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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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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. 
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Membrane Fluidity01:26

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Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is...
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Membrane Fluidity01:23

Membrane Fluidity

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Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.
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Fluid Mosaic Model01:19

Fluid Mosaic Model

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Scientists identified the plasma membrane in the 1890s and its principal chemical components (lipids and proteins) by 1915. The model for plasma membrane structure, proposed in 1935 by Hugh Davson and James Danielli, was the first model to be widely accepted in the scientific community. The model was based on the plasma membrane's "railroad track" appearance in early electron micrographs. Davson and Danielli theorized that the plasma membrane's structure resembled a sandwich...
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Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

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The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
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Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
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Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

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Cellular membrane fluidity in amyloid precursor protein processing.

Xiaoguang Yang1, Grace Y Sun, Gunter P Eckert

  • 1Department of Clinical Neuroscience and Rehabilitation, Institute of Neuroscience and Physiology, Sahlgrenska Academy, University of Gothenburg, 405 30, Gothenburg, Sweden.

Molecular Neurobiology
|February 21, 2014
PubMed
Summary
This summary is machine-generated.

Cell membrane properties influence Alzheimer's disease (AD) pathology. Alterations in membrane fluidity, driven by factors like phospholipases A2 (PLA2s) and cholesterol, affect amyloid precursor protein (APP) processing and amyloid-beta (Aβ) production.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Cell Biology

Background:

  • Senile plaques composed of amyloid-beta (Aβ) are hallmarks of Alzheimer's disease (AD).
  • Aβ is generated through the amyloidogenic pathway involving β- and γ-secretase cleavage of amyloid precursor protein (APP).
  • The nonamyloidogenic pathway, involving α-secretase, produces neuroprotective soluble APP (sAPPα).

Purpose of the Study:

  • To review the critical role of cellular membrane biophysical properties in regulating APP processing.
  • To explore how factors like phospholipases A2 (PLA2s), fatty acids, cholesterol, and Aβ impact membrane fluidity and APP metabolism.

Main Methods:

  • Literature review focusing on the interplay between membrane biophysics and APP processing.
  • Analysis of studies investigating the effects of specific lipids and enzymes on membrane properties and secretase activity.

Main Results:

  • Membrane composition and fluidity significantly influence the activity of secretases involved in APP processing.
  • Phospholipases A2 (PLA2s), fatty acids, and cholesterol modulate membrane fluidity, thereby affecting the balance between amyloidogenic and nonamyloidogenic pathways.
  • Aβ itself can alter membrane properties, potentially creating feedback loops that exacerbate pathology.

Conclusions:

  • Cellular membrane biophysical properties are crucial determinants of APP processing and Aβ generation in AD.
  • Targeting membrane properties may offer novel therapeutic strategies for Alzheimer's disease.
  • Understanding these membrane-centric mechanisms is vital for advancing AD research.