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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 globular domain of the laminin alpha1 chain binds to alpha1beta1 and alpha2beta1 integrins and to the heparan sulfate-containing domains of perlecan.
- Source :
-
FEBS letters [FEBS Lett] 1998 Jul 03; Vol. 430 (3), pp. 217-21. - Publication Year :
- 1998
-
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.
- Subjects :
- Animals
Cell Line
Heparitin Sulfate chemistry
Humans
Integrin alpha1beta1
Laminin genetics
Laminin ultrastructure
Mice
Microscopy, Electron
Peptide Fragments metabolism
Protein Binding
Protein Folding
Proteoglycans chemistry
Receptors, Collagen
Recombinant Fusion Proteins
Heparan Sulfate Proteoglycans
Heparitin Sulfate metabolism
Integrins metabolism
Laminin chemistry
Laminin metabolism
Proteoglycans metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0014-5793
- Volume :
- 430
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 9688542
- Full Text :
- https://doi.org/10.1016/s0014-5793(98)00601-2