Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Peptide Bonds02:43

Peptide Bonds

83.2K
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
83.2K
Animal Mitochondrial Genetics02:59

Animal Mitochondrial Genetics

9.3K
Among all the organelles in an animal cell, only mitochondria have their own independent genomes. Animal mitochondrial DNA is a double-stranded, closed-circular molecule with around 20,000 base pairs. Mitochondrial DNA is unique in that one of its two strands, the heavy, or H, -strand is guanine rich, whereas the complementary strand is cytosine rich and called the light, or L, -strand. Compared to nuclear DNA, mitochondrial DNA has a very low percentage of non-coding regions and is marked by...
9.3K
Replicative Cell Senescence02:15

Replicative Cell Senescence

4.4K
Replicative cell senescence is a property of cells that allows them to divide a finite number of times throughout the organism's lifespan while preventing excessive proliferation. Replicative senescence is associated with the gradual loss of the telomere — short, repetitive DNA sequences found at the end of the chromosomes. Telomeres are bound by a group of proteins to form a protective cap on the ends of chromosomes. Embryonic stem cells express telomerase — an enzyme that adds...
4.4K
Comparing Mitochondrial, Chloroplast, and Prokaryotic Genomes02:16

Comparing Mitochondrial, Chloroplast, and Prokaryotic Genomes

16.4K
The present-day mitochondrial and chloroplast genomes have retained some of the characteristics of their ancestral prokaryotes and also have acquired new attributes during their evolution within eukaryotic cells. Like prokaryotic genomes, mitochondrial and chloroplast genomes neither bind with histone-like proteins nor show complex packaging into chromosome-like structures, as observed in eukaryotes. Unlike mitotic cell divisions observed in eukaryotic cells, mitochondria and chloroplasts...
16.4K
Export of Mitochondrial and Chloroplast Genes02:19

Export of Mitochondrial and Chloroplast Genes

4.2K
A eukaryotic cell can have up to three different types of genetic systems: nuclear, mitochondrial, and chloroplast. During evolution, organelles have exported many genes to the nucleus; this transfer is still ongoing in some plant species. Approximately 18% of the Arabidopsis thaliana nuclear genome is thought to be derived from the chloroplast’s cyanobacterial ancestor, and around 75% of the yeast genome derived from the mitochondria’s bacterial ancestor. This export has occurred...
4.2K
The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

4.7K
The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
4.7K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Development of a Humanized Anti-Fibrotic Antibody Targeting Extracellular Collagen Assembly to Reduce Post-Traumatic Scarring.

bioRxiv : the preprint server for biology·2026
Same author

Simulated Workflow Feasibility Evaluation of a Web-Based Periorbital Measurement Platform: Development and Usability Study.

JMIR human factors·2026
Same author

Alternate splicing converts human CD137 from costimulatory to immunosuppressive function.

Journal of autoimmunity·2025
Same author

Seroprevalence of dengue virus infection among febrile patients visiting healthcare facilities in the selected districts of Afar region, Northeast Ethiopia.

BMC infectious diseases·2025
Same author

Higher order receptor clustering due to the IgG3 subclass is necessary for TLR4 signaling and tolerance induction by novel human anti-TLR4 antibodies.

mAbs·2025
Same author

Neutralization of Marinobufagenin Demonstrates Efficacy In Vitro and In Vivo in Models of Pre-Eclampsia.

Biomedicines·2025

Related Experiment Video

Updated: Feb 7, 2026

Subcellular Fractionation for ERK Activation Upon Mitochondrial-derived Peptide Treatment
07:55

Subcellular Fractionation for ERK Activation Upon Mitochondrial-derived Peptide Treatment

Published on: September 25, 2017

8.3K

Mitochondrial-Derived Peptides Exacerbate Senescence.

Andrew R Mendelsohn1,2, James W Larrick1,2

  • 11 Panorama Research Institute , Sunnyvale, California.

Rejuvenation Research
|July 31, 2018
PubMed
Summary

Mitochondrial-derived peptides (MDPs) show potential in treating age-related diseases. While they protect normal cells, they may worsen inflammation in senescent cells, suggesting combination therapy with senolytics for enhanced outcomes.

Keywords:
MOTS-cSASPhumaninmitochondriamitochondria-derived peptidessenescence

More Related Videos

Far-Red Fluorescent Senescence-Associated β-Galactosidase Probe for Identification and Enrichment of Senescent Tumor Cells by Flow Cytometry
14:01

Far-Red Fluorescent Senescence-Associated β-Galactosidase Probe for Identification and Enrichment of Senescent Tumor Cells by Flow Cytometry

Published on: September 13, 2022

5.8K
Techniques to Induce and Quantify Cellular Senescence
06:51

Techniques to Induce and Quantify Cellular Senescence

Published on: May 1, 2017

35.1K

Related Experiment Videos

Last Updated: Feb 7, 2026

Subcellular Fractionation for ERK Activation Upon Mitochondrial-derived Peptide Treatment
07:55

Subcellular Fractionation for ERK Activation Upon Mitochondrial-derived Peptide Treatment

Published on: September 25, 2017

8.3K
Far-Red Fluorescent Senescence-Associated β-Galactosidase Probe for Identification and Enrichment of Senescent Tumor Cells by Flow Cytometry
14:01

Far-Red Fluorescent Senescence-Associated β-Galactosidase Probe for Identification and Enrichment of Senescent Tumor Cells by Flow Cytometry

Published on: September 13, 2022

5.8K
Techniques to Induce and Quantify Cellular Senescence
06:51

Techniques to Induce and Quantify Cellular Senescence

Published on: May 1, 2017

35.1K

Area of Science:

  • Mitochondrial biology
  • Aging research
  • Molecular medicine

Background:

  • Mitochondrial-derived peptides (MDPs) are encoded by mitochondrial DNA and offer cytoprotection.
  • Humanin and MOTS-c are MDPs with hypothesized antiaging effects, linked to conditions like type 2 diabetes and atherosclerosis.
  • Correlative studies suggest MDPs may counteract aging processes, but their direct impact on cellular senescence is complex.

Purpose of the Study:

  • To investigate the role of MDPs, specifically humanin and MOTS-c, in cellular aging and senescence.
  • To explore the potential of MDPs in combination with senolytic therapies for age-related diseases.
  • To clarify the interaction between MDPs and the senescence-associated secretory phenotype (SASP).

Main Methods:

  • Review of existing literature on MDPs, humanin, MOTS-c, and cellular senescence.
  • Analysis of studies examining MDPs' effects on mitochondrial function, cell viability, and disease models.
  • Examination of recent findings on MDPs' impact on SASP and senescent cells.

Main Results:

  • MDPs demonstrate cytoprotective effects, preserving mitochondrial function and cell viability.
  • Humanin and MOTS-c have shown benefits in models of atherosclerosis and type 2 diabetes.
  • Contrary to expectations of senolytic activity, humanin and MOTS-c were found to exacerbate the SASP in senescent cells by increasing proinflammatory cytokine secretion.

Conclusions:

  • MDPs possess cytoprotective properties beneficial for normal cells, potentially aiding in diseases associated with aging.
  • MDPs may enhance the efficacy of senolytic therapies by modulating the SASP, potentially making senescent cells more susceptible to clearance or senolytic treatment.
  • Combination strategies involving MDPs and senolytics warrant further investigation for synergistic therapeutic benefits in age-related conditions.