The N‐terminal globular domain of the laminin α1 chain binds to α1β1 and α2β1 integrins and to the heparan sulfate‐containing domains of perlecan
- 3 July 1998
- journal article
- Published by Wiley in FEBS Letters
- Vol. 430 (3), 217-221
- https://doi.org/10.1016/s0014-5793(98)00601-2
Abstract
The N-terminal domains VI plus V (62 kDa) and V alone (43 kDa) of the laminin α1 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 α1VI/V, but not fragment α1V, bound to purified α1β1 and α2β1 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.Keywords
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