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

Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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...
Role of ER in the Secretory Pathway01:17

Role of ER in the Secretory Pathway

Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as the secretory pathway.
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
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...
The Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...

You might also read

Related Articles

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

Sort by
Same author

Targeting the Glucokinase-Glucokinase Regulatory Protein Axis: Pharmacophore-Based Identification of Novel Antidiabetic Small Molecules.

ACS medicinal chemistry letters·2026
Same author

Sustainable Synthesis and Biological Aspects of Pyrrolobenzodiazepine Derivatives: An Insight Into Current Developments, Structure-Activity Relationships, and Clinical Studies.

Chemical record (New York, N.Y.)·2026
Same author

Molecular biochemistry of soluble epoxide hydrolase in lipid mediator pathways and neuroinflammatory responses.

The Journal of steroid biochemistry and molecular biology·2026
Same author

From gastric to neuroprotection: pantoprazole mitigates epilepsy via TrkB/BDNF and KCC2 modulation.

Naunyn-Schmiedeberg's archives of pharmacology·2026
Same author

The interplay between exosomal miRNAs and cytokine networks in metabolic diseases.

Frontiers in cell and developmental biology·2026
Same author

Identification of a novel GSK-3β inhibitor for Alzheimer's disease using In-Silico prediction and experiment cycling, validated in a streptozotocin-induced Alzheimer's disease mouse model.

Naunyn-Schmiedeberg's archives of pharmacology·2026

Related Experiment Video

Updated: Jun 19, 2026

Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons
10:50

Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons

Published on: April 24, 2021

Cell-Penetrating Peptide-Mediated Modulation of Endoplasmic Reticulum Stress: A Bioengineered and Translational

Tripti Paliwal1,2, Radhika Joshi1,2, Sarvesh Paliwal1

  • 1Department of Pharmacy, Banasthali Vidyapith, Banasthali, Rajasthan 304022, India.

ACS Pharmacology & Translational Science
|June 18, 2026
PubMed
Summary

Bioengineered cell-penetrating peptides (CPPs) and adipose-derived stem cells (ADSCs) offer a dual approach to combat endoplasmic reticulum (ER) stress. This synergy targets metabolic and inflammatory disorders by restoring cellular homeostasis.

Keywords:
ER stressadipose tissue-derived stem cellscell penetrating peptidemetabolic dysfunction

More Related Videos

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication
10:12

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication

Published on: June 14, 2024

Engineering Cell-permeable Protein
21:08

Engineering Cell-permeable Protein

Published on: December 28, 2009

Related Experiment Videos

Last Updated: Jun 19, 2026

Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons
10:50

Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons

Published on: April 24, 2021

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication
10:12

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication

Published on: June 14, 2024

Engineering Cell-permeable Protein
21:08

Engineering Cell-permeable Protein

Published on: December 28, 2009

Area of Science:

  • Biomedical Engineering
  • Cell Biology
  • Molecular Medicine

Background:

  • Endoplasmic reticulum (ER) stress is a key factor in metabolic and inflammatory diseases like insulin resistance and cardiovascular dysfunction.
  • The unfolded protein response (UPR) activates pathways (PERK, IRE1, ATF6) leading to inflammation, apoptosis, and cellular dysfunction.
  • Targeting ER stress is a promising therapeutic strategy for these disorders.

Purpose of the Study:

  • To explore the synergistic potential of cell-penetrating peptides (CPPs) and adipose-derived stem cells (ADSCs) for modulating ER stress.
  • To evaluate this bioengineered approach as a therapeutic platform for metabolic pathophysiology.

Main Methods:

  • Utilizing CPPs for intracellular delivery of therapeutic agents targeting ER stress mediators (e.g., CHOP, GRP78, IRE1, NF-κB).
  • Leveraging ADSCs for their paracrine effects, secreting anti-inflammatory cytokines, growth factors, and antioxidants.
  • Investigating the combined effects of CPPs and ADSCs on ER homeostasis, inflammation, and cellular survival.

Main Results:

  • CPP-mediated delivery restores ER homeostasis and reduces inflammatory signaling in various cell types.
  • ADSCs secrete factors that mitigate ER stress and oxidative stress, aiding tissue repair and metabolic homeostasis.
  • The combined CPP-ADSC platform demonstrates multifunctional therapeutic potential.

Conclusions:

  • The synergistic combination of CPPs and ADSCs presents a novel, multifunctional therapeutic platform for targeting ER stress.
  • This bioengineered approach holds significant translational potential for precision medicine in metabolic disorders.
  • This strategy advances laboratory innovations towards clinical applications for metabolic pathophysiology.