The N-terminal globular domain of the laminin alpha1 chain binds to alpha1beta1 and alpha2beta1 integrins and to the heparan sulfate-containing domains of perlecan.

The N-terminal domains VI plus V (62 kDa) and V alone (43 kDa) of the laminin alpha1 chain were obtained as recombinant products and shown to be folded into a native form by electron microscopy and immunological assays. Domain VI alone, which corresponds to an LN module, did not represent ...
an autonomously folding unit in mammalian cells, however. Fragment alpha1VI/V, but not fragment alpha1V, bound to purified alpha1beta1 and alpha2beta1 integrins, to heparin, and to heparan sulfate-substituted domains I and V of perlecan. This localized the binding activities to the LN module, which contains two basic sequences suitable for heparin interactions.
Mesh Terms:
Animals, Cell Line, Heparan Sulfate Proteoglycans, Heparitin Sulfate, Humans, Integrin alpha1beta1, Integrins, Laminin, Mice, Microscopy, Electron, Peptide Fragments, Protein Binding, Protein Folding, Proteoglycans, Receptors, Collagen, Recombinant Fusion Proteins
FEBS Lett.
Date: Jul. 03, 1998
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