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Amyloid Fibrils

Amyloid Fibrils

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 Fibrils

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Mitochondrial Precursor Proteins

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70 chaperones are targetted to TOM20-TOM22 receptor complexes.
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Translocation of Proteins into the Mitochondria

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...

Proteins: From Genes to Degradation

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Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick. Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
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Energy to Drive Translocation

Energy to Drive Translocation

Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...

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Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Published on: August 28, 2012

Amyloid precursor protein processing and bioenergetics.

Heather M Wilkins¹, Russell H Swerdlow²

¹Department of Neurology University of Kansas Medical Center, Kansas City, KS, USA; University of Kansas Alzheimer's Disease Center, Kansas City, KS, USA.

Brain Research Bulletin

|August 23, 2016

Summary

This summary is machine-generated.

Mitochondria and cellular energy production influence amyloid precursor protein (APP) processing and amyloid beta (Aβ) formation, key factors in Alzheimer

Keywords:

Alpha secretase Alzheimer's disease Amyloid beta Amyloid precursor protein BACE1 Bioenergetics Gamma secretase Mitochondria

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Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

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Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

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Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Published on: April 28, 2022

Area of Science:

Neuroscience
Biochemistry
Cell Biology

Background:

Amyloid precursor protein (APP) processing into amyloid beta (Aβ) is central to Alzheimer's disease (AD) pathogenesis.
Aβ aggregation into oligomers, protofibrils, and fibrils is a hallmark of AD.
Signaling pathways and cellular physiology impact APP processing.

Purpose of the Study:

To review existing data on the relationship between mitochondria, bioenergetics, and APP processing.
To investigate if mitochondrial function and bioenergetics modulate APP processing and Aβ production.

Main Methods:

Literature review of studies investigating APP processing, Aβ production, mitochondrial function, and cellular bioenergetics.
Analysis of data linking mitochondrial activity to alterations in APP metabolism.

Main Results:

Evidence suggests a connection between mitochondrial function and APP processing.
Cellular bioenergetics appear to influence the production of Aβ.

Conclusions:

Mitochondria and their bioenergetic state play a role in modulating APP processing and Aβ production.
Further research into this relationship may offer new therapeutic targets for Alzheimer's disease.