Epiligrin, a new cell adhesion ligand for integrin alpha 3 beta 1 in epithelial basement membranes

Cell. 1991 May 17;65(4):599-610. doi: 10.1016/0092-8674(91)90092-d.


Epiligrin is a new glycoprotein in most epithelial basement membranes (BMs) and is a ligand for cell adhesion via integrin alpha 3 beta 1. In the extracellular matrix of human foreskin keratinocytes (HFKs), epiligrin contains three disulfide-bonded, glycoprotein subunits, E170, E145, and E135, based on molecular size in kilodaltons. Epiligrin, immunopurified with MAb P1E1, induced cell adhesion and localization of integrin alpha 3 beta 1 in focal adhesions (FAs). Cell adhesion to epiligrin was inhibited with an anti-alpha 3 beta 1 MAb. Epiligrin also colocalized with integrin alpha 6 beta 4 in hemidesmosome-like stable anchoring contacts (SACs). alpha 3 beta 1-FAs encircled alpha 6 beta 4-SACs in a complex adhesion structure. alpha 3 beta 1 and epiligrin localized in BM junctions of epithelial cells primarily in organs of endodermal/ectodermal origin. In epidermis, epiligrin was detected in the lamina lucida of BMs. alpha 3 beta 1 localized in plasma membranes of basal cells in contact with epiligrin and also in lateral/apical membranes. Epiligrin is the ligand of an adhesion super complex composed of alpha 3 beta 1-FAs and alpha 6 beta 4-SACs (hemidesmosomes).

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Antibodies, Monoclonal
  • Basement Membrane / physiology
  • Basement Membrane / ultrastructure
  • Cell Adhesion*
  • Cell Line
  • Cells, Cultured
  • Epithelium / physiology
  • Epithelium / ultrastructure
  • Extracellular Matrix / physiology
  • Extracellular Matrix / ultrastructure
  • Humans
  • Infant, Newborn
  • Integrins / physiology*
  • Intercellular Junctions / physiology
  • Keratinocytes / cytology
  • Keratinocytes / physiology*
  • Keratinocytes / ultrastructure
  • Ligands
  • Macromolecular Substances
  • Male
  • Membrane Glycoproteins / isolation & purification
  • Membrane Glycoproteins / physiology*
  • Microscopy, Electron


  • Antibodies, Monoclonal
  • Integrins
  • Ligands
  • Macromolecular Substances
  • Membrane Glycoproteins