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Related Concept Videos

Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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...
Translation01:31

Translation

Lesson: Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of Life
Translation01:31

Translation

Lesson: Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of Life
Cystic Fibrosis: Pathogenesis01:23

Cystic Fibrosis: Pathogenesis

Cystic fibrosis (CF), an autosomal recessive disorder, significantly affects the function of exocrine glands. This genetically inherited disease is characterized by the production of thick and sticky mucus, which can severely affect various organs and systems in the body.
CF is primarily caused by a genetic mutation in a chromosome 7 gene coding for the cystic fibrosis transmembrane conductance regulator (CFTR) protein. The most common gene mutation leading to CF is the ΔF508 mutation, but...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...

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Related Experiment Video

Updated: Jun 24, 2026

Genetic Analysis of Hereditary Transthyretin Ala97Ser Related Amyloidosis
06:33

Genetic Analysis of Hereditary Transthyretin Ala97Ser Related Amyloidosis

Published on: June 9, 2018

[Transthyretin: it's miracle function and pathogenesis].

Yukio Ando1

  • 1Department of Diagnostic Medicine, Graduate School of Medical Sciences, Kumamoto University, Kumamoto 860-8556, Japan. andoy709@kumamoto-u.ac.jp

Rinsho Byori. the Japanese Journal of Clinical Pathology
|April 15, 2009
PubMed
Summary
This summary is machine-generated.

Transthyretin (TTR), a protein once known as prealbumin, binds retinol-binding protein and thyroxine. This tryptophan-rich protein is crucial in CNS disorders, amyloidosis, and nutrition assessment.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Context:

  • Transthyretin (TTR) was historically misnamed prealbumin due to its electrophoretic mobility.
  • Rodent TTR exhibits different electrophoretic behavior, highlighting the need for a function-based name.
  • TTR's primary functions include binding retinol-binding protein (RBP) and thyroxine (T4).

Purpose:

  • To elucidate the multifaceted roles and significance of Transthyretin (TTR).
  • To detail TTR's synthesis, physiological concentrations, and half-life.
  • To explore TTR's involvement in various pathological conditions and metabolic processes.

Summary:

  • TTR is synthesized in the liver, retina, pancreas, and choroid plexus, with serum concentrations of 20-40 mg/dl and a plasma half-life of 1.9 days.
  • It is the second most abundant protein in cerebrospinal fluid (CSF) and plays a role in Alzheimer's disease, depression, and lead intoxication.
  • As a tryptophan-rich, anti-acute phase protein, TTR's concentration decreases during inflammation; its amyloidogenic nature makes it a precursor for familial amyloidotic polyneuropathy (FAP).

Impact:

  • Highlights TTR's critical role in central nervous system (CNS) disorders, diabetes mellitus, and lipid metabolism.
  • Establishes TTR as a key biomarker for nutrition assessment and a significant factor in inflammatory responses.
  • Underscores TTR's dual nature as both a vital transport protein and a precursor in amyloid diseases.