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Related Concept Videos

Amyloid Fibrils03:03

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, normally used to...
Amyloid Fibrils03:03

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, normally used to...
Inborn Errors of Metabolism01:20

Inborn Errors of Metabolism

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Overview of Protein Metabolism01:21

Overview of Protein Metabolism

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Amino acids play various roles in the body once they are absorbed into cells. They are restructured...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Insulin: Biosynthesis, Chemistry, and Preparation

The endoplasmic reticulum (ER) of pancreatic β-cells synthesizes preproinsulin, which consists of a signal peptide, A and B chains, and a C-peptide. Preproinsulin is then cleaved and folded into proinsulin, which translocates to the Golgi apparatus for sorting and packaging into secretory granules. In these granules, enzymatic clipping generates insulin and C-peptide.
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Related Experiment Video

Updated: Jul 16, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Isoform specific amyloid-beta protein precursor metabolism.

Ana Gabriela Henriques1, Sandra Isabel Vieira, Sandra Rebelo

  • 1Laboratório de Neurociências, Centro de Biologia Celular, Universidade de Aveiro, Aveiro, Portugal.

Journal of Alzheimer'S Disease : JAD
|March 16, 2007
PubMed
Summary

Alzheimer

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Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

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Area of Science:

  • Molecular Biology
  • Neuroscience
  • Biochemistry

Background:

  • Alzheimer's amyloid-beta protein precursor (AbetaPP) exists in multiple isoforms, including AbetaPP(751) (abundant in non-neuronal tissues) and AbetaPP(695) (predominant in neurons).
  • The specific roles and processing differences between AbetaPP isoforms are not well understood.
  • Understanding isoform-specific functions is crucial given their differential expression in neuronal and non-neuronal tissues and potential links to Alzheimer's disease pathology.

Purpose of the Study:

  • To investigate and compare the intracellular processing, targeting, and response to stimuli of AbetaPP(751) and AbetaPP(695) isoforms.
  • To elucidate potential isoform-specific differences in maturation rates and phosphorylation-regulated events.
  • To assess the implications of these isoform-specific characteristics for Alzheimer's disease research.

Main Methods:

  • Utilized endogenous and green fluorescent protein (GFP)-tagged AbetaPP isoforms for isoform-specific monitoring.
  • Measured intracellular processing and targeting differences between AbetaPP(751) and AbetaPP(695).
  • Assessed the impact of okadaic acid (OA) and phorbol 12-myristate 13-acetate (PMA) on soluble AbetaPP (sAbetaPP) production for each isoform.

Main Results:

  • AbetaPP(751) exhibited faster turnover rates (maturation) compared to AbetaPP(695) in both endogenous and transfected proteins.
  • AbetaPP(751) responded robustly to both OA and PMA, with PMA inducing a stronger response in sAbetaPP production.
  • AbetaPP(695) showed a strong response to PMA, but failed to elicit significant sAbetaPP induction with OA, indicating isoform-specific phosphorylation regulation.

Conclusions:

  • AbetaPP(695) is processed/metabolized more slowly and responds differently to OA compared to AbetaPP(751).
  • Isoform-specific processing and differential responses to regulatory agents highlight distinct functional roles.
  • Further investigation into the relevance of AbetaPP isoform-specific processing in Alzheimer's disease is warranted due to differential expression and pathological alterations.