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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: Zeitschriftenartikel
Alternativer Titel : J. Mol. Biol.

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 Urheber:
Sasaki, T.1, Autor           
Göhring, W.2, Autor
Mann, K.3, 4, Autor           
Brakebusch, C.1, Autor           
Yamada, Y., Autor
Fässler, R.5, Autor           
Timpl, R.1, Autor           
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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Schlagwörter: basement membranes; disulfide isomerase; laminin-5; ligand binding; recombinant protein
 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 2001-12-07
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 35071
ISI: 000173469400010
 Art des Abschluß: -

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Titel: Journal of Molecular Biology
  Alternativer Titel : J. Mol. Biol.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 314 (4) Artikelnummer: - Start- / Endseite: 751 - 763 Identifikator: ISSN: 0022-2836