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Related Experiment Videos

LBL, a novel, developmentally regulated, laminin-binding lectin.

Z Z Bao1, J Muschler, A F Horwitz

  • 1Department of Cell and Structural Biology, University of Illinois, Urbana 61801.

The Journal of Biological Chemistry
|March 5, 1992
PubMed
Summary
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Researchers discovered a novel extracellular matrix molecule, termed laminin-binding lectin (LBL), which functions as a galactoside-binding lectin. This protein binds to laminin and is expressed late in avian development.

Area of Science:

  • Extracellular Matrix Biology
  • Developmental Biology
  • Molecular Biology

Background:

  • Integrin preparations often contain associated protein complexes.
  • Novel extracellular matrix molecules play crucial roles in tissue structure and development.
  • Understanding protein interactions within the extracellular matrix is key to deciphering cellular processes.

Purpose of the Study:

  • To purify and characterize a novel 190/220-kDa complex found in integrin preparations.
  • To determine the molecular identity, function, and localization of this novel protein.
  • To investigate its binding properties and developmental expression pattern.

Main Methods:

  • Immunoaffinity purification using monoclonal antibodies.
  • Subunit composition analysis and N-terminal amino acid sequencing.

Related Experiment Videos

  • Hemagglutination assays for lectin activity and carbohydrate-binding specificity.
  • Binding assays with extracellular matrix proteins like laminin, fibronectin, and collagen IV.

    • Main Results:

    • A novel extracellular matrix molecule, a trimer of 70-kDa subunits, was purified.
    • The protein exhibits galactoside-binding lectin activity and binds specifically to laminin.
    • It is widely distributed in basement membranes and connective tissues, with late developmental expression in avian embryos.
    • The protein, named laminin-binding lectin (LBL), is conserved and often copurifies with laminin.

    Conclusions:

    • Laminin-binding lectin (LBL) is a novel extracellular matrix molecule with unique lectin and laminin-binding properties.
    • Its late expression suggests a specific role in later stages of avian development.
    • LBL's conservation and association with laminin highlight its significance in extracellular matrix composition and function.