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Laminin binding proteins

A M Mercurio1, L M Shaw

  • 1Laboratory of Cancer Biology, Deaconess Hospital, Harvard Medical School, Boston, MA 02115.

Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology
|September 1, 1991
PubMed

Insights

Cells interact with laminin via integrins and lectins. Integrins signal laminin presence, while lectins may enhance this function by binding laminin carbohydrates, but cytosolic protein roles require caution.

Area of Science:

  • Cell biology
  • Biochemistry
  • Molecular biology

Background:

  • Basement membranes are crucial extracellular matrices, with laminin as a primary adhesive component.
  • Cellular interactions with laminin are mediated by specific binding proteins.

Purpose of the Study:

  • To elucidate the roles of different laminin-binding proteins in cellular signaling.
  • To differentiate the functions of cell surface receptors versus intracellular proteins in laminin interaction.

Main Methods:

  • Analysis of protein-cell surface interactions.
  • Investigation of signaling pathways initiated by laminin binding.
  • Characterization of carbohydrate-protein interactions.

Main Results:

  • Integrins act as transmembrane receptors, relaying laminin presence from the cell surface to the cytoplasm.
  • Lectins represent another class of laminin-binding proteins that may modulate integrin function through carbohydrate interactions.
  • The functions of cytosolic laminin-binding proteins are less understood and require careful investigation.

Conclusions:

  • Integrins and lectins play distinct but potentially cooperative roles in cellular responses to laminin.
  • Further research is needed to clarify the specific functions of various laminin-binding proteins, particularly those located in the cytosol.

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