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

Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
Amplifying Signals via Second Messengers01:15

Amplifying Signals via Second Messengers

Many receptor binding ligands are hydrophilic; they do not cross the cell membrane but bind to cell-surface receptors. Thus, their message must be relayed by second messengers present in the cell cytoplasm. There are several second messenger pathways, each with its own way of relaying information. For example, the G protein-coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol pathway is active when the receptor induces...
TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors are of three kinds RI, RII, and RIII. The RI...
GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
Two...
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
Adrenergic Receptors: β Subtype01:26

Adrenergic Receptors: β Subtype

β-adrenoceptors have varied sensitivities towards adrenaline, noradrenaline, and isoprenaline. The order of agonist potency is as follows:
Isoprenaline > Adrenaline > Noradrenaline
Neurotransmitter binding to these receptors causes activation of adenylyl cyclase resulting in increased concentrations of cAMP and modulation of calcium ion channels within the cell. They are further classified into β1, β2, and β3 subtypes.
β1-adrenoceptors: β1-adrenoceptors have equal affinities for...

You might also read

Related Articles

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

Sort by
Same author

Proteolytic activation of a single-chain precursor of hepatocyte growth factor by extracellular serine-protease.

Biochemical and biophysical research communications·1992
Same author

[A case of insulinoma with frequent hypoglycemic attacks not showing evident hyperinsulinemia].

Nihon Naibunpi Gakkai zasshi·1992
Same author

Effect of mean airway pressure on bronchial mucosal blood flow in rabbits with oleic acid-induced injury.

Acta paediatrica Japonica : Overseas edition·1992
Same author

[An examination of self-monitoring as a determinant of compliant conforming behaviour].

Shinrigaku kenkyu : The Japanese journal of psychology·1992
Same author

Simple in vivo bioassay without radioisotopes for recombinant human erythropoietins.

Biologicals : journal of the International Association of Biological Standardization·1992
Same author

In vivo biological activities of recombinant human erythropoietin analogues produced by CHO cells, BHK cells and C127 cells.

Biologicals : journal of the International Association of Biological Standardization·1992

Related Experiment Video

Updated: Jul 6, 2026

Measurement of Basal and Forskolin-stimulated Lipolysis in Inguinal Adipose Fat Pads
07:59

Measurement of Basal and Forskolin-stimulated Lipolysis in Inguinal Adipose Fat Pads

Published on: July 21, 2017

The stimulation of beta(3)-adrenoceptor causes phosphorylation of extracellular signal-regulated kinases 1 and 2

K Mizuno1, Y Kanda, Y Kuroki

  • 1Department of Pharmacology, National Defense Medical College, 3-2 Namiki, 359-8513, Tokorozawa, Japan.

European Journal of Pharmacology
|September 12, 2000
PubMed
Summary
This summary is machine-generated.

Three beta(3)-adrenoceptor agonists activate ERK1/2 phosphorylation in adipocytes. This process involves a G(s) protein pathway, distinct from pertussis toxin-sensitive signaling, highlighting a novel mechanism in cellular regulation.

More Related Videos

Studying TGF-β Signaling and TGF-β-induced Epithelial-to-mesenchymal Transition in Breast Cancer and Normal Cells
06:54

Studying TGF-β Signaling and TGF-β-induced Epithelial-to-mesenchymal Transition in Breast Cancer and Normal Cells

Published on: October 27, 2020

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

Related Experiment Videos

Last Updated: Jul 6, 2026

Measurement of Basal and Forskolin-stimulated Lipolysis in Inguinal Adipose Fat Pads
07:59

Measurement of Basal and Forskolin-stimulated Lipolysis in Inguinal Adipose Fat Pads

Published on: July 21, 2017

Studying TGF-β Signaling and TGF-β-induced Epithelial-to-mesenchymal Transition in Breast Cancer and Normal Cells
06:54

Studying TGF-β Signaling and TGF-β-induced Epithelial-to-mesenchymal Transition in Breast Cancer and Normal Cells

Published on: October 27, 2020

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

Area of Science:

  • Cellular and Molecular Biology
  • Biochemistry
  • Pharmacology

Background:

  • Beta(3)-adrenoceptors play a role in regulating adipocyte function.
  • Extracellular signal-regulated kinases (ERK1/2) are key signaling molecules involved in cellular processes.
  • Understanding the signaling pathways activated by beta(3)-adrenoceptor agonists is crucial for metabolic research.

Purpose of the Study:

  • To investigate the signaling pathway mediating ERK1/2 phosphorylation induced by beta(3)-adrenoceptor agonists in 3T3-L1 adipocytes.
  • To determine the involvement of G proteins in this signaling cascade.

Main Methods:

  • Treatment of 3T3-L1 adipocytes with specific beta(3)-adrenoceptor agonists (BRL37344, CGP12177, SR58611).
  • Assessment of ERK1/2 phosphorylation.
  • Pretreatment with pertussis toxin and cholera toxin to elucidate G protein involvement.
  • Comparison with lisophosphatidic acid-induced signaling.

Main Results:

  • Beta(3)-adrenoceptor agonists induced ERK1/2 phosphorylation in 3T3-L1 adipocytes.
  • This phosphorylation was insensitive to pertussis toxin, suggesting a pertussis toxin-insensitive G protein.
  • Cholera toxin mimicked and, upon prolonged treatment, diminished the agonist-induced ERK1/2 phosphorylation, indicating a G(s) protein-dependent pathway.
  • Lisophosphatidic acid-induced ERK1/2 phosphorylation was sensitive to pertussis toxin and unaffected by cholera toxin.

Conclusions:

  • Beta(3)-adrenoceptor agonists activate ERK1/2 phosphorylation in 3T3-L1 adipocytes via a G(s) protein-dependent signaling cascade.
  • This pathway is distinct from the signaling activated by lisophosphatidic acid.
  • The findings elucidate a novel mechanism of beta(3)-adrenoceptor signaling in adipocytes.