Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Cell Line
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Heparan Sulfate Proteoglycans*
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Heparitin Sulfate / chemistry
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Heparitin Sulfate / metabolism*
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Humans
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Integrin alpha1beta1
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Integrins / metabolism*
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Laminin / chemistry*
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Laminin / genetics
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Laminin / metabolism*
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Laminin / ultrastructure
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Mice
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Microscopy, Electron
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Peptide Fragments / metabolism
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Protein Binding
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Protein Folding
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Proteoglycans / chemistry
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Proteoglycans / metabolism*
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Receptors, Collagen
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Recombinant Fusion Proteins
Substances
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Heparan Sulfate Proteoglycans
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Integrin alpha1beta1
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Integrins
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Laminin
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Peptide Fragments
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Proteoglycans
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Receptors, Collagen
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Recombinant Fusion Proteins
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perlecan
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laminin A
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Heparitin Sulfate