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Related Concept Videos

Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Aging01:26

Aging

Aging is a complex biological phenomenon influenced by various processes that affect cellular and systemic functions. Several prominent theories attempt to explain its mechanisms, highlighting cellular limitations, oxidative damage, and hormonal changes as central factors in aging.
Cellular Clock Theory
The cellular clock theory posits that the human lifespan is closely tied to the finite capacity of cells to divide, a phenomenon governed by telomeres, which are protective caps at the ends of...
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
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...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...

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Related Experiment Video

Updated: May 12, 2026

Imaging Approaches to Assessments of Toxicological Oxidative Stress Using Genetically-encoded Fluorogenic Sensors
09:33

Imaging Approaches to Assessments of Toxicological Oxidative Stress Using Genetically-encoded Fluorogenic Sensors

Published on: February 7, 2018

Age-associated, oxidatively modified proteins: A critical evaluation.

S Goto, A Nakamura

    Age
    |April 23, 2013
    PubMed
    Summary

    Oxidative stress modifies proteins, potentially causing disease and aging. Further research is needed to confirm age-related protein carbonyl increases and understand protein degradation in aging tissues.

    Area of Science:

    • Biochemistry
    • Gerontology
    • Molecular Biology

    Background:

    • Reactive oxygen species (ROS) cause oxidative protein damage, forming carbonyls.
    • Protein carbonyls are linked to diseases and age-related physiological decline.
    • The role of protein oxidation in aging is a complex and evolving field.

    Purpose of the Study:

    • To critically evaluate protein carbonyl content as a marker of oxidative stress in aging.
    • To discuss methodologies for measuring and characterizing protein carbonyls.
    • To explore the degradation of oxidatively modified proteins in relation to aging.

    Main Methods:

    • Critical review of existing literature on protein carbonyls and aging.
    • Discussion of methodological challenges in measuring protein carbonyls.

    More Related Videos

    Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
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    Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

    Published on: June 21, 2021

    Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
    10:24

    Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

    Published on: June 7, 2018

    Related Experiment Videos

    Last Updated: May 12, 2026

    Imaging Approaches to Assessments of Toxicological Oxidative Stress Using Genetically-encoded Fluorogenic Sensors
    09:33

    Imaging Approaches to Assessments of Toxicological Oxidative Stress Using Genetically-encoded Fluorogenic Sensors

    Published on: February 7, 2018

    Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
    07:16

    Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

    Published on: June 21, 2021

    Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
    10:24

    Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

    Published on: June 7, 2018

  • Emphasis on immunoblot analysis with two-dimensional gel electrophoresis.

    • Main Results:

    • Current evidence for an age-related increase in protein carbonyls requires further confirmation with advanced methodologies.
    • Methodological variations in protein carbonyl measurement present challenges.
    • The degradation pathways and accumulation of oxidatively modified proteins in aged tissues remain underexplored.

    Conclusions:

    • Definitive conclusions on age-related increases in protein carbonyls await further validation.
    • Improved methodologies are crucial for accurate assessment of oxidative stress markers.
    • Further investigation into the degradation of oxidatively modified proteins is necessary to understand their role in aging.