Interaction of Laminin with Cell Membranes

  • G. Risse
  • J. Dieckhoff
  • H. G. Mannherz
  • K. von der Mark
Part of the NATO ASI Series book series (NSSA, volume 133)


Laminin, a major component of basement membranes, is a large (Mr =106) glycoprotein with diverse biological functions. By binding to various matrix components including type IV collagen, heparan sulfate proteoglycan and nidogen it plays a key role in the organization of the basal lamina. Furthermore laminin is involved in a variety of interactions of the basement membrane with the adjacent epithelial and mesenchymal cells. In studies on isolated cells and organoids in vitro laminin has been shown to promote cell migration and adhesion, to effect cell shape and polarity, to induce outgrowth of cell processes and neurites and to stimulate proliferation and differentiation (for recent review see 1). Laminin seems to influence predominantly epithelial cell behaviour, but also effects on mesenchymal cells have been described, for example on muscle cell differentiation. We could show that laminin if present as substrate on culture dishes selects for2 myogenic versus fibroblastic cells and stimulates myodifferentiation. These observations initiated the search for laminin-binding components on the muscle cell surface. Affinity chromatography of detergent solubilised muscle cell membranes resulted in the isolation of a 68kd protein, which upon reconstitution into liposomes binds specifically to laminin3.


Skeletal Myoblast Laminin Receptor Muscle Cell Membrane Chicken Gizzard Smooth Muscle Cell Membrane 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.



Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. (1).
    K. v.d. Mark and U. Kühl, Laminin and its receptor, Biochim. biophys. Acta 823:147 (1985).PubMedGoogle Scholar
  2. (2).
    U. Kühl, M. öcalan, R. Timpl and K. v.d. Mark, Role of laminin and fibronectin in selecting myogenic versus fibrogenic cells from skeletal muscle cells in vitro, Develop. Biol., in the press.Google Scholar
  3. (3).
    H. Lesot, U. Kühl and K. v.d. Mark, Isolation of a laminin-binding protein from muscle cell membranes, Eur. Mol. Biol. Organ. J. 2:861 (1983).Google Scholar
  4. (4).
    J. Dieckhoff, J. Mollenhauer, U. Kühl, B. Niggenmeyer, K. v.d. Mark and H.G. Mannherz, The extracellular matrix proteins laminin and fibronectin modify the AMPase activity of 5’nucleotidase from chicken gizzard smooth muscle, FEBS Lett. 195:824 (1986).CrossRefGoogle Scholar
  5. (5).
    V.P. Terranova, C.N. Rao, T. Kalebic, I.M. Margulies and L.A. Liotta, Laminin receptor on breast carcinoma cells, Proc. Natl. Acad. Sci. USA 80:444 (1983).PubMedCrossRefGoogle Scholar
  6. (6).
    G. A. Cates and P. C. Holland, Biosynthesis of plasma-membrane proteins during myogenesis of skeletal muscle in vitro, Biochem. J. 174:873 (1978).PubMedGoogle Scholar
  7. (7).
    P.T. Kelly, K. v.d. Mark and G.W. Conrad, Identification of collagen types I, II, III and V by two-dimensional fingerprints of 125- I-labeled peptides, Analyt. Biochem. 112:105 (1981).PubMedCrossRefGoogle Scholar
  8. (8).
    A. Zachowsky, H.W. Evans and A. Paraf, Immunological evidence that plasma-membrane 5’nucleotidase is a transmembrane protein, Biochim. biophys. Acta 664:121 (1981).Google Scholar
  9. (9).
    G.W. Kreutzberg, M. Reddington and H. Zimmermann, “Cellular Biology of Ectoenzymes”, Springer Verlag, Berlin (1986).CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • G. Risse
    • 1
  • J. Dieckhoff
    • 2
  • H. G. Mannherz
    • 2
  • K. von der Mark
    • 1
  1. 1.Abteilung für BindegewebsforschungMax-Planck-Institut für BiochemieMartinsried/MünchenDeutschland
  2. 2.Institut für Anatomie und ZellbiologieUniversität MarburgDeutschland

Personalised recommendations