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          Institute: MPI für Biochemie     Collection: Molecular Medicine (R. Fässler)     Display Documents

ID: 35071.0, MPI für Biochemie / Molecular Medicine (R. Fässler)
Short arm region of laminin-5 gamma 2 chain: Structure, mechanism of processing and binding to heparin and proteins
Authors:Sasaki, T.; Göhring, W.; Mann, K.; Brakebusch, C.; Yamada, Y.; Fässler, R.; Timpl, R.
Date of Publication (YYYY-MM-DD):2001-12-07
Title of Journal:Journal of Molecular Biology
Journal Abbrev.:J. Mol. Biol.
Issue / Number:4
Start Page:751
End Page:763
Review Status:Peer-review
Audience:Not Specified
Abstract / Description: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.
Free Keywords:basement membranes; disulfide isomerase; laminin-5; ligand binding; recombinant protein
Comment of the Author/Creator:Date: 2001, DEC 7
External Publication Status:published
Document Type:Article
Communicated by:N.N.
Affiliations:MPI für Biochemie/Molecular Medicine (R. Fässler)/Extracellular Matrix Proteins (T. Sasaki)
MPI für Biochemie/Independent Junior Research Groups/Regulation of Cytoskeletal Organisation (C. Brakebusch, Department of Molecular Medicine, Heisenberg)
MPI für Biochemie/Emeriti Groups/Protein Chemistry (R. Timpl)
External Affiliations:Lund Univ, Dept Expt Pathol, S-22185 Lund, Sweden; NIDCR, NIH, Bethesda, MD USA
Identifiers:ISI:000173469400010 [ID No:1]
ISSN:0022-2836 [ID No:2]
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