Related Experiment Video
Updated: Apr 1, 2026
09:31
Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry
Published on: March 7, 2019
11.2K
Golgi fragmentation in Alzheimer's disease
Gunjan Joshi1, Michael E Bekier1, Yanzhuang Wang2
1Department of Molecular, Cellular and Developmental Biology, University of Michigan Ann Arbor, MI, USA.
Frontiers in Neuroscience
|October 7, 2015
Summary
Golgi apparatus fragmentation, linked to Alzheimer's disease (AD) protein dysfunction, can be reversed by inhibiting GRASP65 phosphorylation, restoring cell structure and reducing amyloid-beta production.
Area of Science:
- Cell Biology
- Neuroscience
- Biochemistry
Background:
- The Golgi apparatus is crucial for protein modification, sorting, and transport.
- Golgi structure and function are impaired in neurodegenerative diseases, including Alzheimer's disease (AD).
- Golgi fragmentation is observed in AD, suggesting a role in disease pathogenesis.
Purpose of the Study:
- To review the cellular impact of impaired Golgi morphology.
- To explore the potential relationship between Golgi defects and Alzheimer's disease development.
- To highlight the role of GRASP65 phosphorylation in Golgi fragmentation in AD.
Main Methods:
- Review of recent studies on Golgi apparatus function and neurodegeneration.
- Analysis of the role of GRASP65 phosphorylation in Golgi structure.
- Investigation of therapeutic strategies targeting Golgi fragmentation in AD models.
Main Results:
- Phosphorylation of GRASP65 disrupts Golgi structure, leading to fragmentation.
- Inhibiting GRASP65 phosphorylation can restore Golgi morphology.
- Restoring Golgi structure reduces amyloid-beta (Aβ) production in AD models.
- Golgi dysfunction impacts neuronal protein trafficking, potentially promoting AD.
Conclusions:
- Impaired Golgi morphology is a significant factor in Alzheimer's disease.
- Targeting GRASP65 phosphorylation offers a potential therapeutic strategy for AD.
- Further research into Golgi-neuron interactions is vital for understanding and treating AD.
More Related Videos
Related Concept Videos
01:26Alzheimer's Disease: Overview
2.0K
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...
The clinical diagnosis of AD hinges on the presence of memory and other cognitive impairments. Biomarkers, such as changes in Aβ...
2.0K
03:03Amyloid Fibrils
13.0K
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,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
13.0K
03:03Amyloid Fibrils
7.0K
7.0K
01:12Golgi Matrix Proteins
2.5K
Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
2.5K
01:22Alzheimer's Disease: Treatment
1.2K
Alzheimer's Disease (AD), a neurodegenerative disorder, is pathologically identified by amyloid plaques and neurofibrillary tangles composed of tau protein. AD pharmacotherapy aims to manage cognitive symptoms, delay disease progression, and treat behavioral symptoms. The treatment is primarily symptomatic and palliative, with no definitive disease-modifying therapy available. Cholinesterase inhibitors, including donepezil (Aricept), rivastigmine (Exelon), and galantamine (Razadyne), are...
1.2K
01:26Transport Across the Golgi
6.7K
While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
6.7K