Laminins in basement membrane assembly

Cell Adh Migr. Jan-Feb 2013;7(1):56-63. doi: 10.4161/cam.21831. Epub 2012 Oct 17.


The heterotrimeric laminins are a defining component of all basement membranes and self-assemble into a cell-associated network. The three short arms of the cross-shaped laminin molecule form the network nodes, with a strict requirement for one α, one β and one γ arm. The globular domain at the end of the long arm binds to cellular receptors, including integrins, α-dystroglycan, heparan sulfates and sulfated glycolipids. Collateral anchorage of the laminin network is provided by the proteoglycans perlecan and agrin. A second network is then formed by type IV collagen, which interacts with the laminin network through the heparan sulfate chains of perlecan and agrin and additional linkage by nidogen. This maturation of basement membranes becomes essential at later stages of embryo development.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Agrin / metabolism
  • Animals
  • Basement Membrane / cytology
  • Basement Membrane / metabolism*
  • Collagen Type IV / genetics
  • Collagen Type IV / metabolism
  • Cytoskeleton / metabolism*
  • Dystroglycans / metabolism
  • Extracellular Matrix / metabolism*
  • Heparan Sulfate Proteoglycans / metabolism
  • Humans
  • Integrin alpha Chains / metabolism
  • Laminin / genetics
  • Laminin / metabolism*
  • Polymerization
  • Protein Binding
  • Protein Interaction Mapping
  • Protein Structure, Tertiary


  • Agrin
  • Collagen Type IV
  • Heparan Sulfate Proteoglycans
  • Integrin alpha Chains
  • Laminin
  • perlecan
  • Dystroglycans