含有4的V集和免疫球蛋白域作为阿尔茨海默病和晚期衰老的潜在预测因子

相关实验视频

Updated: May 21, 2025

Generalized Psychophysiological Interaction PPI Analysis of Memory Related Connectivity in Individuals at Genetic Risk for Alzheimer's Disease

Published on: November 14, 2017

14.8K

Bowen Yang¹, Aygun Teymur¹, Chenling Tang¹

¹Department of Biomedical Engineering, University of Houston, Houston, TX, USA.

Journal of Alzheimer's disease : JAD

|March 21, 2025

概括

在阿尔茨海默病 (AD) 患者中,含有4 (VSIG4) 的血清V集和免疫球蛋白域升高,与认知衰退和神经炎症标志物相关. 这表明VSIG4的存在.

科学领域:

免疫学免疫学免疫学
神经科学是一个神经科学.
生物化学生物化学

背景情况:

含有4 (VSIG4) 的V-集和免疫球蛋白域与免疫系统通路有关.
VSIG4已被确定为阿尔茨海默病 (AD) 和衰老研究中的潜在枢纽基因.

研究的目的:

评估血清VSIG4水平在阿尔茨海默病中的诊断效用.
调查血清VSIG4和其他AD生物标志物和认知评估之间的关系.

主要方法:

酶相关免疫吸收试验 (ELISA) 用于量化血清VSIG4度.
在AD患者和健康对照者之间比较了血清VSIG4水平.
研究了VSIG4,年龄,其他血清蛋白 (总tau,NfL,YKL-40,CD14,FABP3,TNF-α) 和神经测试结果之间的相关性.

主要成果:

与健康对照人群相比,AD患者的VSIG4血清水平显著更高 (p=0.0074).
在血清VSIG4和已确定的AD/炎症标志物之间观察到显著的相关性,包括总tau,神经丝光 (NfL),YKL-40,CD14,FABP3和TNF-α.
血清VSIG4度与神经和认知测试结果有显著的相关性.

结论:

血清VSIG4升高可能成为阿尔茨海默病的潜在生物标志物.
血清VSIG4水平可能反映了潜在的神经炎症和在AD和衰老中改变的脂质处理.
VSIG4与认知表现的关联凸显了它在AD病变发生过程中的作用.

关键词:

阿尔茨海默病的疾病阿尔茨海默病的疾病.在VSIG4中使用VSIG4.老化的老化衰老的老化生物标志物生物标志物补充 C3 补充 C3 补充

相关概念视频

01:26

Alzheimer's Disease: Overview

405

Alzheimer's Disease (AD) is a continually advancing neurodegenerative disorder, distinguished by escalating memory loss, cognitive dysfunction, and dementia. The disease unfolds in three stages: preclinical, mild cognitive impairment (MCI), and dementia. Its onset is insidious, and the progression gradual, with the cause not well explained by other disorders.
The clinical diagnosis of AD hinges on the presence of memory and other cognitive impairments. Biomarkers, such as changes in Aβ...

405

01:31

Immunoglobulin-like Cell Adhesion Molecules

3.2K

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...

3.2K

03:03

Amyloid Fibrils

9.1K

Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...