Related Experiment Video
Updated: Oct 13, 2025

09:58
Lipidomics and Transcriptomics in Neurological Diseases
Published on: March 18, 2022
3.7K
Neurodegenerative Disorders: Spotlight on Sphingolipids
1Institute of Neurogenetics, University of Luebeck, Ratzeburger Allee 160, 23562 Lübeck, Germany.
International Journal of Molecular Sciences
|November 13, 2021
Summary
Sphingolipids are crucial in neurodegenerative diseases, impacting brain function and cellular processes. This review highlights their role in conditions like Parkinson
Area of Science:
- Neuroscience, Biochemistry, Genetics
Background:
- Neurodegenerative diseases involve progressive neuronal loss and dysfunction.
- Protein deposits and mitochondrial damage are common hallmarks.
- Sphingolipids, essential brain components, are increasingly linked to neurodegeneration pathogenesis.
Purpose of the Study:
- To review key findings on sphingolipids in neurodegenerative diseases.
- To focus on the role of sphingolipids in neurodegeneration with brain iron accumulation and Parkinson's disease.
Main Methods:
- Literature review of studies on sphingolipids and neurodegeneration.
- Analysis of sphingolipid involvement in cellular processes like apoptosis and autophagy.
- Examination of sphingolipid metabolism and its impact on neuronal health.
Main Results:
- Sphingolipids play vital roles in cell growth, apoptosis, and autophagy.
- Dysregulation of sphingolipid metabolism is implicated in neurodegenerative conditions.
- Specific sphingolipids are highlighted for their relevance in neurodegeneration with brain iron accumulation and Parkinson's disease.
Conclusions:
- Sphingolipids are critical players in the pathogenesis of neurodegenerative diseases.
- Targeting sphingolipid pathways may offer therapeutic strategies.
- Further research into sphingolipid biochemistry is essential for understanding and treating these conditions.
Related Concept Videos
Parkinson's Disease: Overview
824
Neurodegenerative disorders are progressive diseases that cause irreversible damage and loss to neurons in specific brain areas. Examples of these disorders include Parkinson's disease, Alzheimer's disease, Multiple Sclerosis (MS), and Amyotrophic Lateral Sclerosis (ALS). These disorders share characteristics such as proteinopathies, selective neuronal vulnerability, and a complex interplay between genetic and environmental factors. The primary therapeutic goal for these conditions is...
824
Glial Cells
90.3K
Overview
90.3K
Lysosomal Hydrolases
4.0K
Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
4.0K
Neural Regulation
40.5K
Digestion begins with a cephalic phase that prepares the digestive system to receive food. When our brain processes visual or olfactory information about food, it triggers impulses in the cranial nerves innervating the salivary glands and stomach to prepare for food.
40.5K
Alzheimer's Disease: Overview
740
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...
740
Amyloid Fibrils
10.7K
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,...
10.7K

