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

You might also read

Related Articles

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

Sort by
Same author

A self-attention-based deep learning model for identifying key genes in insect pupal metamorphosis.

BMC genomics·2026
Same author

Plasmonic Re-Excitation Enables Superoxide-Mediated Ethane Conversion to Acetic Acid under Visible Light.

Journal of the American Chemical Society·2026
Same author

One-Step Chemoenzymatic Labeling and Oxime-Reversible Enrichment for O-GlcNAcylation Profiling under Oxidative Stress.

Analytical chemistry·2026
Same author

AutoPELSA: An Automated Sample Preparation System for Proteome-Wide Identification of Target Proteins of Diverse Ligands.

Analytical chemistry·2026
Same author

High-Throughput Virtual Screening of Small Molecule Quenchers for Near-Infrared Fluorophores.

Angewandte Chemie (International ed. in English)·2026
Same author

A practical CO<sub>2</sub>-mediated synthesis of 5,6-carboxylated silicon-rhodamines for targeted probe development.

Beilstein journal of organic chemistry·2026

Related Experiment Video

Updated: Nov 15, 2025

Determining Cell-surface Expression and Endocytic Rate of Proteins in Primary Astrocyte Cultures Using Biotinylation
10:42

Determining Cell-surface Expression and Endocytic Rate of Proteins in Primary Astrocyte Cultures Using Biotinylation

Published on: July 3, 2017

9.8K

Rapid Enzyme-Mediated Biotinylation for Cell Surface Proteome Profiling.

Yanan Li1, Yan Wang1,2, Yating Yao1

  • 1CAS Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences (CAS), Dalian 116023, China.

Analytical Chemistry
|March 4, 2021
PubMed
Summary

This study introduces a rapid cell surface labeling method for identifying surface proteins within seconds. The technique effectively tracks dynamic surfaceome changes, offering insights into cellular signaling responses.

More Related Videos

"Cell Surface Capture" Workflow for Label-Free Quantification of the Cell Surface Proteome
06:31

"Cell Surface Capture" Workflow for Label-Free Quantification of the Cell Surface Proteome

Published on: March 24, 2023

2.8K
Measuring Plasma Membrane Protein Endocytic Rates by Reversible Biotinylation
11:32

Measuring Plasma Membrane Protein Endocytic Rates by Reversible Biotinylation

Published on: December 23, 2009

17.3K

Related Experiment Videos

Last Updated: Nov 15, 2025

Determining Cell-surface Expression and Endocytic Rate of Proteins in Primary Astrocyte Cultures Using Biotinylation
10:42

Determining Cell-surface Expression and Endocytic Rate of Proteins in Primary Astrocyte Cultures Using Biotinylation

Published on: July 3, 2017

9.8K
"Cell Surface Capture" Workflow for Label-Free Quantification of the Cell Surface Proteome
06:31

"Cell Surface Capture" Workflow for Label-Free Quantification of the Cell Surface Proteome

Published on: March 24, 2023

2.8K
Measuring Plasma Membrane Protein Endocytic Rates by Reversible Biotinylation
11:32

Measuring Plasma Membrane Protein Endocytic Rates by Reversible Biotinylation

Published on: December 23, 2009

17.3K

Area of Science:

  • Proteomics
  • Cell Biology
  • Biochemistry

Background:

  • The cell surface is crucial for sensing external signals, and understanding its dynamic changes is key to deciphering cellular responses.
  • Identifying transient alterations in the surfaceome upon perturbation can reveal critical signaling molecules driving cellular phenotypes.

Purpose of the Study:

  • To develop and validate a rapid, selective cell surface labeling strategy for proteomic analysis.
  • To apply this method for tracking dynamic surfaceome changes in response to stimuli like insulin.

Main Methods:

  • A novel peroxidase-mediated oxidative tyrosine coupling strategy for cell surface labeling within seconds.
  • Quantitative proteomics to identify and quantify labeled surface proteins from HeLa and HepG2 cells.
  • Time-resolved analysis of surfaceome alterations following insulin stimulation.

Main Results:

  • Identified 2684 proteins, with 51% annotated as cell surface proteins, using a 1-minute labeling time in HeLa cells.
  • Validated the enrichment of cell surface proteins, with 68% of significantly enriched proteins being cell surface-annotated.
  • Detected 32 significantly regulated proteins, including key signaling molecules like INSR and CTNNB1, in HepG2 cells after insulin stimulation at different time points.

Conclusions:

  • The developed method provides a powerful tool for high-time-resolution analysis of surfaceome dynamics.
  • This technique enables the study of transient cell surface protein changes and the elucidation of cellular signaling pathways.
  • The findings highlight the potential for this technology in understanding temporal and spatial regulation of cellular processes.