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

2.9K
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...
2.9K
Role of ER in the Secretory Pathway01:17

Role of ER in the Secretory Pathway

6.7K
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...
6.7K
The Unfolded Protein Response01:37

The Unfolded Protein Response

6.1K
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...
6.1K
Cell Specific Gene Expression01:58

Cell Specific Gene Expression

16.1K
Multicellular organisms contain a variety of structurally and functionally distinct cell types, but the DNA in all the cells originated from the same parent cells. The differences in the cells can be attributed to the differential gene expression. Liver cells, whose functions include detoxification of blood, production of bile to metabolize fats, and synthesis of proteins essential for metabolism, must express a specific set of genes to perform their functions. Gene expression also varies with...
16.1K
Smooth Endoplasmic Reticulum01:21

Smooth Endoplasmic Reticulum

7.6K
Smooth endoplasmic reticulum or smooth ER is a sub-organelle with specialized functions in animal cells and plant cells. It is often associated with the tubule morphology of the endoplasmic reticulum.
The ER provides optimal conditions for synthesizing steroid hormones and lipids, such as phospholipids and triglycerides. Traditionally, lipid metabolism was considered to be a smooth ER function. However, there is no direct evidence to prove that rough ER is completely excluded from lipid...
7.6K
Regulation of Food Intake01:30

Regulation of Food Intake

2.2K
Short-term regulation of food intake primarily involves neural signals from the gastrointestinal (GI) tract, blood nutrient levels, and GI tract hormones. Communication between the gut and brain via vagal nerve fibers plays a significant role in evaluating the contents of the gut. Clinical studies have shown that protein ingestion produces a more prolonged response in these nerve fibers compared to an equivalent amount of glucose. Additionally, the activation of stretch receptors caused by GI...
2.2K

You might also read

Related Articles

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

Sort by
Same author

APOC3 Promotes DGAT2-Dependent Triglyceride Accumulation in Hepatocytes During Early Metabolic Dysfunction.

Biomolecules·2026
Same author

Optimising the Therapeutic Window: A Systematic Review and Network Meta-Analysis of Pregabalin Dosing Strategies for Painful Diabetic Neuropathy.

Diabetes, obesity & metabolism·2026
Same author

Plasma EV miR-186-5p as an Early Biomarker and Regulator of IFN-α-Mediated Oxidative and β-Cell Dysfunction in Prediabetes.

Antioxidants (Basel, Switzerland)·2026
Same author

Sphingolipid metabolism-related genes B4GALNT1 and CERS4 as prognostic biomarkers in lung adenocarcinoma.

PloS one·2026
Same author

Magnolol Ameliorates Cisplatin-Induced Acute Kidney Injury with Activation of Nrf2-Associated Antioxidant Responses.

Current issues in molecular biology·2026
Same author

Plasma Mucin-1 as a Potential Biomarker for Diabetic Peripheral Neuropathy in Type 2 Diabetes.

Biomolecules·2026

Related Experiment Video

Updated: Dec 28, 2025

Measuring the Rate of Lipolysis in Ex Vivo Murine Adipose Tissue and Primary Preadipocytes Differentiated In Vitro
09:41

Measuring the Rate of Lipolysis in Ex Vivo Murine Adipose Tissue and Primary Preadipocytes Differentiated In Vitro

Published on: March 17, 2023

3.5K

Regulation of Adipsin Expression by Endoplasmic Reticulum Stress in Adipocytes.

Ka-Young Ryu1, Eon Ju Jeon2, Jaechan Leem3

  • 1Department of Physiology, Keimyung University School of Medicine, Daegu 42601, Korea.

Biomolecules
|February 22, 2020
PubMed
Summary

Obesity reduces adipsin, an insulin-boosting adipokine. This study reveals that endoplasmic reticulum (ER) stress in fat tissue suppresses adipsin by downregulating PPARγ, offering new therapeutic targets.

Keywords:
adipocytesadipsindiabetes mellitusendoplasmic reticulum stressobesity

More Related Videos

Mechanism of Regulation of Adipocyte Numbers in Adult Organisms Through Differentiation and Apoptosis Homeostasis
08:34

Mechanism of Regulation of Adipocyte Numbers in Adult Organisms Through Differentiation and Apoptosis Homeostasis

Published on: June 3, 2016

15.6K
An Adipocyte Cell Culture Model to Study the Impact of Protein and Micro-RNA Modulation on Adipocyte Function
09:20

An Adipocyte Cell Culture Model to Study the Impact of Protein and Micro-RNA Modulation on Adipocyte Function

Published on: May 4, 2021

4.1K

Related Experiment Videos

Last Updated: Dec 28, 2025

Measuring the Rate of Lipolysis in Ex Vivo Murine Adipose Tissue and Primary Preadipocytes Differentiated In Vitro
09:41

Measuring the Rate of Lipolysis in Ex Vivo Murine Adipose Tissue and Primary Preadipocytes Differentiated In Vitro

Published on: March 17, 2023

3.5K
Mechanism of Regulation of Adipocyte Numbers in Adult Organisms Through Differentiation and Apoptosis Homeostasis
08:34

Mechanism of Regulation of Adipocyte Numbers in Adult Organisms Through Differentiation and Apoptosis Homeostasis

Published on: June 3, 2016

15.6K
An Adipocyte Cell Culture Model to Study the Impact of Protein and Micro-RNA Modulation on Adipocyte Function
09:20

An Adipocyte Cell Culture Model to Study the Impact of Protein and Micro-RNA Modulation on Adipocyte Function

Published on: May 4, 2021

4.1K

Area of Science:

  • Metabolism and Endocrinology
  • Cellular Biology

Background:

  • Adipsin, an adipokine, enhances insulin secretion and glucose tolerance.
  • Adipsin expression is significantly reduced in obesity, but the underlying mechanisms are unclear.
  • Endoplasmic reticulum (ER) stress is implicated in obesity-related conditions and can alter gene expression.

Purpose of the Study:

  • To investigate the link between ER stress and adipsin expression in adipose tissue during obesity.
  • To elucidate the molecular mechanisms by which ER stress affects adipsin levels.

Main Methods:

  • Comparison of adipsin levels and ER stress markers in adipose tissue and serum of obese and lean mice.
  • Investigation of ER stress effects on adipsin expression in adipocytes.
  • Analysis of the role of peroxisome proliferator-activated receptor γ (PPARγ) in ER stress-mediated adipsin downregulation.
  • In vivo and in vitro treatment with chemical chaperones to assess recovery of adipsin and PPARγ levels.

Main Results:

  • Obese mice showed decreased adipsin and increased ER stress markers in adipose tissue and serum.
  • ER stress was found to suppress adipsin expression through adipocyte-intrinsic mechanisms.
  • Downregulation of adipsin by ER stress was partly mediated by reduced PPARγ expression.
  • Chemical chaperone treatment reversed ER stress-induced suppression of adipsin and PPARγ.

Conclusions:

  • Activated ER stress in adipose tissue is a significant factor contributing to adipsin suppression in obesity.
  • Targeting ER stress pathways may offer a therapeutic strategy to restore adipsin levels and improve metabolic health.