相关实验视频

Updated: Jun 4, 2025

Preparation of Acute Hippocampal Slices from Rats and Transgenic Mice for the Study of Synaptic Alterations during Aging and Amyloid Pathology

Preparation of Acute Hippocampal Slices from Rats and Transgenic Mice for the Study of Synaptic Alterations during Aging and Amyloid Pathology

Published on: March 23, 2011

在老的内腔皮层中失调的信号传递与陶过酸化相关

S Bathla, D Datta, D Bolat

bioRxiv : the preprint server for biology

|December 23, 2024

概括

早期阿尔茨海默氏病 (AD) 在内耳皮层 (ERC) 的tau病理涉及信号传递. 的与年龄相关的变化表明,高酸化的信号质tau失调,导致早期AD神经退行.

科学领域:

神经科学是一个神经科学.
病理学病理学病理学
生物化学生物化学

背景情况:

阿尔茨海默氏病 (AD) 的tau病理始于脑内皮层 (ERC).
研究人类大脑中早期,可溶性病理的研究是具有挑战性的,因为死后的脱化.
rhesus 表现出与人类AD相似的与年龄相关的 tau 病理,作为一个有价值的模型.

研究的目的:

研究的ERC中早期tau病理的分子机制.
检查和炎症信号通路在陶过酸化中的作用.

主要方法:

对的ERC分子变化的分析.
专注于二酶4 (PDE4),calpain-2和瓜尼利基环酶生成酶II (GCPII) 的活性.
在特定表位 (pS214-tau, pT181-tau, pT217-tau) 上评估高酸化.

主要成果:

观察到与年龄相关的PDE4活性下降.
卡尔巴因-2和GCPII水平的增加与陶过酸化相关.
早期的高酸化发生在多个部位,包括pS214-tau,pT181-tau和pT217-tau.

结论:

在ERC中失调的信号传递,从中年开始,似乎是超酸化的先行和主要的tau.
这些分子变化可能驱动病理和阿尔茨海默氏症神经退行症的初始阶段.
了解ERC的漏洞对于理解AD的发病过程至关重要.

更多相关视频

Fluorescence and Bioluminescence Imaging of Subcellular Ca2+ in Aged Hippocampal Neurons

Fluorescence and Bioluminescence Imaging of Subcellular Ca2+ in Aged Hippocampal Neurons

Published on: December 1, 2015

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

相关概念视频

Long-term Depression

Long-term Depression

Long-term depression, or LTD, is one of the ways by which synaptic plasticity—changes in the strength of chemical synapses—can occur in the brain. LTD is the process of synaptic weakening that occurs over time between pre and postsynaptic neuronal connections. The synaptic weakening of LTD works in opposition to synaptic strengthening by long-term potentiation (LTP) and together are the main mechanisms that underlie learning and memory.
Calcium Ion Concentration Mechanism
If over...

Calmodulin-dependent Signaling

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...