Syndecan-1 interaction with the LG4/5 domain in laminin-332 is essential for keratinocyte migration
In: Journal of Cellular Physiology, Jg. 214 (2007), S. 238-249
Online
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Zugriff:
Laminin 5/laminin 332 (LN332) is an adhesion substrate for epithelial cells. After secretion of LN332, a regulated cleavage occurs at the carboxy-terminus of its alpha3 subunit, which releases a tandem of two globular modules named LG4/5. We show that the presence of the LG4/5 domain in precursor LN332 decreases its integrin-mediated cell adhesion properties in comparison with mature LN332. Whereas cell adhesion to the recombinant LG4/5 fragment relies solely on the heparan sulfate proteoglycan (HSPG) receptor syndecan-1, we reveal that both syndecan-1 and the alpha3beta1 integrin bind to precursor LN332. We further demonstrate that syndecan-1 mediated cell adhesion to the LG4/5 fragment and pre-LN332 allows the formation of fascin-containing protrusions, depending on the GTPases Rac and Cdc42 activation. Reducing syndecan-1 expression in normal keratinocytes prevents cell protrusions on pre-LN332 with subsequent failure of the peripheral localization of the alpha3beta1 integrin. We finally show that cell migration on pre-LN332 requires syndecan-1. Therefore, the LG4/5 domain in precursor LN332 appears to trigger intracellular signaling events, which participate in keratinocyte motility.
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Syndecan-1 interaction with the LG4/5 domain in laminin-332 is essential for keratinocyte migration
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Autor/in / Beteiligte Person: | Letourneur, François ; Bachy, Sophie ; Rousselle, Patricia |
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Zeitschrift: | Journal of Cellular Physiology, Jg. 214 (2007), S. 238-249 |
Veröffentlichung: | Wiley, 2007 |
Medientyp: | unknown |
ISSN: | 1097-4652 (print) ; 0021-9541 (print) |
DOI: | 10.1002/jcp.21184 |
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