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 Experiment Videos

Cell type-specific integrin variants with alternative alpha chain cytoplasmic domains.

R N Tamura1, H M Cooper, G Collo

  • 1Scripps Research Institute, La Jolla, CA 92037.

Proceedings of the National Academy of Sciences of the United States of America
|November 15, 1991
PubMed
Summary

Integrin alpha 6 and alpha 3 subunits have distinct structural variants (A and B) with different cytoplasmic domains. Their cell-type-specific expression influences cellular responses to basement membrane ligands.

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

Low risk management intervention: Limited impact of remedial tillage on net ecosystem carbon balance at a commercial Miscanthus plantation.

Global change biology. Bioenergy·2024
Same author

Purinoceptors in the Central Nervous System.

Drug development research·2024
Same author

CXCR2 expression during melanoma tumorigenesis controls transcriptional programs that facilitate tumor growth.

Molecular cancer·2023
Same author

CXCR2 expression during melanoma tumorigenesis controls transcriptional programs that facilitate tumor growth.

bioRxiv : the preprint server for biology·2023
Same author

Overriding water table control on managed peatland greenhouse gas emissions.

Nature·2021
Same author

Olfactory dysfunction in patients with chronic rhinosinusitis with nasal polyps is associated with clinical-cytological grading severity.

Acta otorhinolaryngologica Italica : organo ufficiale della Societa italiana di otorinolaringologia e chirurgia cervico-facciale·2019

Area of Science:

  • Cellular and Molecular Biology
  • Integrin Biology
  • Extracellular Matrix Interactions

Background:

  • Integrin heterodimers, specifically alpha 6 beta 1 and alpha 6 beta 4, function as receptors for laminin and basement membrane components.
  • The alpha 3 beta 1 integrin interacts with various extracellular matrix proteins, including laminin, collagen, fibronectin, and epiligrin.
  • Integrin function is modulated by distinct subunit isoforms and their associated cytoplasmic domains.

Purpose of the Study:

  • To identify and characterize structural variants (isoforms A and B) of the alpha 6 and alpha 3 integrin subunits.
  • To investigate the cell-type-dependent expression patterns of these alpha 6 and alpha 3 integrin isoforms.
  • To explore the potential functional implications of alternative cytoplasmic domains in integrin-mediated cellular responses.

Related Experiment Videos

Main Methods:

  • Identification of structural variants through mRNA amplification techniques.
  • Antibody immunoprecipitation was used to confirm the expression of alpha 6A and alpha 6B isoforms.
  • Analysis of tissue and cell line expression patterns for alpha 3A and alpha 3B mRNA.

Main Results:

  • Structural variants (A and B) of alpha 6 and alpha 3 integrin subunits, differing in cytoplasmic domains, were identified.
  • Expression of alpha 6A and alpha 6B isoforms is cell-type specific; transformed cell lines express both, embryonic fibroblasts express alpha 6A, and embryonic stem cells express alpha 6B.
  • Differential expression of alpha 3A and alpha 3B mRNA was observed across various tissues and cell lines, with alpha 3B predominantly found in heart and brain.

Conclusions:

  • Alternative splicing generates distinct cytoplasmic domains in alpha 6 and alpha 3 integrin subunits, leading to isoform diversity.
  • Cell-type-specific expression of these integrin isoforms suggests a regulatory mechanism for cellular adhesion and signaling.
  • The distinct cytoplasmic domains likely mediate differential cellular responses to extracellular matrix ligands, adapting cell behavior to specific tissue environments.