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Related Experiment Videos

Cell surface receptors for extracellular matrix molecules.

C A Buck1, A F Horwitz

  • 1Wistar Institute, Philadelphia, Pennsylvania 19104.

Annual Review of Cell Biology
|January 1, 1987
PubMed
Summary
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Cellular receptors like integrins bind extracellular matrix components with varying affinities. This differential binding influences cell adhesion, motility, and tissue development, with implications for morphogenesis.

Area of Science:

  • Cell Biology
  • Biochemistry
  • Developmental Biology

Background:

  • Extracellular matrix (ECM) receptors mediate cell adhesion and signaling.
  • Integrins and other receptors exhibit a wide range of binding affinities for ECM ligands.
  • These affinities are crucial for diverse cellular functions.

Purpose of the Study:

  • To explore the functional significance of varying binding affinities of ECM receptors.
  • To investigate the specificity and regulation of cell-ECM interactions.
  • To understand the role of receptor multiplicity in cell adhesion and morphogenesis.

Main Methods:

  • Analysis of binding affinities (dissociation constants) of various ECM receptors.
  • Examination of receptor specificity for ECM ligands, including RGD sequences.

Related Experiment Videos

  • Comparison of avian and mammalian integrin characteristics.
  • Consideration of receptor co-expression and subunit combinations.

    • Main Results:

    • Integrin affinity for fibronectin is moderate, enabling rapid complex dynamics important for cell motility.
    • High-affinity laminin receptors stabilize tissues.
    • Avian integrins show promiscuous binding, while mammalian receptors are more specific.
    • Multiple receptors and subunit combinations contribute to cell-specific adhesion.

    Conclusions:

    • Differential binding affinities of ECM receptors are critical for cell behavior and tissue organization.
    • Receptor specificity and multiplicity play key roles in cell adhesion and developmental processes like morphogenesis.
    • Regulation of integrin-ligand interactions occurs at multiple levels, including distribution and post-translational modification.