 mg/kg in case of cell lines or 4 mg/kg intragastrically to adult rats to protect against A beta-induced neurodegeneration. Assay for cell viability, mitochondrial membrane potential (Psi m), intracellular free Ca2+ and apoptotic cells (fluoro-jade B and TUNEL) were performed in vitro while western blot analyses were performed to the hippocampal proteins of adult rats. Our results showed that A beta(1-42) treatment reduced cell viability, disturbed the psi m and Ca2+ homeostasis in and out of the cell, and increased neuronal apoptosis. Treatment with anthocyanins for 12 hr retained the cell viability, normalized psi m and Ca2+ level, and decreased the neuronal cell death. In accordance, anthocyanins reversed A beta-induced effect on protein expression of mitochondrial apoptotic pathway (Bax. cytochrome C, caspase-9 and caspase-3) and major Alzheimer's markers i.e. A beta, APP, P-tau and BACE-1. Overall, our results showed that anthocyanins are potential candidates to treat neurodegenerative disorders like AD. (C) 2014 Elsevier Ltd. All rights reserved.

The assembly of the gamma-secretase complex, an Alzheimer disease-related protease required for beta-amyloid generation, is tightly regulated and predominantly limited by the stoichiometrical availability of its components. We have identified a novel endoplasmic reticulum-located protein complex that is regulated in a similar fashion. It contains the recently identified Nodal signaling antagonists Nicalin ( a distant homolog of the gamma-secretase component Nicastrin) and NOMO ( Nodal modulator). Using an RNA interference approach, we found that Nicalin and NOMO became unstable in the absence of the respective binding partner, suggesting that complex formation has a stabilizing effect. Overexpression of Nicalin resulted in an increase in NOMO, whereas endogenous Nicalin was reduced below the detection limit. Both effects were shown to occur at a post-transcriptional level. Thus, NOMO is most likely produced in excess amounts and either stabilized by Nicalin or rapidly degraded. In contrast, Nicalin levels are limited independently of NOMO. We, therefore, propose that Nicalin controls the assembly and stability of the Nicalin-NOMO complex.