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  Short arm region of laminin-5 gamma 2 chain: Structure, mechanism of processing and binding to heparin and proteins

Sasaki, T., Göhring, W., Mann, K., Brakebusch, C., Yamada, Y., Fässler, R., et al. (2001). Short arm region of laminin-5 gamma 2 chain: Structure, mechanism of processing and binding to heparin and proteins. Journal of Molecular Biology, 314(4), 751-763.

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Genre: Journal Article
Alternative Title : J. Mol. Biol.

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 Creators:
Sasaki, T.1, Author              
Göhring, W.2, Author
Mann, K.3, 4, Author              
Brakebusch, C.1, Author              
Yamada, Y., Author
Fässler, R.5, Author              
Timpl, R.1, Author              
Affiliations:
1Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565145              
2External Organizations, ou_persistent22              
3Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              
4Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              
5Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565147              

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Free keywords: basement membranes; disulfide isomerase; laminin-5; ligand binding; recombinant protein
 Abstract: Laminin-5 is a typical component of several epithelial tissues and contains a unique gamma2 chain which can be proteolytically processed by BMP-1. This occurs in the N-terminal half of the gamma2 chain (606 residues), which consists of two rod-like tandem arrays of LE modules, LE1-3 and LE4-6, that flank a globular L4m module containing the cleavage site. Recombinant analysis of L4m, which includes an additional imperfect LE module essential for proper folding, demonstrated an unusual pattern of disulfide bonding. These connectivities prevented the release of gamma2LE1-3L4 m after BMP-1 cleavage which required in addition disulfide reshuffling by isomerases. The liberated segment bound through its L4 m module to heparin, nidogen-1, fibulin-1 and fibulin-2. A further heparin/sulfatide-binding site could be attributed to some arginine residues in module LE1. The gamma2LE4-6 segment remaining in processed laminin-5 showed only a strong binding to fibulin-2. Immunological studies showed a similar partial processing in cell culture and tissues and the persistence of the released fragment in tissues. This indicated that both N- terminal regions of the gamma2 chain may have a function in vivo. (C) 2001 Academic Press.

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Language(s): eng - English
 Dates: 2001-12-07
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 35071
ISI: 000173469400010
 Degree: -

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Title: Journal of Molecular Biology
  Alternative Title : J. Mol. Biol.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 314 (4) Sequence Number: - Start / End Page: 751 - 763 Identifier: ISSN: 0022-2836