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Related Experiment Videos

Embryonic mesodermal defects in alpha 5 integrin-deficient mice

J T Yang1, H Rayburn, R O Hynes

  • 1Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge 02139.

Development (Cambridge, England)
|December 1, 1993
PubMed
Summary
This summary is machine-generated.

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A mutation in the alpha 5 integrin gene causes embryonic lethality in mice. Despite the absence of alpha 5 beta 1 integrin, mutant cells can still interact with fibronectin, indicating alternative receptor involvement.

Area of Science:

  • Developmental Biology
  • Cell Biology
  • Molecular Genetics

Background:

  • Integrins are crucial cell surface receptors involved in cell adhesion, migration, and development.
  • Alpha 5 beta 1 integrin is a known receptor for fibronectin, a key extracellular matrix protein.
  • Previous studies suggested alpha 5 beta 1 integrin is essential for fibronectin-mediated cellular functions.

Purpose of the Study:

  • To investigate the in vivo role of alpha 5 integrin using gene targeting in mice.
  • To determine the necessity of alpha 5 beta 1 integrin for fibronectin matrix assembly, focal contact formation, and cell migration.

Main Methods:

  • Gene targeting in embryonic stem cells to create alpha 5 integrin-null mice.
  • Analysis of embryonic development and defects in mutant embryos.

Related Experiment Videos

  • In vitro studies using cells derived from alpha 5-null embryos to assess fibronectin interactions.

    • Main Results:

    • Loss of function mutation in the murine alpha 5 integrin gene results in recessive embryonic lethality around days 10-11 of gestation.
    • Alpha 5-null embryos exhibit significant defects in posterior trunk and yolk sac mesodermal structures.
    • Mutant cells lacking alpha 5 beta 1 integrin can still assemble fibronectin matrix, form focal contacts, and migrate on fibronectin.

    Conclusions:

    • Alpha 5 beta 1 integrin is essential for normal embryonic development, particularly mesoderm formation and integrity.
    • Fibronectin-mediated cellular functions, previously thought to require alpha 5 beta 1 integrin, can be accomplished by alternative fibronectin receptors.
    • This study reveals functional redundancy among fibronectin receptors in vitro, despite the critical in vivo role of alpha 5 integrin.